Creative Enzymes - Products

Enzyme manufacturing for life science research and medicines, food, alcohol, fabric, paper etc. Uses include: drug discovery, cancer and infectious disease research, microbiology and personalized medicine.

Product	Description	Suppliers Website
Native Rabbit Pyruvate Kinase Quick inquiry Where to buy	Pyruvate kinase is an enzyme involved in glycolysis. It catalyzes the transfer of a phosphate group from phosphoenolpyruvate (PEP) to ADP, yielding one molecule of pyruvate and one molecule of ATP. Pyruvate kinase from rabbit muscle catalyzes an atp-dependent phosphorylation of glycolate to yield 2-phosphoglycolate. Applications: Pyruvate kinase from rabbit muscle has been used in a structural study to understand the reaction mechanism of the final step in glycolysis. it has also been used in a study to investigate atp-dependent phosphorylation of α-substituted carboxylic acids. Group: Enzymes. Synonyms: Pyruvate kinase; EC 2.7.1.40; 9001-59-6; phosphoenolpyruvate kinase...7 kDa and exists as a tetramer of four equal subunits of molecular weight 57 kDa. Activity: 350-600 units/mg protein. Storage: -20°C. Form: Type I, ammonium sulfate suspension, Suspension in 3.2 M (NH4)2SO4 solution, pH 6; Type II, lyophilized powder; Type III, buffered aqueous glycerol solution, Solution in 50% glycerol containing 0.01 M phosphate, pH 7.0. Source: Rabbit muscle. Species: Rabbit. Pyruvate kinase; EC 2.7.1.40; 9001-59-6; phosphoenolpyruvate kinase; phosphoenol transphosphorylase; pyruvate kinase (phosphorylating); fluorokinase; fluorokinase (phosphorylating); pyruvic kinase; pyruvate phosphotransferase; ATP:pyruvate 2-O-phosphotransferase; PK. Cat No: NATE-0567.
Native Rabbit Pyruvate Kinase/Lactic Dehydrogenase enzymes Quick inquiry Where to buy	Lactate dehydrogenase from rabbit muscle can be inhibited by ascorbate. Aldolase and actin were shown to block this inhibitory effect. Pyruvate kinase requires bivalent and monovalent cations such as Mg2+ and K+ respectively for activation to occur. Pyruvate kinase from rabbit muscle catalyzes an atp-dependent phosphorylation of glycolate to yield 2-phosphoglycolate. buffered aqueous glycerol solution, 900-1400 units/ml lactic dehydrogenase, 600-1 kda units/ml pyruvate kinase. Applications: Pyruvate kinase from rabbit muscle has been used in a study to assess nuclear magnetic relaxation studies of the conformation of adenosine 5?-triphosphate. it has also been used in a study to investigate heterogeneity of presumably homogeneous protein preparations. Group: Enzymes. Synonyms: Pyruvate Kinase/Lactic Dehydrogenase enzymes; PK/LDH enzymes. PK/LDH enzymes. Activity: 900-1400 units/mL lactic dehydrogenase; 600-1,000 units/mL pyruvate kinase. Stability: -20°C. Form: buffered aqueous glycerol solution. Source: rabbit muscle. Species: Rabbit. Pyruvate Kinase/Lactic Dehydrogenase enzymes; PK/LDH enzymes. Cat No: NATE-0568.
Native Rabbit S-(5'-Adenosyl)-L-homocysteine Hydrolase Quick inquiry Where to buy	Enzyme in vertebrates which catabolizes S-adenosyl-L-homocysteine. Group: Enzymes. Synonyms: Adenosylhomocysteinase; EC 3.3.1.1; S-adenosylhomocysteine synthase; S-adenosylhomocysteine hydrolase; adenosylhomocysteine hydrolase (ambiguous); S-adenosylhomocysteinase; SAHase; AdoHcyase; 9025-54-1. Enzyme Commission Number: EC 3.3.1.1. CAS No. 9025-54-1. AHCY. Activity: > 10 units/mg protein (Lowry). Storage: -70°C. Form: buffered aqueous glycerol solution; Solution in 25 mM Tris, pH 7.4, containing 1 mM dithiothreitol, 1 mM EDTA, and 20% glycerol. Source: Rabbit erythrocytes. Species: Rabbit. Adenosylhomocysteinase; EC 3.3.1.1; S-adenosylhomocysteine synthase; S-adenosylhomocysteine hydrolase; adenosylhomocysteine hydrolase (ambiguous); S-adenosylhomocysteinase; SAHase; AdoHcyase; 9025-54-1. Cat No: NATE-0662.
Native Rabbit Thrombin Quick inquiry Where to buy	Thrombin is a serine protease that in humans is encoded by the F2 gene. Prothrombin (coagulation factor II) is proteolytically cleaved to form thrombin in the coagulation cascade, which ultimately results in the reduction of blood loss. Thrombin in turn acts as a serine protease that converts soluble fibrinogen into insoluble strands of fibrin, as well as catalyzing many other coagulation-related reactions. The nih assay procedure uses 0.2 ml diluted plasma (1:1 with saline) as a substrate and 0.1 ml of thrombin sample (stabilized in a 1% buffered albumin solution) based on a modification of the method of biggs. only clotting times in the range of 15-25 seconds are used for determining thrombin concentrations. activity is expressed in nih units obtained by direct comparison to a nih thrombin reference standard. Group: Enzymes. Synonyms: thrombin; 9002-04-4; EC 3.4.21. Enzyme Commission Number: EC 3.4.21.5. CAS No. 9002-4-4. Thrombin. Activity: 600-2,000 NIH units/mg protein (biuret) or > 2,000 NIH units/mg protein (E1%/280 = 19.5); > 125 NIH units/mg protein (biuret). Source: Rabbit plasma. Species: Rabbit. thrombin; 9002-04-4; EC 3.4.21.5; fibrinogenase; thrombase; thrombofort; topical; thrombin-C; tropostasin; activated blood-coagulation factor II; blood-coagulation factor IIa; factor IIa; E thrombin; β-thrombin; γ-thrombin. Cat No: NATE-0700.
Native Rabbit Triosephosphate Isomerase Quick inquiry Where to buy	Triose-phosphate isomerase (TPI or TIM) is an enzyme (EC 5.3.1.1) that catalyzes the reversible interconversion of the triose phosphate isomers dihydroxyacetone phosphate and D-glyceraldehyde 3-phosphate. TPI plays an important role in glycolysis and is essential for efficient energy production. TPI has been found in nearly every organism searched for the enzyme, including animals such as mammals and insects as well as in fungi, plants, and bacteria. However, some bacteria that do not perform glycolysis, like ureaplasmas, lack TPI. Applications: Triosephosphate isomerase has been used in a study to assess molecular characterizations of cryptosporidium, giardia, and enter ...e phosphate mutase; D-glyceraldehyde-3-phosphate ketol-isomerase; TPI; TIM; EC 5.3.1.1; 9023-78-3. Enzyme Commission Number: EC 5.3.1.1. CAS No. 9023-78-3. TPI. Activity: Type I, > 4,000 units/mg protein; Type II, > 3,500 units/mg protein. Storage: -20°C. Form: Type I, ammonium sulfate suspension; Crystalline suspension in 3.2 M (NH4)2SO4 solution, pH 6.0; Type II, lyophilized powder, Sulfate-free, contains EDTA and borate buffer salts. Source: Rabbit muscle. Species: Rabbit. Triose-phosphate isomerase; phosphotriose isomerase; triose phosphoisomerase; triose phosphate mutase; D-glyceraldehyde-3-phosphate ketol-isomerase; TPI; TIM; EC 5.3.1.1; 9023-78-3. Cat No: NATE-0712.
Native Rat Angiotensin Converting Enzyme Quick inquiry Where to buy	Angiotensin-converting enzyme (EC 3.4.15.1), or "ACE" indirectly increases blood pressure by causing blood vessels to constrict. It does that by converting angiotensin I to angiotensin II, which constricts the vessels. For this reason, drugs known as ACE inhibitors are used to lower blood pressure. ACE, angiotensin I and angiotensin II are part of the renin-angiotensin system (RAS), which controls blood pressure by regulating the volume of fluids in the body. ACE is secreted in the lungs and kidneys by cells in the endothelium (inner layer) of blood vessels. Applications: Positive control. Group: Enzymes. Synonyms: ACE; Angiotensin Converting Enzyme; EC 3.4.15.1; dipeptid....1 M phosphate buffer and 300 mM NaCl at pH 8.3 at 37°C. Storage: Maintain at -20°C in undiluted aliquots for up to 6 months. Avoid repeated freeze/thaw cycles. Form: Liquid in 100 mM phosphate buffered saline, 150 mM NaCl, pH 7.4 with 0.2mM CHAPS. Source: Rat lung. Species: Rat. ACE; Angiotensin Converting Enzyme; EC 3.4.15.1; dipeptidyl carboxypeptidase I; peptidase P; dipeptide hydrolase, peptidyl dipeptidase; angiotensin converting enzyme; kininase II; angiotensin I-converting enzyme; carboxycathepsin; dipeptidyl carboxypeptidase; "hypertensin converting enzyme" peptidyl dipeptidase I; peptidyl-dipeptide hydrolase; peptidyldipeptide hydrolase; endothelial cell peptidy
Native Rat Arginase Quick inquiry Where to buy	Arginase (EC 3.5.3.1, arginine amidinase, canavanase, L-arginase, arginine transamidinase) is a manganese-containing enzyme. The reaction catalyzed by this enzyme is:arginine + H2O ? ornithine + urea. It is the final enzyme of the urea cycle. It is ubiquitous to all domains of life. Group: Enzymes. Synonyms: Arginase; arginine amidinase; canavanase; L-arginase; arginine transamidinase; EC 3.5.3.1. Enzyme Commission Number: EC 3.5.3.1. CAS No. 9000-96-8. Purity: Purified. Arginase. Activity: > 200 U/mg. Storage: -20°C. Form: Lyophilized. Source: Rat Liver. Species: Rat. Arginase; arginine amidinase; canavanase; L-arginase; arginine transamidinase; EC 3.5.3.1. Cat No: NATE-0086.
Native Rat Calmodulin-dependent Protein Kinase II Quick inquiry Where to buy	Serine-threonine protein kinase:these kinases appear to be involved in neurotransmitter release, control of stimulus-induced gene expression, and in the phosphorylation of microtubule related proteins. Group: Enzymes. Synonyms: Calmodulin-dependent Protein Kinase II; 9026-43-1. CAS No. 9026-43-1. Calmodulin-dependent Protein Kinase II. Activity: 800-1,100 units/mg protein (Lowry). Stability: -70°C. Form: buffered aqueous glycerol solution. Source: Rat brain. Species: Rat. Calmodulin-dependent Protein Kinase II; 9026-43-1. Cat No: NATE-0099.
Native Rat Creatine Kinase MM Quick inquiry Where to buy	Creatine kinase, muscle also known as CKM is a creatine kinase that in humans is encoded by the CKM gene. In the figure to the right, the crystal structure of the muscle-type M-CK monomer is shown. In vivo, two such monomers arrange symmetrically to form the active MM-CK enzyme. In heart, in addition to the MM-CK homodimer, also the heterodimer MB-CK consisting of one muscle (M-CK) and one brain-type (B-CK) subunit is expressed. The latter may be an important serum marker for myocardial infarction, if released from damaged myocardial cells into the blood where it can be detected by clinical chemistry. Applications: Diagnostic controls, calibrators & standards; clinical chemistry; testing/assay validation; life science; manufacturing. Group: Enzymes. Synonyms: CKM; creatine kinase, muscle; CKMM; creatine kinase M-type; creatine kinase-M; creatine kinase M chain; M-CK; MM-CK. Purity: > 90% (SDS-PAGE). CK. Stability: 2 years. Storage: Store at -20°C. Form: Liquid in 50% Glycerol, 10mM Tris.Cl, 20mM NaCl, 0.05% NaN3. Source: Rat Skeletal Muscle. Species: Rat. CKM; creatine kinase, muscle; CKMM; creatine kinase M-type; creatine kinase-M; creatine kinase M chain; M-CK; MM-CK. Cat No: NATE-0960.
Native Rat Glutathione-S-Transferase Quick inquiry Where to buy	Glutathione S-transferases (GSTs), previously known as ligandins, comprise a family of eukaryotic and prokaryotic phase II metabolic isozymes best known for their ability to catalyze the conjugation of the reduced form of glutathione (GSH) to xenobiotic substrates for the purpose of detoxification. The GST family consists of three superfamilies:the cytosolic, mitochondrial, and microsomal--also known as MAPEG--proteins. Members of the GST superfamily are extremely diverse in amino acid sequence, and a large fraction of the sequences deposited in public databases are of unknown function. The Enzyme Function Initiative (EFI) is using GSTs as a model superfamily to identify new GST functions. Group: Enzymes. Synonyms: Glutathione S-transferases; GSTs; GST; Glutathione S-alkenetransferase; Glutathione S-alkyltransferase; Glutathione S-aralkyltransferase; Glutathione S-aryltransferase;. Enzyme Commission Number: EC 2.5.1.18. CAS No. 50812-37-8. Purity: Purified. Glutathione S-Transferase. Activity: > 10 U/mg. Storage: -20°C. Form: Lyophilized. Source: Rat Liver. Species: Rat. Glutathione S-transferases; GSTs; GST; Glutathione S-alkenetransferase; Glutathione S-alkyltransferase; Glutathione S-aralkyltransferase; Glutathione S-aryltransferase; Glutathione S-epoxidetransferase; RX:Glutathione R-transferase; EC 2.5.1.18; 50812-37-8. Cat No: NATE-0327.
Native Rat Histamine N-Methyl Transferase Quick inquiry Where to buy	(HNMT) is the enzyme which catalyzes the n-methylation of histamine as follows: Histamine + S-Adenosyl methionine ------> (SAM)methyladed Histamine. The mechanism involves the transfer of an active methyl group from S-Adenosyl methionine (SAM) to histamine. Histamine is present in most of mammalian tissues and HNMT is the enzyme responsible for inactivation of histamine in mammals. Methylation is major route of histamine metabolism. HNMT has been used to measure histamine by radio-enzymatic method. HNMT has been purified from rat kidney. Molecular weight equals 33,400, pH optimum is 8.00-8.25. We have also purified it from bovine kidney which seems to be very similar to rat kidney. Group: Enzymes. Synonyms: Histamine N-Methyl Transferase; HNMT; EC 2.1.1.8. Enzyme Commission Number: EC 2.1.1.8. CAS No. 9029-80-5. HNMT. Mole weight: 33.4 kDa. Activity: 50-100 U/mg. Stability: Store at -20°C (-4°F). Form: Freeze-dried powder. Source: Rat Kidney. Species: Rat. Histamine N-Methyl Transferase; HNMT; EC 2.1.1.8. Cat No: NATE-0898.
Native Rat Protein Kinase C Quick inquiry Where to buy	Protein kinase C is a family of protein kinase enzymes that are involved in controlling the function of other proteins through the phosphorylation of hydroxyl groups of serine and threonine amino acid residues on these proteins. PKC enzymes in turn are activated by signals such as increases in the concentration of diacylglycerol (DAG) or calcium ions (Ca2+). Hence PKC enzymes play important roles in several signal transduction cascades. Group: Enzymes. Synonyms: EC 2.7.11.13; 141436-78-4; Protein kinase C; PKC; calcium-dependent protein kinase C; calcium-independent protein kinase C; calcium/phospholipid dependent protein kinase; cPKCα; cPKCβ; cPKCγ; nPKC&de. Enzyme Commission Number: EC 2.7.1.37. CAS No. 141436-78-4. Purity: > 90% (SDS-PAGE). PKC. Mole weight: mol wt 82 kDa by SDS-PAGE. Activity: Type I, 50-200 units/mL. Stability: -70°C. Form: Type I, buffered aqueous glycerol solution; Type II, lyophilized powder. Source: Rat brain. Species: Rat. EC 2.7.11.13; 141436-78-4; Protein kinase C; PKC; calcium-dependent protein kinase C; calcium-independent protein kinase C; calcium/phospholipid dependent protein kinase; cPKCα; cPKCβ; cPKCγ; nPKCδ; nPKCε; nPKCη; nPKCθ; PKCα; PKCβ; PKCγ; PKCδ; PKCε; PKCζ; Pkc1p; protein kinase Cε; STK24. Cat No: NATE-0573.
Native Rat Protein Kinase C Catalytic Subunit Quick inquiry Where to buy	Protein Kinase C (PKC) is a serine/threonine kinase that is activated intracellularly by signal transduction pathways that produce DAG from phosphatidylinositol diphosphate (PIP2) and phosphatidylcholine (PC) through the action of various activated phospholipases. Phorbol esters also stimulate PKC. At least 11 PKC isozymes have been identified that differ in primary structure, tissue distribution, subcellular localization, response to extracellular signals, and substrate specificity. The isozymes can be grouped into three subfamilies. Members of the first family require Ca2+ and phospholipid and include PKCα, βI, βII, and &gamma. Members of the second family are phospholipid-dependent but Ca2+-independent, and include PKCδ, ε, η, and &theta. Members of the third family are not activated by either DAG or phorbol esters and include PKCξ, μ, and &Iota. Does not require ca2+ or phosphatidylserine for its activity. Group: Enzymes. Synonyms: PKC-M, PKM; PKCM; Protein Kinase C Catalytic Subunit. Purity: > 90% (SDS-PAGE). PKC. Activity: > 800 units/mg protein. Stability: -70°C. Source: rat brain. Species: Rat. PKC-M, PKM; PKCM; Protein Kinase C Catalytic Subunit. Pack: vial of 200 ng. Cat No: NATE-0578.
Native Rat Sorbitol Dehydrogenase Quick inquiry Where to buy	Sorbitol dehydrogenase (or SDH) is a cytosolic enzyme. In humans this protein is encoded by the SORD gene. Sorbitol dehydrogenase is an enzyme in carbohydrate metabolism converting sorbitol, the sugar alcohol form of glucose, into fructose. Together with aldose reductase, it provides a way for the body to produce fructose from glucose without using ATP. Sorbitol dehydrogenase uses NAD+ as a cofactor; its reaction is sorbitol + NAD+--> fructose + NADH + H+. A zinc ion is also involved in catalysis. Organs that use it most frequently include the liver and seminal vesicle; it is found in all kinds of organisms from bacteria to humans. A secondary use is the metabolism of dietar...5-oxidoreductase; L-iditol (sorbitol) dehydrogenase; glucitol dehydrogenase; L-iditol:NAD+ oxidoreductase; NAD+-dependent sorbitol dehydrogenase; NAD+-sorbitol dehydrogenase. Enzyme Commission Number: EC 1.1.1.14. CAS No. 9028-21-1. Purity: Purified. SDH. Activity: Reported in U/mg. Storage: -20°C. Form: Lyophilized. Source: Rat Liver. Species: Rat. Sorbitol Dehydrogenase; SDH; EC 1.1.1.14; 9028-21-1; L-iditol 2-dehydrogenase; polyol dehydrogenase; sorbitol dehydrogenase; L-iditol:NAD+ 5-oxidoreductase; L-iditol (sorbitol) dehydrogenase; glucitol dehydrogenase; L-iditol:NAD+ oxidoreductase; NAD+-dependent sorbitol dehydrogenase; NAD+-sorbitol dehydrogenase. Cat No: NATE-0667.
Native Rat Thioredoxin Reductase Quick inquiry Where to buy	Thioredoxin reductase (TrxR) is an NADPH-dependent oxidoreductase containing one FAD per subunit that reduces the active site disulfide in oxidised thioredoxin (Trx). The molecular weight of the isozymes from mammalian sources vary between 55-67 kDa as compared with 35 kDa in prokaryotes, plants or yeast. The substrate specificity of the mammalian enzyme is much broader than the prokaryotic enzyme reducing both mammalian and E. coli thioredoxins as well as well as non-disulfide substrates such selenite, lipoic acids, lipid hydroperoxides and hydrogen peroxide. Applications: Thioredoxin reductase from rat liver can be used for studying the uptake and reduction of a-lipoic acid... NADP-thioredoxin reductase; NADPH-thioredoxin reductase; thioredoxin reductase (NADPH); NADPH2:oxidized thioredoxin oxidoreductase; thioredoxin-disulfide reductase; EC 1.8.1.9; TrxR; 9074-14-0. Enzyme Commission Number: EC 1.8.1.9. CAS No. 9074-14-0. TrxR. Activity: > 100 units/mg protein (Bradford). Storage: -20°C. Form: buffered aqueous glycerol solution; Solution in 50 mM Tris-HCl, pH 7.5, 300 mM NaCl, 1 mM EDTA, and 10% glycerol. Source: Rat liver. Species: Rat. NADP-thioredoxin reductase; NADPH-thioredoxin reductase; thioredoxin reductase (NADPH); NADPH2:oxidized thioredoxin oxidoreductase; thioredoxin-disulfide reductase; EC 1.8.1.9; TrxR; 9074-14-0. Cat No: NATE-0713.
Native Rat Thrombin Quick inquiry Where to buy	Thrombin is a serine protease that in humans is encoded by the F2 gene. Prothrombin (coagulation factor II) is proteolytically cleaved to form thrombin in the coagulation cascade, which ultimately results in the reduction of blood loss. Thrombin in turn acts as a serine protease that converts soluble fibrinogen into insoluble strands of fibrin, as well as catalyzing many other coagulation-related reactions. Thrombin is the final coagulation protease in regard to hemostasis, promoting both procoagulant and anticoagulant effects. Applications: Thrombin is used for site specific cleavage of recombinant fusion proteins containing an accessible thrombin recognition site for removal of affinity tags. thrombin has been used in a study to investigate activation of equine platelet-rich plasma. Group: Enzymes. Synonyms: thrombin; 9002-04-4; EC 3.4.21.5; fibrin. Enzyme Commission Number: EC 3.4.21.5. CAS No. 9002-4-4. Thrombin. Activity: 600-2,000 NIH units/mg protein (biuret) or > 2,000 NIH units/mg protein (E1%/280 = 19.5); > 125 NIH units/mg protein (biuret). Form: lyophilized powder. Source: Rat plasma. Species: Rat. thrombin; 9002-04-4; EC 3.4.21.5; fibrinogenase; thrombase; thrombofort; topical; thrombin-C; tropostasin; activated blood-coagulation factor II; blood-coagulation factor IIa; factor IIa; E thrombin; β-thrombin; γ-thrombin. Cat No: NATE-0701.
Native Rhizopus niveus Lipase Quick inquiry Where to buy	Triacylglycerol lipase is an enzyme with system name triacylglycerol acylhydrolase. This enzyme catalyses the following chemical reaction:triacylglycerol + H2O<-> diacylglycerol + a carboxylate. Group: Enzymes. Synonyms: Triacylglycerol acylhydrolase; Triacylglycerol lipase. Enzyme Commission Number: EC 3.1.1.3. CAS No. 9001-62-1. Lipase. Mole weight: ~83,000. Activity: >1.5 U/mg. Storage: 2-8°C. Form: Powder (fine). Source: Rhizopus niveus. EC 3.1.1.3; lipase; triglyceride lipase; tributyrase; butyrinase; glycerol ester hydrolase; tributyrinase; Tween hydrolase; steapsin; triacetinase; tributyrin esterase; Tweenase; amno N-AP; Takedo 1969-4-9; Meito MY 30; Tweenesterase; GA 56; capalase L; triglyceride hydrolase; triolein hydrolase; tween-hydrolyzing esterase; amano CE; cacordase; triglyceridase; triacylglycerol ester hydrolase; amano P; amano AP; PPL; glycerol-ester hydrolase; GEH; meito Sangyo OF lipase; hepatic lipase; lipazin; post-heparin plasma protamine-resistant lipase; salt-resistant post-heparin lipase; heparin releasable hepatic lipase; amano CES; amano B; tributyrase; triglyceride lipase; liver lipase; hepatic monoacylglycerol acyltransferase; 9001-62-1. Cat No: NATE-1612.
Native Rhizopus oryzae Esterase Quick inquiry Where to buy	An esterase is a hydrolase that splits esters into acids and alcohols. Group: Enzymes. Synonyms: EC 3.1.1.1; ali-esterase; B-esterase; monobutyrase; cocaine esterase; procaine esterase; methylbutyrase; vitamin A esterase; butyryl esterase; carboxyesterase; carboxylate esterase; carboxylic esterase; methylbutyRate esterase; triacetin esterase; carboxyl ester hydrolase; butyRate esterase; methylbutyrase; α-carboxylesterase; propionyl esterase; nonspecific carboxylesterase; esterase D; esterase B; esterase A; serine esterase; carboxylic acid esterase; cocaine esterase; 9016-18-6. Enzyme Commission Number: EC 3.1.1.1. CAS No. 9016-18-6. Esterase. Activity: > 20 U/g. Storage: 2-8°C. Form: powder; light beige. Source: Rhizopus oryzae. EC 3.1.1.1; ali-esterase; B-esterase; monobutyrase; cocaine esterase; procaine esterase; methylbutyrase; vitamin A esterase; butyryl esterase; carboxyesterase; carboxylate esterase; carboxylic esterase; methylbutyRate esterase; triacetin esterase; carboxyl ester hydrolase; butyRate esterase; methylbutyrase; α-carboxylesterase; propionyl esterase; nonspecific carboxylesterase; esterase D; esterase B; esterase A; serine esterase; carboxylic acid esterase; cocaine esterase; 9016-18-6. Pack: Bottomless glass bottle. Contents are inside inserted fused cone. Cat No: NATE-0239.
Native Rhizopus oryzae Lipase Quick inquiry Where to buy	Triacylglycerol lipase is an enzyme with system name triacylglycerol acylhydrolase. This enzyme catalyses the following chemical reaction:triacylglycerol + H2O<-> diacylglycerol + a carboxylate. Applications: Lipases are used industrially for the resolution of chiral compounds and the transesterification production of biodiesel. Group: Enzymes. Synonyms: EC 3.1.1.3; 9001-62-1; Lipase; Triacylglycerol acylhydrolase; Triacylglycerol lipase; butyrinase; tributyrinase; Tween hy. Enzyme Commission Number: EC 3.1.1.3. CAS No. 9001-62-1. Lipase. Activity: > 30 U/mg. Form: powder, light brown. Source: Rhizopus oryzae. EC 3.1.1.3; 9001-62-1; Lipase; Triacylglycerol acylhydrolase; Triacylglycerol lipase; butyrinase; tributyrinase; Tween hydrolase; steapsin; triacetinase; tributyrin esterase; Tweenase; amno N-AP; Takedo 1969-4-9; Meito MY 30; Tweenesterase; GA 56; capalase L; triglyceride hydrolase; triolein hydrolase; tween-hydrolyzing esterase; amano CE; cacordase; triglyceridase; triacylglycerol ester hydrolase; amano P; amano AP; PPL; glycerol-ester hydrolase; GEH; meito Sangyo OF lipase; hepatic lipase; lipazin; post-heparin plasma protamine-resistant lipase; salt-resistant post-heparin lipase; heparin releasable hepatic lipase; amano CES; amano B; tributyrase; triglyceride lipase; liver lipase; hepatic monoacylglycerol acyltransferase. Cat No: NATE-0404.
Native Rhizopus sp. Amyloglucosidase Quick inquiry Where to buy	Glucan 1,4-alpha-glucosidase is an enzyme located on the brush border of the small intestine with system name 4-alpha-D-glucan glucohydrolase. This enzyme catalyses the following chemical reaction:Hydrolysis0 of terminal (1->4)-linked alpha-D-glucose residues successively from non-reducing ends of the chains with release of beta-D-glucose. Most forms of the enzyme can rapidly hydrolyse 1,6-alpha-D-glucosidic bonds when the next bond in the sequence is 1,4. Applications: Amyloglucosidase is used to hydrolyze α-d-glucosides. it may be used in the brewing of beer and in the production of bread and juices. amyloglucosidase, from rhizopus sp., has been used to study the cl...; amyloglucosidase; γ-amylase; lysosomal α-glucosidase; acid maltase; exo-1,4-α-glucosidase; glucose amylase; γ-1,4-glucan glucohydrolase; acid maltase; 1,4-α-D-glucan glucohydrolase; EC 3.2.1.3; 9032-08-0. Enzyme Commission Number: EC 3.2.1.3. CAS No. 9032-08-0. Glucoamylase. Activity: > 40,000 units/g solid. Storage: -20°C. Form: Lyophilized salt free powder. Source: Rhizopus sp. glucoamylase; amyloglucosidase; γ-amylase; lysosomal α-glucosidase; acid maltase; exo-1,4-α-glucosidase; glucose amylase; γ-1,4-glucan glucohydrolase; acid maltase; 1,4-α-D-glucan glucohydrolase; EC 3.2.1.3; 9032-08-0. Cat No: NATE-0076.
Native Rhizopus sp. Glucoamylase Quick inquiry Where to buy	Glucan 1,4-alpha-glucosidase is an enzyme located on the brush border of the small intestine with system name 4-alpha-D-glucan glucohydrolase. This enzyme catalyses the following chemical reaction: Hydrolysis of terminal (1->4)-linked alpha-D-glucose residues successively from non-reducing ends of the chains with release of beta-D-glucose. Most forms of the enzyme can rapidly hydrolyse 1,6-alpha-D-glycosidic bonds when the next bond in the sequence is 1,4. Applications: This enzyme is useful for structural investigation of carbohydrates and for enzymatic determination of α-amylase when coupled with the related enzymes in clinical analysis. Group: Enzymes. Synonyms: EC 3.2.1.3; glucoamylase; amyloglucosidase; gamma-amylase; lysosomal alpha-glucosidase; acid maltase; exo-1,4-alpha-glucosidase; glucose amylase; gamma-1,4-glucan glucohydrolase; acid maltase; 1,4-alpha-D-glucan glucohydrolase. Enzyme Commission Number: EC 3.2.1.3. CAS No. 9032-08-0. Activity: 30U/mg-solid or more. Appearance: White amorphous powder (salt-free), lyophilized. Form: Freeze dried powder. Source: Rhizopus sp. EC 3.2.1.3; glucoamylase; amyloglucosidase; gamma-amylase; lysosomal alpha-glucosidase; acid maltase; exo-1,4-alpha-glucosidase; glucose amylase; gamma-1,4-glucan glucohydrolase; acid maltase; 1,4-alpha-D-glucan glucohydrolase. Cat No: DIA-190.
Native Rhizopus sp. Pectinase Quick inquiry Where to buy	Pectinases hydrolyses pectin, which is a component of the cell wall. They may attack methyl-esterified pectin or de-esterified pectin. It is a source of pectinase activity, also containing cellulase and hemicellulase activities. Applications: Used in plant protoplast preparation to digest cell wall prior to organelle isolation. petctinase is an enzyme from rhizopus sp. that is used in plant protoplast preparation to digest cell wall prior to organelle isolation. it has been used to digest the cell wall of arabidopsis root cells to study peroxin 16 in peroxisomes and endoplasmic reticulum. pectinases are used to study their role in the invasion of plant tissues by phytopathogens, the spoilage of produce and various food processing and plant biotechnology applications. Group: Enzymes. Synonyms: Pectinase; pectin depolymerase; endopolygalacturonase; pectolase; pectin hydrolase;. Enzyme Commission Number: EC 3.2.1.15. CAS No. 9032-75-1. Pectinase. Activity: > 5 units/mg protein (Lowry). Form: powder. Source: Rhizopus sp. Pectinase; pectin depolymerase; endopolygalacturonase; pectolase; pectin hydrolase; pectin polygalacturonase; endo-polygalacturonase; poly-α-1,4-galacturonide glycanohydrolase; endogalacturonase; endo-D-galacturonase; poly (1,4-α-D-galacturonide) glycanohydrolase; polygalacturonase; EC 3.2.1.15; 9032-75-1. Cat No: NATE-0536.
Native Rhizopus sp. Protease Quick inquiry Where to buy	A protease (also called peptidase or proteinase) is any enzyme that performs proteolysis, that is, begins protein catabolism by hydrolysis of the peptide bonds that link amino acids together in a polypeptide chain. Proteases have evolved multiple times, and different classes of protease can perform the same reaction by completely different catalytic mechanisms. Proteases can be found in animals, plants, bacteria, archaea and viruses. Acidic protease exhibits both proteolytic and lipolytic activities. stable in the acid range of ph 3-5. ph optimum is 3.0. Applications: Protease from rhizopus spp. has been used in a study to assess the amino acid sequences near the amino termini using automated edman degradation. it has also been used in a study to investigate inactivation of the enzyme by reaction with diazoacetyl-dl-norleucine methyl ester in the presence of cupric acetate. Group: Enzymes. Synonyms: Protease; peptidase; proteinase; 9001-92-7. CAS No. 9001-92-7. Protease. Activity: > 0.2 unit/mg solid. Storage: 2-8°C. Form: Supplied as a powder containing dextrin as a stabilizer. Source: Rhizopus sp. Protease; peptidase; proteinase; 9001-92-7. Cat No: NATE-0629.
Native Rhodococcus rhodochrous Epoxide Hydrolase Quick inquiry Where to buy	Epoxide hydrolase (also known as epoxide hydratase) functions in detoxification during drug metabolism. It converts epoxides to trans-dihydrodiols, which can be conjugated and excreted from the body. Epoxides result from the degradation of aromatic compounds. Deficiency in this enzyme in patients receiving aromatic-type anti-epileptic drugs such as phenytoin is reported to lead to DRESS syndrome. Epoxides are significant as cytochrome P450 oxidase metabolites of unsaturated carbon-carbon bonds, but are also mutagenic. Epoxide hydrolase is present in large quantity on endoplasmic reticulum. Group: Enzymes. Synonyms: EC 3.3.2.3; epoxide hydratase; epoxide hydratase (ambiguous); microsomal epoxide hydratase; epoxide hydrase; microsomal epoxide hydrase; arene-oxide hydratase (ambiguous); benzo[a]pyrene-4,5-oxide hydratase; benzo (a)pyrene-. Enzyme Commission Number: EC 3.3.2.3. CAS No. 9048-63-9. mEH. Activity: > 0.5 U/g. Storage: -20°C. Form: lyophilized powder, beige. Source: Rhodococcus rhodochrous. EC 3.3.2.3; epoxide hydratase; epoxide hydratase (ambiguous); microsomal epoxide hydratase; epoxide hydrase; microsomal epoxide hydrase; arene-oxide hydratase (ambiguous); benzo[a]pyrene-4,5-oxide hydratase; benzo (a)pyrene-4,5-epoxide hydratase; aryl epoxide hydrase (ambiguous); cis-epoxide hydrolase; mEH; 9048-63-9. Cat No: NATE-0449.
Native Rhodopseudomonas sphaeroides β-Hydroxybutyrate Dehydrogenase Quick inquiry Where to buy	In mammalian systems, β-hydroxybutyrate dehydrogenase is localized on the inner mitochondrial membrane and requires phosphatidyl choline for activity. In contrast, the enzyme from Pseudomonas is a soluble cytosolic enzyme that does not require a phospholipid allosteric activator. The enzyme is required for the utilization of ketone bodies as a source of metabolic energy. It catalyzes the oxidation of 3-hydroxybutyrate to acetoacetate, the first step in the conversion of ketone bodies to citric acid, which is then further metabolized via the tricarboxylic acid cycle (Krebs cycle). Applications: Suitable for the determination of acetoacetate and d (-)-3...nase; EC 1.1.1.30; 9028-38-0. Enzyme Commission Number: EC 1.1.1.30. CAS No. 9028-38-0. 3-HBDH. Activity: 250-750 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing Tris buffer salts. Source: Rhodopseudomonas sphaeroides. 3-hydroxybutyrate dehydrogenase; 3-HBDH; NAD-β-hydroxybutyRate dehydrogenase; hydroxybutyRate oxidoreductase; β-hydroxybutyRate dehydrogenase; D-β-hydroxybutyRate dehydrogenase; D-3-hydroxybutyRate dehydrogenase; D-(-)-3-hydroxybutyRate dehydrogenase; β-hydroxybutyric acid dehydrogenase; 3-D-hydroxybutyRate dehydrogenase; β-hydroxybutyric dehydrogenase; EC 1.1.1.30; 9028-38-0. Cat No: NATE-0004.
Native Rhodothermus marinus Laminarinase/Lichenase Quick inquiry Where to buy	β-glucanases degrade β-1,4-glucans of cellulose, xyloglucan and β-1,4-xylan. β-Glucanase represents a group of carbohydrate enzymes which break down glycosidic bonds within beta-glucan. It forms the main constituent of fungal cell walls and could be a potential structural and storage polysaccharide of marine macro-algae. It has the ability to degrade fungal cell walls and may be involved in defense mechanism of plants against pathogenic fungi. Group: Enzymes. Synonyms: endo-1,3-β-D-glucanase; laminarinase; laminaranase; β-1,3-glucanase; β-1,3-1,4-glucanase; endo-1,3-β-glucanase; endo-β-1,3 (4)-glucanase; endo-β-1,3-1,4-glucanase; endo-β-(1?3)-D-glucanase; endo-1,3-1,4-β-D-glucanase; endo-β-(1-3)-D-glucan. Enzyme Commission Number: EC 3.2.1.6. CAS No. 62213-14-3. β-glucanase. Source: Rhodothermus marinus. EC 3.2.1.6; endo-1,3-β-D-glucanase; laminarinase; laminaranase; β-1,3-glucanase; β-1,3-1,4-glucanase; endo-1,3-β-glucanase; endo-β-1,3 (4)-glucanase; endo-β-1,3-1,4-glucanase; endo-β-(1?3)-D-glucanase; endo-1,3-1,4-β-D-glucanase; endo-β-(1-3)-D-glucanase; endo-β-1,3-glucanase IV; endo-1,3-β-D-glucanase; 1,3-(1,3; 1,4)-β-D-glucan 3 (4)-glucanohydrolase; endo-1,3 (4)-β-glucanase. Cat No: NATE-0376.
Native Rhodothermus obamensis Hexokinase Quick inquiry Where to buy	A hexokinase is an enzyme that phosphorylates hexoses (six-carbon sugars), forming hexose phosphate. In most organisms, glucose is the most important substrate of hexokinases, and glucose-6-phosphate the most important product. Hexokinase can transfer an inorganic phosphate group from ATP to a substrate. Hexokinases should not be confused with glucokinase, which is a specific isoform of hexokinase. While other hexokinases are capable of phosphorylating several hexoses, glucokinase acts with a 50-fold lower substrate affinity and its only hexose substrate is glucose. Applications: This enzyme is useful for enzymatic determination of glucose or creatinine kinase activity when coupled with glucose-6-phosphate dehydrogenase. Group: Enzymes. Synonyms: hexokinase (phosphorylating); ATP-dependent hexokinase; glucose ATP phosphotransferase; hexokinase; ATP:D-hexose 6-. Enzyme Commission Number: EC 2.7.1.1. CAS No. 9001-51-8. Hexokinase. Mole weight: 140 kDa (gel filtration). Activity: 100 - 400 U/mg. Appearance: White to light grayish lyophilized powder. Storage: Storage at -20°C in the presence of a desiccant is recommended. Form: Freeze dried powder. Source: Rhodothermus obamensis. hexokinase (phosphorylating); ATP-dependent hexokinase; glucose ATP phosphotransferase; hexokinase; ATP:D-hexose 6-phosphotransferase; EC 2.7.1.1. Cat No: NATE-1156.
Native Rhodotorula glutinis Phenylalanine Ammonia-Lyase Quick inquiry Where to buy	Phenylalanine Ammonia-Lyase from Rhodotorula glutinis can be cleaved and inactivated by the proteases chymotrypsin, subtilisin, and trypsin. Applications: Phenylalanine ammonia-lyase has been used in a study to assess the effect of heat treatment on lignification of postharvest bamboo shoots. it has also been used in a study to investigate the effect of light on gene expression and podophyllotoxin biosynthesis in linum album cell culture. Group: Enzymes. Synonyms: phenylalanine ammonia-lyase; EC 4.3.1.24; phenylalanine deaminase; phenylalanine ammonium-lyase; PAL; L-phenylalanine ammonia-lyase; Phe ammonia-lyase; 9024-28-6. Enzyme Commission Number: EC 4.3.1.24. CAS No. 9024-28-6. PAL. Activity: 0.8-2.0 units/mg protein. Storage: -20°C. Form: buffered aqueous glycerol solution; Solution in 60% glycerol, 3 mM Tris-HCl, pH 7.5, containing up to 0.5 M (NH4)2SO4. Source: Rhodotorula glutinis. phenylalanine ammonia-lyase; EC 4.3.1.24; phenylalanine deaminase; phenylalanine ammonium-lyase; PAL; L-phenylalanine ammonia-lyase; Phe ammonia-lyase; 9024-28-6. Cat No: NATE-0502.
Native Rhus vernicifera Laccase Quick inquiry Where to buy	Laccase is a blue copper oxidase that reduces molecular oxygen to water. Laccase oxidizes polyphenols, methoxy-substituted phenols and diamines, but not tyrosine. Oxidation by laccase is an one-electron reaction that generates a free radical. Group: Enzymes. Synonyms: Laccases; EC 1.10.3.2; 80498-15-3; urishiol oxidase; urushiol oxidase; p-diphenol oxidase; benzenediol:oxygen oxidoreductase. Enzyme Commission Number: EC 1.10.3.2. CAS No. 80498-15-3. Laccase. Activity: > 50 units/mg solid. Storage: -20°C. Form: crude acetone powder. Source: Rhus vernicifera. Laccases; EC 1.10.3.2; 80498-15-3; urishiol oxidase; urushiol oxidase; p-diphenol oxidase; benzenediol:oxygen oxidoreductase. Cat No: NATE-0373.
Native Rice α-Glucosidase Quick inquiry Where to buy	Alpha-glucosidase is a glucosidase located in the brush border of the small intestine that acts upon 1,4-alpha bonds. This is in contrast to beta-glucosidase. Alpha-glucosidase breaks down starch and disaccharides to glucose. Maltase, a similar enzyme that cleaves maltose, is nearly functionally equivalent. The enzyme catalyses the hydrolyzis of a-1.6 linked a-galactose residues from oligosaccharides. Group: Enzymes. Synonyms: Alpha-glucosidase; EC 3.2.1.20; maltase; glucoinvertase; glucosidosucrase; maltase-glucoamylase; alpha-glucopyranosidase; glucosidoinvertase; alpha-D-glucosidase; alpha-glucoside hydrolase; alpha-1,4-glucosidase; alpha-D-glucoside glucohydrolase. Enzyme Commission Number: EC 3.2.1.20. CAS No. 9001-42-7. α-Glucosidase. Source: Rice. Alpha-glucosidase; EC 3.2.1.20; maltase; glucoinvertase; glucosidosucrase; maltase-glucoamylase; alpha-glucopyranosidase; glucosidoinvertase; alpha-D-glucosidase; alpha-glucoside hydrolase; alpha-1,4-glucosidase; alpha-D-glucoside glucohydrolase. Cat No: NATE-0041.
Native Russell's viper venom Factor V Activating Enzyme Quick inquiry Where to buy	Factor V activator for RVV contains fucose, mannose, galactose, glucosamine, and neuraminic acid. Factor V activating enzyme from RVV is an arginine esterase that is sensitive to diisopropyl fluorophosphate (DFP). Applications: Factor v activating enzyme from russells viper venom (rvv) is a single-chain glycoprotein that is involved in the rapid clotting of blood. factor v circulates in the blood as an inactive cofactor and must be activated by proteases such as factor v activating enzyme from rvv 1. this product may be useful in studying the blood coagulation cascade as well as the inherited deficiency called parahemophilia. Group: Enzymes. Synonyms: EC 3.4.21.95; Factor V Activating Enzyme; Snake venom factor V activator; 65522-14-7; Factor V activator. Enzyme Commission Number: EC 3.4.21.95. CAS No. 65522-14-7. Factor V activator. Activity: 20 units/mg protein. Storage: -20°C. Form: lyophilized powder; Stabilized in albumin and sodium chloride. Source: Russell's viper venom. EC 3.4.21.95; Factor V Activating Enzyme; Snake venom factor V activator; 65522-14-7; Factor V activator. Cat No: NATE-0249.
Native Saccharomyces cerevisiae Adenosine-5'-triphosphate Sulfurylase Quick inquiry Where to buy	In enzymology, a sulfate adenylyltransferase (EC 2.7.7.4) is an enzyme that catalyzes the chemical reaction:ATP + sulfate<-> diphosphate + adenylyl sulfate. Thus, the two substRates of this enzyme are ATP and sulfate, whereas its two products are diphosphate and adenylyl sulfate. This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). This enzyme participates in 3 metabolic pathways:purine metabolism, selenoamino acid metabolism, and sulfur metabolism. Applications: Adenosine-5?-triphosphate sulfurylase (atp sulfurylase) may be used to study sulfur metabolism and h...s. Synonyms: ATP-sulfurylase; adenosine-5'-triphosphate sulfurylase; adenosinetriphosphate sulfurylase; adenylylsulfate pyrophosphorylase; ATP sulfurylase; sulfurylase; EC 2.7.7.4; 9012-39-9; Sulfate adenylate transferase. Enzyme Commission Number: EC 2.7.7.4. CAS No. 9012-39-9. ATP-sulfurylase. Activity: > 1.0 units/mg protein. Storage: -20°C. Form: lyophilized powder. Contains Citrate buffer salts. Source: Saccharomyces cerevisiae. ATP-sulfurylase; adenosine-5'-triphosphate sulfurylase; adenosinetriphosphate sulfurylase; adenylylsulfate pyrophosphorylase; ATP sulfurylase; sulfurylase; EC 2.7.7.4; 9012-39-9; Sulfate adenylate transferase. Cat No: NATE-0090.
Native Saccharomyces cerevisiae Alcohol Dehydrogenase Quick inquiry Where to buy	Alcohol dehydrogenases (ADH) are a group of dehydrogenase enzymes that occur in many organisms and facilitate the interconversion between alcohols and aldehydes or ketones with the reduction of nicotinamide adenine dinucleotide (NAD+ to NADH). In Humans and many other animals, they serve to break down alcohols that otherwise are toxic, and they also participate in geneRation of useful aldehyde, ketone, or alcohol groups during biosynthesis of various metabolites. In yeast, plants, and many bacteria, some alcohol dehydrogenases catalyze the opposite reaction as part of fermentation to ensure a constant supply of NAD+. Applications: Alcohol dehydrogenase from sacchar...dehydrogenase; NADH-alcohol dehydrogenase; NADH-aldehyde dehydrogenase; primary alcohol dehydrogenase; yeast alcohol dehydrogenase; EC 1.1.1.1. Enzyme Commission Number: EC 1.1.1.1. CAS No. 9031-72-5. Activity: > 300 units/mg protein. Storage: -20°C. Form: Solids containing <2% Citrate buffer salts. Source: Saccharomyces cerevisiae. aldehyde reductase; ADH; alcohol dehydrogenase (NAD); aliphatic alcohol dehydrogenase; ethanol dehydrogenase; NAD-dependent alcohol dehydrogenase; NAD-specific aromatic alcohol dehydrogenase; NADH-alcohol dehydrogenase; NADH-aldehyde dehydrogenase; primary alcohol dehydrogenase; yeast alcohol dehydrogenase; EC 1.1.1.1. Cat No: NATE-0035.
Native Saccharomyces cerevisiae α-Glucosidase Quick inquiry Where to buy	Alpha-glucosidase is a glucosidase located in the brush border of the small intestine that acts upon 1,4-alpha bonds. This is in contrast to beta-glucosidase. Alpha-glucosidase breaks down starch and disaccharides to glucose. Maltase, a similar enzyme that cleaves maltose, is nearly functionally equivalent. Protein determined by biuret. Applications: For the determination of α-amylase and the synthesis of various 1?-o-sucrose and 1-o-fructose esters. α-glucosidase is used for the determination of α-amylase and the synthesis of various 1?-o-sucrose and 1-o-fructose esters. it was also used in the measurement of glycosidase inhibition. Group: Enzymes. Synonyms: α-glucosidase; maltase; glucoinvertase; glucosidosucrase; maltase-glucoamylase; α-glucopyranosidase; glucosidoinve. Enzyme Commission Number: EC 3.2.1.20. CAS No. 9001-42-7. α-Glucosidase. Mole weight: Mr ~63 kDa. Activity: 4-8 units/mg; > 10 units/mg protein (using p-nitrophenyl α-D-glucoside as substrate.). Storage: -20°C. Form: lyophilized powder. Source: Saccharomyces cerevisiae. α-glucosidase; maltase; glucoinvertase; glucosidosucrase; maltase-glucoamylase; α-glucopyranosidase; glucosidoinvertase; α-D-glucosidase; α-glucoside hydrolase; α-1,4-glucosidase; EC 3.2.1.20; 9001-42-7. Cat No: NATE-0752.
Native Saccharomyces cerevisiae Esterase Quick inquiry Where to buy	An esterase is a hydrolase that splits esters into acids and alcohols. Applications: The compound is commonly used for the synthesis of biodiesel and biopolymers, as well as in the production of pharmaceuticals, agr ochemicals and flavor compounds. Group: Enzymes. Synonyms: EC 3.1.1.1; ali-esterase; B-esterase; monobutyrase; cocaine esterase; procaine esterase; methylbutyrase; vitamin A esterase; butyryl esterase; carboxyesterase; carboxylate esterase; carboxylic esterase; methylbutyRate esterase; triacetin esterase; carboxyl ester hydrolase; butyRate esterase; methylbutyrase; α-carboxylesterase; propionyl esterase; nonspecific carboxylesterase; esterase D; esterase B; es. Enzyme Commission Number: EC 3.1.1.1. CAS No. 9016-18-6. Esterase. Activity: ~2 U/g. Storage: 2-8°C. Form: lyophilized powder. Source: Saccharomyces cerevisiae. EC 3.1.1.1; ali-esterase; B-esterase; monobutyrase; cocaine esterase; procaine esterase; methylbutyrase; vitamin A esterase; butyryl esterase; carboxyesterase; carboxylate esterase; carboxylic esterase; methylbutyRate esterase; triacetin esterase; carboxyl ester hydrolase; butyRate esterase; methylbutyrase; α-carboxylesterase; propionyl esterase; nonspecific carboxylesterase; esterase D; esterase B; esterase A; serine esterase; carboxylic acid esterase; cocaine esterase; 9016-18-6. Cat No: NATE-0240.
Native Saccharomyces cerevisiae Glyoxalase I Quick inquiry Where to buy	Glyoxalase I is universally expressed and involved in the protection against cellular damage due to cytotoxic metabolites such as advanced glycation end products (AGEs). It is an integral component of the detoxification system, catalyzing the conversion of reactive, acyclic a-oxoaldehydes into the corresponding a-hydroxyacids in a glutathione-dependent manner. Glyoxalase detoxification system consists of glyoxalase (glo)-i and glo-ii. glo-i is a cytosolic, 42 kda, dimeric zn2+ metalloenzyme. Group: Enzymes. Synonyms: lactoylglutathione lyase; EC 4.4.1.5; methylglyoxalase; aldoketomutase; ketone-aldehyde mutase; glyoxylase I; (R)-S-lactoylglutathione methylglyoxal-lyase (isomerizing); 9033-12-9. Enzyme Commission Number: EC 4.4.1.5. CAS No. 9033-12-9. Glyoxalase I. Mole weight: 42 kDa. Activity: > 400 units/mg protein. Storage: 2-8°C. Form: buffered aqueous glycerol solution; Solution in 50% glycerol, 0.4 M (NH4)2SO4 and 0.002 M KH2PO4 pH 6.5. Source: Saccharomyces cerevisiae. lactoylglutathione lyase; EC 4.4.1.5; methylglyoxalase; aldoketomutase; ketone-aldehyde mutase; glyoxylase I; (R)-S-lactoylglutathione methylglyoxal-lyase (isomerizing); 9033-12-9. Cat No: NATE-0308.
Native Saccharomyces cerevisiae Hexokinase Quick inquiry Where to buy	A hexokinase is an enzyme that phosphorylates hexoses (six-carbon sugars), forming hexose phosphate. In most organisms, glucose is the most important substrate of hexokinases, and glucose-6-phosphate the most important product. Hexokinase can transfer an inorganic phosphate group from ATP to a substrate. Hexokinases should not be confused with glucokinase, which is a specific isoform of hexokinase. While other hexokinases are capable of phosphorylating several hexoses, glucokinase acts with a 50-fold lower substrate affinity and its only hexose substrate is glucose. Group: Enzymes. Synonyms: hexokinase type IV glucokinase; hexokinase D; hexokinase type IV. Enzyme Commission Number: EC 2.7.1.1. CAS No. 9001-51-8. Hexokinase. Mole weight: ~ 54 kDa (monomer); ~110 kDa (dimer). Activity: Type I, > 350 units/mg protein; Type II, > 25 units/mg protein (biuret); Type III, > 130 units/mg protein (biuret). Storage: -20°C. Form: Type I, Lyophilized powder containing phosphate/Citrate pH approx. 7.0; Type II, Type III, Lyophilized powder containing approx. 15% sodium Citrate. Source: Saccharomyces cerevisiae. hexokinase type IV glucokinase; hexokinase D; hexokinase type IV; hexokinase (phosphorylating); ATP-dependent hexokinase; glucose ATP phosphotransferase; hexokinase; ATP:D-hexose 6-phosphotransferase; EC 2.7.1.1; 9001-51-8. Cat No: NATE-0342.
Native Saccharomyces cerevisiae Invertase Glycoprotein Standard Quick inquiry Where to buy	Invertase is an enzyme that catalyzes the hydrolysis (breakdown) of sucrose (table sugar). The resulting mixture of fructose and glucose is called inverted sugar syrup. Related to invertases are sucrases. Invertases and sucrases hydrolyze sucrose to give the same mixture of glucose and fructose. Invertases cleave the O-C (fructose) bond, whereas the sucrases cleave the O-C (glucose) bond. Typically used in manufacturing confectionaries, dietary supplements, and other food grade applications. Applications: The invertase glycoprotein standard can be used to demonstrate n-glycosylation using pngase f with both in-solution and in-gel pr ocedures. the extent of deglycosylation can be assessed by mobility shift on sds-page gels. used in the production of confectionary foods and artificial honey. Group: Enzymes. Synonyms: EC 3.2.1.26; invertase; saccharase; glucosucrase; β-h-fructosidase; &bet. Enzyme Commission Number: EC 3.2.1.26. CAS No. 9001-57-4. Invertase. Storage: 2-8°C. Form: lyophilized powder. Source: Saccharomyces cerevisiae. EC 3.2.1.26; invertase; saccharase; glucosucrase; β-h-fructosidase; β-fructosidase; invertin; sucrase; maxinvert L 1000; fructosylinvertase; alkaline invertase; acid invertase; β-fructofuranosidase; β-D-fructofuranoside fructohydrolase; 9001-57-4. Cat No: NATE-0359.
Native Schizophyllum commune Cholesterol Esterase Quick inquiry Where to buy	Sterol esterase belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. The systematic name of this enzyme class is steryl-ester acylhydrolase. This enzyme participates in bile acid biosynthesis. Applications: This enzyme is useful for enzymatic determination of total cholesterol when coupled with cholesterol oxidase in clinical analysis. Group: Enzymes. Synonyms: cholesterol esterase; cholesteryl ester synthase; triterpenol esterase; cholesteryl esterase; cholesteryl ester hydrolase; sterol ester hydrolase; cholesterol ester hydrolase; cholesterase; acylcholesterol lipase; EC 3.1.1.13; Sterol esterase. Enzyme Commission Number: EC 3.1.1.13. CAS No. 9026-00-0. Cholesterol Esterase. Mole weight: approx. 130 kDa. Activity: GradeIII 2.0 U/mg-solid or more (containing approx. 20% of stabilizers). Stability: Store at -20°C. Appearance: Light brown amorphous powder, lyophilized. Source: Schizophyllum commune. cholesterol esterase; cholesteryl ester synthase; triterpenol esterase; cholesteryl esterase; cholesteryl ester hydrolase; sterol ester hydrolase; cholesterol ester hydrolase; cholesterase; acylcholesterol lipase; EC 3.1.1.13; Sterol esterase. Cat No: DIA-133.
Native Serratia sp. Serrapeptase Quick inquiry Where to buy	Serrapeptase is a protein decomposition enzymes produced by bacteria serratia. Can decompose slow bradykinin, fibrin and fibrinogen. Applications: 1. as pharmaceutical raw materials manufacturing injection, oral agents, executive standard: ybh clinic? used for anti-inflammation, eliminate swelling. promote the dissolution of sputum, thick liquid to drain. promote the migration of antibiotics to lesion. 2. plant and animal protein hydrolysate powder (hap, hvp) production applications the flora and fauna of macromolecular protein hydrolysis into small molecular peptides or amino acids, to facilitate the effective absorption and utilization of protein. 3. the application of baki...y used in beer production, proteins can be ruled out "cold cloudy" phenomenon 7. application of textile industry processing of wool, and improve quality 8. application of leather industry made from the hair removal agent. 9. application of feed industry to improve protein utilization and lower costs. Group: Enzymes. Synonyms: Serratiopeptidase; Serratia E-15 protease; serralysin; serrapeptase; serratiapeptase; serratia peptidase; serratio peptidase; serrapeptidase. CAS No. 70851-98-8. Serrapeptase. Source: Serratia sp. Serratiopeptidase; Serratia E-15 protease; serralysin; serrapeptase; serratiapeptase; serratia peptidase; serratio peptidase; serrapeptidase. Cat No: PHAM-381.
Native Sheep 6-Phosphogluconic Dehydrogenase Quick inquiry Where to buy	In enzymology, a phosphogluconate dehydrogenase (decarboxylating) (EC 1.1.1.44) is an enzyme that catalyzes the chemical reaction:6-phospho-D-gluconate + NADP+<-> D-ribulose 5-phosphate + CO2 + NADPH. Thus, the two substRates of this enzyme are 6-phospho-D-gluconate and NADP+, whereas its 3 products are D-ribulose 5-phosphate, CO2, and NADPH. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. Protein determined by biuret. Group: Enzymes. Synonyms: 6-Phosphogluconic Dehydrogenase; phosphogluconic acid dehydrogenase; 6-phosphogluconic dehydrogenase; 6-phosphogluconic carboxylase; 6-phosphogluconate dehydrogenase (decarboxylating); 6-phospho-D-gluconate dehydrogenase; EC 1.1.1.44; phosphogluconate dehydrogenase; decarbo. Enzyme Commission Number: EC 1.1.1.44. CAS No. 9073-95-4. 6-Phosphogluconic Dehydrogenase. Activity: 2-10 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing Tris buffer. Source: Sheep liver. Species: Sheep. 6-Phosphogluconic Dehydrogenase; phosphogluconic acid dehydrogenase; 6-phosphogluconic dehydrogenase; 6-phosphogluconic carboxylase; 6-phosphogluconate dehydrogenase (decarboxylating); 6-phospho-D-gluconate dehydrogenase; EC 1.1.1.44; phosphogluconate dehydrogenase; decarboxylating; 9073-95-4. Cat No: NATE-0008.
Native Sheep Cyclooxygenase 1 Quick inquiry Where to buy	COX-1 catalyzes the conversion of arachidonic acid to prostaglandin H2 (the first step in the biosynthesis of prostaglandins, thromboxanes, and prostacyclins). It is involved in the homeostatic role of eicosanoids and constitutively almost all animal tissues. Has an apparent KM of 8.3 μM for arachidonic acid. Group: Enzymes. Synonyms: COX-1; Constitutive cyclooxygenase; Prostaglandin H synthase 1; Prostaglandin endoperoxide synthase; EC 1.14.99.1; prostaglandin synthase; prostaglandin G/H synthase; (PG)H synthase; PG synthetase; prostaglandin synthetase; fatty acid cyclooxygenase; prostaglandin endoperoxide synthetase. Enzyme Commission Number: EC 1.14.99.1. CAS No. 9055-65-6. Purity: > 95% (SDS-PAGE). COX-1. Mole weight: dimer subunit mol wt 70 kDa. Activity: > 40,000 units/mg protein. Storage: -70°C. Form: aqueous solution. Solution in 80 mM Tris-HCl, pH 8, with 0.1% TWEEN 20 and 300 μM diethyldithiocarbamate. Source: Sheep. COX-1; Constitutive cyclooxygenase; Prostaglandin H synthase 1; Prostaglandin endoperoxide synthase; EC 1.14.99.1; prostaglandin synthase; prostaglandin G/H synthase; (PG)H synthase; PG synthetase; prostaglandin synthetase; fatty acid cyclooxygenase; prostaglandin endoperoxide synthetase. Cat No: NATE-0149.
Native Sheep Hyaluronidase Quick inquiry Where to buy	Hyaluronidase degrades hyaluronan and has been found to be inappropriately regulated during cancer progression. These enzymes randomly cleave β-N-acetylhexosamine-[1?4] glycosidic bonds in hyaluronic acid, chondroitin, and chondroitin sulfates. Group: Enzymes. Synonyms: hyaluronoglucosaminidase; hyaluronidase; hyaluronoglucosidase; chondroitinase; chondroitinase I; hyaluronate 4-glycanohydrolase; EC 3.2.1.35; 37326-33-3. Enzyme Commission Number: EC 3.2.1.35. CAS No. 37326-33-3. Hyaluronidase. Mole weight: mol wt 55 kDa. Activity: Type I, > 1,500 units/mg solid; Type II, > 300 units/mg solid. Storage: -20°C. Form: Type I, lyophilized powder; Type II, Lyophilized powder containing lactose. Source: Sheep testes. Species: Sheep. hyaluronoglucosaminidase; hyaluronidase; hyaluronoglucosidase; chondroitinase; chondroitinase I; hyaluronate 4-glycanohydrolase; EC 3.2.1.35; 37326-33-3. Cat No: NATE-0348.
Native Sheep Sorbitol Dehydrogenase Quick inquiry Where to buy	Sorbitol dehydrogenase is an enzyme in carbohydrate metabolism converting sorbitol, the sugar alcohol form of glucose, into fructose. Together with aldose reductase, it provides a way for the body to produce fructose from glucose without using ATP. Sorbitol dehydrogenase uses NAD+ as a cofactor; its reaction is sorbitol + NAD+--> fructose + NADH + H+. A zinc ion is also involved in catalysis. Organs that use it most frequently include the liver and seminal vesicle; it is found in all kinds of organisms from bacteria to humans. A secondary use is the metabolism of dietary sorbitol, though sorbitol is known not to be absorbed as well in the intestine as its related compounds ...rogenase; glucitol dehydrogenase; L-iditol:NAD+ oxidoreductase; NAD+-dependent sorbitol dehydrogenase; NAD+-sorbitol dehydrogenase; L-iditol 2-dehydrogenase. Enzyme Commission Number: EC 1.1.1.14. CAS No. 9028-21-1. SDH. Activity: > 20 units/mg protein. Storage: -20°C. Form: lyophilized powder; Contains maltose. Source: Sheep liver. Species: Sheep. Sorbitol dehydrogenase; SDH; EC 1.1.1.14; 9028-21-1; polyol dehydrogenase; sorbitol dehydrogenase; L-iditol:NAD+ 5-oxidoreductase; L-iditol (sorbitol) dehydrogenase; glucitol dehydrogenase; L-iditol:NAD+ oxidoreductase; NAD+-dependent sorbitol dehydrogenase; NAD+-sorbitol dehydrogenase; L-iditol 2-dehydrogenase. Cat No: NATE-0668.
Native Silphium perfoliatum L. Superoxide Dismutase Quick inquiry Where to buy	Superoxide dismutase (SOD) catalyzes the dismutation of superoxide radicals to hydrogen peroxide and molecular oxygen. SOD plays a critical role in the defense of cells against the toxic effects of oxygen radicals. SOD competes with nitric oxide (NO) for superoxide anion (which reacts with NO to form peroxynitrite), thereby SOD promotes the activity of NO. SOD has also been shown to suppress apoptosis in cultured rat ovarian follicles, neural cell lines, and transgenic mice by preventing the conversion of NO to peroxynitrate, an inducer of apoptosis. Applications: Mainly used in health food, cosmetics, medical drugs, biochemical agents supporting raw materials and additives. Group: Enzymes. Synonyms: Superoxide dismutases; EC 1.15.1.1; copper-zinc superoxide dismutase; Cu-Zn superoxide dismutase; Cu,Zn-SOD. Enzyme Commission Number: EC 1.15.1.1. CAS No. 9054-89-1. SOD. Mole weight: 32kD. Storage: at -4-25°C, dry, dark conditions for 3 years. Form: Light blue-green lyophilized powder. Source: Silphium perfoliatum L. Superoxide dismutases; EC 1.15.1.1; superoxidase dismutase; copper-zinc superoxide dismutase; Cu-Zn superoxide dismutase; Cu,Zn-SOD. Cat No: NATE-1619.
Native Sinapis alba (white mustard) seed Thioglucosidase Quick inquiry Where to buy	Myrosinases are present in many bacteria, fungi, and edible plants, including those of the Brassicaceae (Cruciferae) family. The enzyme hydrolyzes the S-glucosidic bond of a glucosinolate substrate to form an unstable aglycone that rearranges with the loss of sulfate primarily to the isothiocyanate, though thiocyanates and nitriles are also formed. Many of the isothiocyanate products of aliphatic and aromatic glucosinolates have cancer chemopreventive properties. Thioglucosidase research has f ocused mainly on the cruciferous crops due to their economic importance and cancer preventive benefits. Applications: Thioglucosidase has been used in a study to assess brassica species screening for glucosinolate content. thioglucosidase has also been used in a study to investigate a negative regulatory role for auxin in sulphate deficiency response in arabidopsis thaliana. Group: Enzymes. Synonyms: thioglucosidase; EC 3.2.1.147; myrosinase; sinigrinase; sinigrase; Glucosinolase; Thioglucoside glucohydrolase; 90. Enzyme Commission Number: EC 3.2.1.147. CAS No. 9025-38-1. Myrosinase. Activity: > 100 units/g solid. Storage: -20°C. Source: Sinapis alba (white mustard) seed. Species: Sinapis alba. thioglucosidase; EC 3.2.1.147; myrosinase; sinigrinase; sinigrase; Glucosinolase; Thioglucoside glucohydrolase; 9025-38-1. Cat No: NATE-0468.
Native Snake Venom Carinactivase Quick inquiry Where to buy	Native Snake Venom Carinactivase. Group: Enzymes. Synonyms: CA-1; Prothrombin activator. Purity: > 90% (SDS-PAGE). Carinactivase. Mole weight: 55000. Stability: 1 year. Storage: at -20°CNote: Do not freeze. Form: Liquid, Solution in 50% glycerol (w/v). Source: Snake Venom. CA-1; Prothrombin activator; Carinactivase. Cat No: NATE-1605.
Native Sphingomyelinase from Streptomyces sp. Quick inquiry Where to buy	Sphingomyelin phosphodiesterase is a hydrolase enzyme that is involved in sphingolipid metabolism reactions. SMase is a member of the DNase I superfamily of enzymes and is responsible for breaking sphingomyelin (SM) down into phosphocholine and ceramide. The activation of SMase has been suggested as a major route for the production of ceramide in response to cellular stresses. Applications: This enzyme is useful for enzymatic determination of sphingomyelin when coupled with alkaline phosphatase and choline oxidase. Group: Enzymes. Synonyms: Sphingomyelin phosphodiesterase; EC 3.1.4.12; neutral sphingomyelinase; 9031-54-3; sphingomyelin cholinephosphohydrolase; sphingomyelinase; Smase. Enzyme Commission Number: EC 3.1.4.12. CAS No. 9031-54-3. SMase. Mole weight: 37.5 kDa (SDS-PAGE). Activity: > 500 U/mg. Stability: At least one year at ?20°C. Appearance: White to brownish amorphous powder?lyophilized. Storage: Storage at ?20°C in the presence of a desiccant is recommended. Form: Freeze dried powder. Source: Streptomyces sp. Sphingomyelin phosphodiesterase; EC 3.1.4.12; neutral sphingomyelinase; 9031-54-3; sphingomyelin cholinephosphohydrolase; sphingomyelinase; Smase. Cat No: NATE-1160.
Native Spinach Aldolase Quick inquiry Where to buy	Fructose-bisphosphate aldolase (EC 4.1.2.13), often just aldolase, is an enzyme catalyzing a reversible reaction that splits the aldol, fructose 1,6-bisphosphate, into the triose phosphates dihydroxyacetone phosphate (DHAP) and glyceraldehyde 3-phosphate (G3P). Aldolase can also produce DHAP from other (3S,4R)-ketose 1-phosphates such as fructose 1-phosphate and sedoheptulose 1,7-bisphosphate. Gluconeogenesis and the Calvin cycle, which are anabolic pathways, use the reverse reaction. Glycolysis, a catabolic pathway, uses the forward reaction. Aldolase is divided into two classes by mechanism. Protein determined by lowry. Group: Enzymes. Synonyms: aldolase; fructose-1,6-bisphosphate triosephosphate-lyase; Fructose-bisphosphate aldolase; fructose diphosphate aldolase; D-fructose-1,6-bisphosphate D-glyceraldehyde-3-phosphate-lyase; EC 4.1.2.13; 9024-52-6. Enzyme Commission Number: EC 4.1.2.13. CAS No. 9024-52-6. Aldolase. Activity: 0.3-1.0 units/mg protein. Storage: -20°C. Form: lyophilized powder. Source: Spinach. aldolase; fructose-1,6-bisphosphate triosephosphate-lyase; Fructose-bisphosphate aldolase; fructose diphosphate aldolase; D-fructose-1,6-bisphosphate D-glyceraldehyde-3-phosphate-lyase; EC 4.1.2.13; 9024-52-6. Cat No: NATE-0049.
Native Spinach D-Ribulose 1,5-Diphosphate Carboxylase Quick inquiry Where to buy	Ribulose-1,5-bisphosphate carboxylase/oxygenase, commonly known by the abbreviation RuBisCO, is an enzyme involved in the first major step of carbon fixation, a process by which atmospheric carbon dioxide is converted by plants to energy-rich molecules such as glucose. In chemical terms, it catalyzes the carboxylation of ribulose-1,5-bisphosphate (also known as RuBP). It is probably the most abundant protein on Earth. Applications: D-ribulose 1,5-diphosphate carboxylase from spinach has been used in a study to assess catalytic by-product formation and ligand binding by ribulose bisphosphate carboxylases from different phylogenies. d-ribulose 1,5-diphosphate carboxy...hate carboxylase/oxygenase; rubisco; 3-phospho-D-glyceRate carboxy-lyase (dimerizing; D-ribulose 1,5-bisphosphate-forming); 3-phospho-D-glyceRate carboxy-lyase (dimerizing); 9027-23-0. Enzyme Commission Number: EC 4.1.1.39. CAS No. 9027-23-0. RuBisCO. Activity: 0.01-0.1 unit/mg solid. Storage: -20°C. Form: partially purified powder. Source: Spinach. EC 4.1.1.39, D-ribulose 1,5-diphosphate carboxylase; D-ribulose-1,5-bisphosphate carboxylase; RuBP carboxylase; carboxydismutase; diphosphoribulose carboxylase; ribulose 1,5-bisphosphate carboxylase; ribulose 1,5-bisphosphate carboxylase/oxygenase; ribulose 1,5-diphosphate carboxylase; ribulose 1,5-diphosphate carboxylas
Native Spinach Glutathione Reductase Quick inquiry Where to buy	Glutathione reductase (GR) is a crucial flavoenzyme in the antioxidant defense system. Reduced glutathione (GSH) is used by glutathione peroxidase to detoxify hydrogen peroxide and in the precess is converted to oxidized glutathione (GSSG). The GSSG is then recycled back to GSH by glutathione reductase (GR) using NADPH that is then converted to NADP+. The regenerated GSH is then available to detoxify more hydrogen peroxide. The enzyme uses FAD as a cofactor. GR and glutathione peroxidase may inhibit lipid peroxidation by functioning as antioxidant enzymes in sperm. Glutathione reductase shares a structural motif with a number of other proteins including aspartyl proteases, ...PH-glutathione reductase; GSH reductase; GSSG reductase; NADPH-GSSG reductase; glutathione S-reductase; NADPH:oxidized-glutathione oxidoreductase. Enzyme Commission Number: EC 1.6.4.2. CAS No. 9001-48-3. GR. Mole weight: mol wt 118 kDa. Activity: 100-200 units/mg protein. Storage: 2-8°C. Form: ammonium sulfate suspension; Suspension in 3.6 M (NH4)2SO4 mM, 10 mM potassium phosphate, pH 7.0. Source: Spinach. EC 1.6.4.2; 9001-48-3; Glutathione Reductase; GR; glutathione reductase; glutathione reductase (NADPH); NADPH-glutathione reductase; GSH reductase; GSSG reductase; NADPH-GSSG reductase; glutathione S-reductase; NADPH:oxidized-glutathione oxidoreductase. Cat No: NATE-0318.
Native Spinach Phosphoriboisomerase Quick inquiry Where to buy	Phosphoriboisomerase is responsible for the converstion of ribose 5-phosphate to ribulose 5-phosphate. Applications: Phosphoriboisomerase is used to study the ribulose monophosphate pathway. phosphoriboisomerase from spinach is used in enzyme assays to convert ribose 5-phosphate to ribulose 5-phosphate. Group: Enzymes. Synonyms: ribose-5-phosphate isomerase; phosphopentosisomerase; phosphoriboisomerase; ribose phosphate isomerase; 5-phosphoribose isomerase; D-ribose 5-phosphate isomerase; D-ribose-5-phosphate ketol-isomerase; EC 5.3.1.6; 9023-83-0. Enzyme Commission Number: EC 5.3.1.6. CAS No. 9023-83-0. Phosphoriboisomerase. Activity: > 75 units/mg protein (biuret). Storage: -20°C. Form: partially purified powder. Source: Spinach. ribose-5-phosphate isomerase; phosphopentosisomerase; phosphoriboisomerase; ribose phosphate isomerase; 5-phosphoribose isomerase; D-ribose 5-phosphate isomerase; D-ribose-5-phosphate ketol-isomerase; EC 5.3.1.6; 9023-83-0. Cat No: NATE-0561.
Native Spinacia oleracea (Spinach) Ferredoxin-NADP+ Reductase Quick inquiry Where to buy	Ferredoxin-NADP+ reductase catalyzes the reversible conversion of reduced ferredoxin to oxidized ferredoxin during photosynthesis. Ferredoxin-NADP (H) reductase constitutes a family of hydrophilic FAD-containing monomeric enzymes that deliver NADPH or low potential one-electron donors to redox-based metabolisms in plastids, mitochondria, and bacteria. Applications: Ferredoxin-nadp+ reductase was used in in vitro ferredoxin-dependent desaturation of fatty acids in cyanobacterial thylakoid membranes. it was also used to regulate glyceraldehyde-3-phosphate dehydrogenase. Group: Enzymes. Synonyms: EC 1.18.1.2; ferredoxin-nicotinamide adenine dinucleotide phosphate reductase; ferredoxin-NADP+ reducta. Enzyme Commission Number: EC 1.18.1.2. CAS No. 9029-33-8. FNR. Activity: > 15 units/mg solid, secondary activity: > 10 units/mg solid NADPH diaphorase. Storage: -20°C. Form: lyophilized powder. Source: Spinacia oleracea (Spinach). EC 1.18.1.2; ferredoxin-nicotinamide adenine dinucleotide phosphate reductase; ferredoxin-NADP+ reductase; TPNH-ferredoxin reductase; ferredoxin-NADP+oxidoreductase; NADP+:ferredoxin oxidoreductase; ferredoxin-TPN reductase; ferredoxin-NADP+-oxidoreductase; NADPH:ferredoxin oxidoreductase; ferredoxin-nicotinamide-adenine dinucleotide phosphate (oxidized) reductase; 9029-33-8; FNR. Cat No: NATE-0256.
Native Sporosarcina sp. L-Phenylalanine Dehydrogenase Quick inquiry Where to buy	Phenylalanine dehydrogenase is a member of a large family of amino-acid dehydrogenases, which includes glutamate dehydrogenase, alanine dehydrogenase, leucine dehydrogenase, lysine EUR-dehydrogenase, and meso-a,EUR-diaminopimelate D-dehydrogenase. The three known gene sequences are octomers. It has a two-domain, three-dimensional structure. Applications: L-phenylalanine dehydrogenase is a nad+-dependent oxidoreductase that catalyzes the reversible, oxidative deamination of l-phenylalanine which results in its degradation. l-phenylalanine dehydrogenase is used to study phenylalanine metabolism and phenylalanine, tyrosine and tryptophan biosynthesis. Group: Enzymes. Synonyms: phenylalanine dehydrogenase; EC 1.4.1.20; L-phenylalanine dehydrogenase; PHD; 69403-12-9. Enzyme Commission Number: EC 1.4.1.20. CAS No. 69403-12-9. PHD. Activity: > 6 units/mg solid. Storage: -20°C. Form: lyophilized powder. Source: Sporosarcina sp. phenylalanine dehydrogenase; EC 1.4.1.20; L-phenylalanine dehydrogenase; PHD; 69403-12-9. Cat No: NATE-0558.
Native Staph aureus V8 Protease (Endoproteinase Glu-C) Quick inquiry Where to buy	Protease S. aureus V8 (Endoproteinase-Glu-C) specifically cleaves peptide bonds on the COOH-terminal side of either aspartic or glutamic acids. In the presence of ammonium, the enzyme specificity is limited to glutamic sites. It has a molecular weight of 27 kDa daltons and optimum pH's of 4.0 and 7.8 with hemoglobin as the substrate. Protease S. aureus V8 is inhibited by diisopropylfluorophosphate and monovalent anions such as F-, Cl-, CH3COO-and NO3. Enzyme activity is determined by the casein digestion assay described by Drapeau. Protease s. aureus v8 (endoproteinase-glu-c) specifically cleaves peptide bonds on the cooh-terminal side of either aspartic or glutamic acids. Group: Enzymes. Synonyms: EC 3.4.21.19; Staph aureus V8 Protease; Prot. Enzyme Commission Number: EC 3.4.21.19. CAS No. 137010-42-5. Purity: Chromatographically purified. V8 Protease. Mole weight: 27 kDa (Drapeau 1978). Activity: > 500 units per mg dry weight. Stability: Autolysis occurs at temperatures > 40°C. The enzyme is fully active in USP 0.2% SDS. Stable for 12 months at 2-8°C. Storage: Store at 2-8°C. Form: Lyophilized powder. Source: Staph aureus V8. EC 3.4.21.19; Staph aureus V8 Protease; Protease, Staph aureus (Endoproteinase Glu-C); Glutamyl endopeptidase; V8 proteinase, endoproteinase Glu-C; staphylococcal serine proteinase. Cat No: NATE-0730.
Native Staphylococcus aureus α-Hemolysin Quick inquiry Where to buy	α-Hemolysin is a 33 kDa extracellular protein secreted by most strains of pathogenic Staphylococcus aureus. It is selectively hemolytic and has a marked preference for rabbit red blood cells. It induces dermonecrosis, spastic muscle paralysis, and it is lethal for laboratory animals. The toxin must be in the monomeric form to initially bind to a membrane and specific receptors are not required for binding. Upon binding to biological membranes and/or artificial membranes, self-oligomerization occurs, resulting in ring structures (hexameric aggregates) believed to represent transmembrane pores, which are permeable to ions and small metabolites. Group: Enzymes. Synonyms: α-Hemolysin; 94716-94-6; α-Toxin. α-Hemolysin. Activity: > 10,000 units/mg protein. Storage: 2-8°C. Source: Staphylococcus aureus. α-Hemolysin; 94716-94-6; α-Toxin. Cat No: NATE-0753.
Native Staphylococcus aureus Nuclease micrococcal Quick inquiry Where to buy	Micrococcal Nuclease is an endo-exonuclease that preferentially digests single-stranded nucleic acids. The rate of cleavage is 30 times greater at the 5' side of A or T than at G or C and results in the production of mononucleotides and oligonucleotides with terminal 3'-phosphates. The enzyme is also active against double-stranded DNA and RNA and all sequences will be ultimately cleaved. Applications: Nuclease from staphyl oc occus aureus has been used in a study to assess coagulase and heat-resistant strains found in animals. it has also been used in a study to investigate the expression characteristic of two genes in s. aureus that encode two thermostable nucleases. Group: Enzymes. Synonyms: Micrococcal Nuclease; EC 3.1.31.1; spleen endonuclease; thermonuclease; nuclease T; micrococcal endonuclease; nuclease T'; staphylococcal nucle. Enzyme Commission Number: EC 3.1.31.1. CAS No. 9013-53-0. MNase. Activity: 100-300 units/mg protein. Storage: -20°C. Source: Staphylococcus aureus. Micrococcal Nuclease; EC 3.1.31.1; spleen endonuclease; thermonuclease; nuclease T; micrococcal endonuclease; nuclease T'; staphylococcal nuclease; spleen phosphodiesterase; Staphylococcus aureus nuclease; Staphylococcus aureus nuclease B; ribonucleate (deoxynucleate) 3'-nucleotidohydrolase; 9013-53-0; Endonuclease micrococcal; MNase. Cat No: NATE-0452.
Native Staphylococcus aureus Sphingomyelinase Quick inquiry Where to buy	Sphingomyelin phosphodiesterase is a hydrolase enzyme that is involved in sphingolipid metabolism reactions. SMase is a member of the DNase I superfamily of enzymes and is responsible for breaking sphingomyelin (SM) down into phosphocholine and ceramide. The activation of SMase has been suggested as a major route for the production of ceramide in response to cellular stresses. Group: Enzymes. Synonyms: Sphingomyelin phosphodiesterase; EC 3.1.4.12; neutral sphingomyelinase; 9031-54-3; sphingomyelin cholinephosphohydrolase; sphingomyelinase; SMase. Enzyme Commission Number: EC 3.1.4.12. CAS No. 9031-54-3. SMase. Activity: 100-300 units/mg protein (Lowry). Storage: 2-8°C. Form: buffered aqueous glycerol solution; Solution in 50% glycerol containing 0.25 M phosphate buffer, pH 7.5. Source: Staphylococcus aureus. Sphingomyelin phosphodiesterase; EC 3.1.4.12; neutral sphingomyelinase; 9031-54-3; sphingomyelin cholinephosphohydrolase; sphingomyelinase; SMase. Cat No: NATE-0673.
Native Staphylococcus aureus Staphopain A Quick inquiry Where to buy	Staphopains A and B are part of the staphylococcal proteolytic cascade (SPC) and may contribute to tissue invasion and metastatic infections of Staphylococcus aureus. Staphopain A, along with Staphopain B, may contribute to septic shock through the release of bradykinin and S-kinin from human kininogens. This activity required proteolytically-active Staphopain A and was augmented by Staphopain B. Staphopain a is inhibited by staphostatin a, e-64, and heavy metal ions such as hg2+ and ag+. staphopain a is also inhibited by plasma α2-macroglobulin but not by human cystatin c. staphopain a and staphopain b, members of the peptidase c47 family, are the major cysteine proteases secreted by s. aureus. Applications: Staphopain a was used for cleaving the n terminus of atypical chemokine receptor (ackr2) to suppress its ligand internalization activity in a study on the pivotal role of ackr2 in ligand binding, internalization and scavenging of inflammatory responses. Group: Enzymes. Synonyms: Staphopain; EC 3.4.2. Enzyme Commission Number: EC 3.4.22.48. CAS No. 347841-89-8. Staphopain. Mole weight: mol wt ~20 kDa by SDS-PAGE. Storage: -20°C. Form: lyophilized powder. Source: Staphylococcus aureus. Staphopain; EC 3.4.22.48; staphylopain; 347841-89-8; ScpA; Staphopain A; Staphylococcal cysteine proteinase A; Staphylopain A. Cat No: NATE-0666.
Native Staphylococcus aureus Staphopain B Quick inquiry Where to buy	Staphopains A and B are part of the staphylococcal proteolytic cascade (SPC) and may contribute to tissue invasion and metastatic infections of Staphylococcus aureus. Staphopain A, along with Staphopain B, may contribute to septic shock through the release of bradykinin and S-kinin from human kininogens. This activity required proteolytically-active Staphopain A and was augmented by Staphopain B. Staphopain activity is inhbited by staphostatin b (sspc) and e-64. staphopain activity is stimulated by edta. staphopain a and staphopain b, members of the peptidase c47 family, are the major cysteine proteases secreted by s. aureus. Group: Enzymes. Synonyms: Staphopain; EC 3.4.22.48; staphylopain; 347841-89-8; Staphopain B; Staphylococcal cysteine proteinase B; Staphylopain B; sspB. Enzyme Commission Number: EC 3.4.22.48. CAS No. 347841-89-8. Purity: > 95% (SDS-PAGE). Staphopain. Mole weight: mol wt ~20 kDa by SDS-PAGE. Storage: -20°C. Source: Staphylococcus aureus. Staphopain; EC 3.4.22.48; staphylopain; 347841-89-8; Staphopain B; Staphylococcal cysteine proteinase B; Staphylopain B; sspB. Cat No: NATE-0683.
Native Staphylococcus epidermidis D-Lactic Dehydrogenase Quick inquiry Where to buy	D-lactic dehydrogenase catalyzes the conversion of D-lactate into D-pyruvate while reducing NAD+ to NADH and H+. Applications: D-lactic dehydrogenase can be used to generate inhibitors of angiotensin converting enzyme by catalyzing the production of the intermediate (r)-2-hydroxy-4-phenylbutyric acid. d-lactic dehydrogenase has been used in a study to assess mechanisms of active transport in isolated membrane vesicles. it has also been used in a study to investigate β-galactoside transport in bacterial membrane preparations. Group: Enzymes. Synonyms: EC 1.1.1.28, D-Lactic Dehydrogenase; 9028-36-8; lactic acid dehydrogenase; D-specific lactic dehydrogenase; D-(-)-lactate dehydrogenase (NAD); D-lactic acid dehydrogenase; D-lactic dehydrogenase; (R)-Lactate:NAD+ oxidoreductase; D-LDH. Enzyme Commission Number: EC 1.1.1.28. CAS No. 9028-36-8. D-LDH. Activity: > 80 units/mg solid. Storage: -20°C. Form: Lyophilized powder containing primarily dextran. Source: Staphylococcus epidermidis. EC 1.1.1.28, D-Lactic Dehydrogenase; 9028-36-8; lactic acid dehydrogenase; D-specific lactic dehydrogenase; D-(-)-lactate dehydrogenase (NAD); D-lactic acid dehydrogenase; D-lactic dehydrogenase; (R)-Lactate:NAD+ oxidoreductase; D-LDH. Cat No: NATE-0197.
Native Staphylococcus staphylolyticus Lysostaphin Quick inquiry Where to buy	Lysostaphin is a Staphylococcus simulans metalloendopeptidase. It can function as an antimicrobial against Staphylococcus aureus. Lysostaphin is a 27 KDa glycylglycine endopeptidase, an antibacterial enzyme which is capable of cleaving the crosslinking pentaglycin bridges in the cell wall of Staphylococci. Group: Enzymes. Synonyms: Lysostaphin; EC 3.4.24.75; glycyl-glycine endopeptidase; 9011-93-2. Enzyme Commission Number: EC 3.4.24.75. CAS No. 9011-93-2. Lysostaphin. Activity: Type I, > 2,000 units/mg protein; Type II, > 500 units/mg protein. Storage: -20°C. Form: lyophilized powder. Source: Staphylococcus staphylolyticus. Lysostaphin; EC 3.4.24.75; glycyl-glycine endopeptidase; 9011-93-2. Cat No: NATE-0429.
Native Streptococcus faecalis L-Phenylalanine decarboxylase Quick inquiry Where to buy	In enzymology, a phenylalanine decarboxylase (EC 4.1.1.53) is an enzyme that catalyzes the chemical reaction:L-phenylalanine<-> phenylethylamine + CO2. Hence, this enzyme has one substrate, L-phenylalanine, and two products, phenylethylamine and CO2. This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. This enzyme participates in phenylalanine metabolism. It employs one cofactor, pyridoxal phosphate. Group: Enzymes. Synonyms: phenylalanine decarboxylase; L-phenylalanine decarboxylase; aromatic L-amino acid decarboxylase; L-phenylalanine carboxy-lyase; EC 4.1.1.53; 9075-72-3. Enzyme Commission Number: EC 4.1.1.53. CAS No. 9075-72-3. L-Phenylalanine decarboxylase. Activity: > 5 units/g solid. Storage: -20°C. Form: Dried cells from which activity can be extracted. Source: Streptococcus faecalis. phenylalanine decarboxylase; L-phenylalanine decarboxylase; aromatic L-amino acid decarboxylase; L-phenylalanine carboxy-lyase; EC 4.1.1.53; 9075-72-3. Cat No: NATE-0415.
Native Streptococcus faecalis L-Tyrosine Decarboxylase Quick inquiry Where to buy	In enzymology, a tyrosine decarboxylase (EC 4.1.1.25) is an enzyme that catalyzes the chemical reaction:L-tyrosine<-> tyramine + CO2. Hence, this enzyme has one substrate, L-tyrosine, and two products, tyramine and carbon dioxide. This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. This enzyme participates in tyrosine metabolism and alkaloid biosynthesis. It employs one cofactor, pyridoxal phosphate. Applications: L-tyrosine decarboxylase from strept oc occus faecalis has been used in a study to isolate and identify the carbonyl-active site of diamine oxidase by gas chromatographic mass spectrometry. l-tyrosine decarboxylase from strept oc occus faecalis has also been used in a study to investigate the adsorption of strept oc occus faecalis on diatomite carriers for use in biotransformations. Group: Enzymes. Synonyms: tyrosine decarboxylase; EC 4.1.1.25; L-tyrosine decarboxylase; L-(-)-tyrosine apodecarboxylase; L-tyrosine carboxy-lyase; 9002-09-9. Enzyme Commission Number: EC 4.1.1.25. CAS No. 9002-9-9. L-Tyrosine Decarboxylase. Activity: > 0.1 unit/mg solid. Storage: -20°C. Source: Streptococcus faecalis. tyrosine decarboxylase; EC 4.1.1.25; L-tyrosine decarboxylase; L-(-)-tyrosine apodecarboxylase; L-tyrosine carboxy-lyase; 9002-09-9. Cat No: NATE-0421.
Native Streptococcus faecalis L-Tyrosine Decarboxylase Apoenzyme Quick inquiry Where to buy	In enzymology, a tyrosine decarboxylase (EC 4.1.1.25) is an enzyme that catalyzes the chemical reaction:L-tyrosine<-> tyramine + CO2. Hence, this enzyme has one substrate, L-tyrosine, and two products, tyramine and carbon dioxide. This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. This enzyme participates in tyrosine metabolism and alkaloid biosynthesis. It employs one cofactor, pyridoxal phosphate. Applications: L-tyrosine decarboxylase apoenzyme from strept oc occus faecalis has been used in a study to purify and characterize tyrosine decarboxylase and aromatic-l-amino-acid decarboxylase. l-tyrosine decarboxylase apoenzyme from strept oc occus faecalis has also been used in a study to investigate the stereospecificity of sodium borohydride reduction of tyrosine decarboxylase. Group: Enzymes. Synonyms: tyrosine decarboxylase; EC 4.1.1.25; L-tyrosine decarb. Enzyme Commission Number: EC 4.1.1.25. CAS No. 9002-9-9. L-Tyrosine Decarboxylase. Activity: <0.005 unit/mg solid (without pyridoxal 5-phosphate),> 0.05 unit/mg solid (with excess pyridoxal 5-phosphate). Storage: -20°C. Source: Streptococcus faecalis. tyrosine decarboxylase; EC 4.1.1.25; L-tyrosine decarboxylase; L-(-)-tyrosine apodecarboxylase; L-tyrosine carboxy-lyase; 9002-09-9. Cat No: NATE-0420.
Native Streptococcus faecalis Ornithine Transcarbamylase Quick inquiry Where to buy	Ornithine transcarbamylase (OTC) is an enzyme that catalyzes the reaction between carbamoyl phosphate (CP) and ornithine (Orn) to form citrulline (Cit) and phosphate (Pi). In plants and microbes, OTC is involved in arginine (Arg) biosynthesis, whereas in mammals it is located in the mitochondria and is part of the urea cycle. Group: Enzymes. Synonyms: Ornithine transcarbamylase; EC 2.1.3.3; citrulline phosphorylase; ornithine transcarbamylase; OTC; OTCase; carbamylphosphate-ornithine transcarbamylase; L-ornithine carbamoyltransferase; L-ornithine carbamyltransferase; L-ornithine transcarbamylase; ornithine carbamyltransferase; 9001-69-8. Enzyme Commission Number: EC 2.1.3.3. CAS No. 9001-69-8. OTC. Activity: > 600 units/mg protein. Storage: -20°C. Form: Lyophilized powder contains Tris buffer salts. Source: Streptococcus faecalis. Ornithine transcarbamylase; EC 2.1.3.3; citrulline phosphorylase; ornithine transcarbamylase; OTC; OTCase; carbamylphosphate-ornithine transcarbamylase; L-ornithine carbamoyltransferase; L-ornithine carbamyltransferase; L-ornithine transcarbamylase; ornithine carbamyltransferase; 9001-69-8. Cat No: NATE-0499.
Native Streptococcus hemolyticus Streptokinase Quick inquiry Where to buy	Streptokinase (SK) is an enzyme secreted by several species of streptococci that can bind and activate human plasminogen. SK is used as an effective and inexpensive thrombolysis medication in some cases of myocardial infarction (heart attack) and pulmonary embolism. Streptokinase belongs to a group of medications known as fibrinolytics, and complexes of streptokinase with human plasminogen can hydrolytically activate other unbound plasminogen by activating through bond cleavage to produce plasmin. Streptokinase from β-hemolytic streptococcus (lancefield group c). Applications: Streptokinase is commonly used as a thrombolytic agent in the therapy of ischemic stroke. this therapy carries the important risk of intracerebral hemorrhage. streptokinase is also used in the treatment of complicated parapneumonic effusions and empyema where adverse reactions, allergic type, are rare. Group: Enzymes. Synonyms: St. Enzyme Commission Number: EC 3.4.99.0. CAS No. 9002-1-1. SK. Activity: > 3,500 units/mg solid. Appearance: Appearance (Color): Conforms to Requirements Off-White to Light Yellow to Light Beige. Form: Lyophilized powder containing ~50% total protein by biuret and sodium glutamate. Total protein composed of enzyme protein and human serum albumin. Source: Streptococcus hemolyticus. Streptokinase; SK; EC 3.4.99.0. Cat No: PHAM-261.
Native Streptococcus pneumoniae α (2?3) Neuraminidase Quick inquiry Where to buy	Neuraminidase enzymes are glycoside hydrolase enzymes (EC 3.2.1.18) that cleave the glycosidic linkages of neuraminic acids. Neuraminidase enzymes are a large family, found in a range of organisms. The best-known neuraminidase is the viral neuraminidase, a drug target for the prevention of the spread of influenza infection. The viral neuraminidases are frequently used as antigenic determinants found on the surface of the Influenza virus. Some variants of the influenza neuraminidase confer more virulence to the virus than others. Other homologs are found in mammalian cells, which have a range of functions. Group: Enzymes. Synonyms: neuraminidase; sialidase; α-neuraminidase; acetylneuraminidase; exo-α-sialidase; EC 3.2.1.18; 9001-67-6. Enzyme Commission Number: EC 3.2.1.18. CAS No. 9001-67-6. Neuraminidase. Storage: 2-8°C. Form: buffered aqueous solution. Solution in 50 mM sodium phosphate, pH 7.5. Source: Streptococcus pneumoniae. neuraminidase; sialidase; α-neuraminidase; acetylneuraminidase; exo-α-sialidase; EC 3.2.1.18; 9001-67-6. Cat No: NATE-0757.
Native Streptococcus pneumoniae β(1-4)-Galactosidase Quick inquiry Where to buy	The enzyme releases non-reducing terminal β(1-4)-linked galactose from oligosaccharides and glycoproteins. This specificity is only evident at enzyme concentrations < 100mU/ml. At higher concentrations, hydrolysis of β(1-3)-linked galactose occurs. Applications: Due to its high selectivity the enzyme is an extremely useful reagent for the identification of non-reducing terminal β(1-4)-linked galactose residues. as such the enzyme has been extensively used for detailed structural analysis in conjunction with broader specificity bovine testes β-galactosidase or jack bean β-galactosidase. Group: Enzymes. Synonyms: β-galactosidase; beta-gal; β-gal; lactase; β-lactosidase; maxilact; hydrolact; β-D-lactosidase; lactozym; trilactase; β-D-galactanase; oryzatym; sumiklat; β-D-galactoside galactohydrolase. β-gal. Mole weight: 220-247 kD. Form: 20 mM Tris-HCl, 25 mM NaCl (pH 7.5). Source: Streptococcus pneumoniae. β(1-4)-Galactosidase; β-galactosidase; beta-gal; β-gal; EC 3.2.1.23; lactase; β-lactosidase; maxilact; hydrolact; β-D-lactosidase; S 2107; lactozym; trilactase; β-D-galactanase; oryzatym; sumiklat; β-D-galactoside galactohydrolase. Cat No: NATE-0974.
Native Streptococcus pyogenes Streptolysin O Quick inquiry Where to buy	Streptolysin O possesses a single polypeptide chain with a molecular weight of f62 kDa. Streptolysin O binds to membrane cholesterol and oligomerizes to create a ring structure that consists of 45 to 50 units. The ring structure inserts into the membrane to make a large pore (25 to 30 nm), which DNA, RNA, peptides and proteins may pass. It is thiol-activated. It is inhibited by allicin, an active component of garlic. Applications: Permeabilizes membranes to permit cellular uptake of large or charged molecules. streptolysin o is a toxin secreted by streptococcus pyogenes and is a prototype member of poreforming bacterial cytolysins. it is used permeabilize cell membranes to permit cellular uptake of large or charged molecules. it is used to study macromolecule delivery. it is a potential anticancer agent and is used to study suicide cancer gene therapy. Group: Enzymes. Synonyms: Streptolysin O; 98072-47-0; SLO. CAS No. 98072-47-0. SLO. Mole weight: 69 kDa. Storage: 2-8°C. Form: lyophilized powder. Source: Streptococcus pyogenes. Streptolysin O; 98072-47-0; SLO. Cat No: NATE-0671.

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