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| Product | Description | |
|---|---|---|
| Native Aspergillus sp. Lysing Enzymes | Native Aspergillus sp. Lysing Enzymes. Group: Enzymes. Synonyms: Lysing Enzymes. Lysing Enzymes. Storage: 2-8°C. Form: powder (brown). Source: Aspergillus sp. Lysing Enzymes. Cat No: NATE-0427. |  |
| Native Bacillus subtilis Xylanase Enzyme (Food Grade) | Xylanase is the name given to a class of enzymes which degrade the linear polysaccharide beta-1,4-xylan into xylose, thus breaking down hemicellulose, one of the major components of plant cell walls. As such, it plays a major role in micro-organisms thriving on plant sources for the degradation of plant matter into usable nutrients. Xylanases are produced by fungi, bacteria, yeast, marine algae, protozoans, snails, crustaceans, insect, seeds, etc., (mammals do not produce xylanases). Xylanase which made from the best strain of bacillus subtilis. it is a kind of purified endo-bacteria-xylanase. it can be applied in the flour treatment for bread powder and steam brea...and chewy. 2) in the storage of bread, the appropriate xylanase can retrad bread staling, improve the water holding capacity of the bread and optimize the gluten network, thereby, preventing water loss and re-allocate, stabilize the organizational structure of the bread. Group: Enzymes. Synonyms: EC 3.2.1.8; endo-(1?4)-β-xylan 4-xylanohydrolase; endo-1,4-xylanase; xylanase; β-1,4-xylanase; endo-1,4-xylanase; endo-β-1,4-xylanase; endo-1,4-β-D-xylanase; 1,4-β-xylan xylanohydrolase; β-xylanase; β-1,4-xylan xylanohydrolase; endo-1,4-β-xylanase; β-D-xylanase; endo-1,4-β-xylanase. Enzyme Commission Number: EC 3.2.1.8. CAS | |
| Native Bacterial Environmental DNA Glucan elongation enzyme | A thermostable 4-α-glucanotransferase that elongates linear alpha-glucan chains in starch and amylose by catalyzing the transfer of one glucose unit from the non-reducing end to a new position in an acceptor, which may be triose or larger. The enzyme can be used various applications, such as for modifications of alpha-polysaccharides and is ideal for making clear size ladders of oligosaccharides larger than maltose. The enzyme was developed from metagenome DNA obtained from environmental sample from a geothermal environment. The enzyme catalyzes the formation of the alpha-1,4-glucosidic linkages. the enzyme transfers a segment of a (1->4)-alpha-d-glucan to a new position in an acceptor, which may be glucose or a (1->4)-alpha-d-glucan. Group: Enzymes. Synonyms: Glucan elongation enzyme. Glucan elongation enzyme. Source: Bacterial Environmental DNA. Glucan elongation enzyme. Cat No: NATE-0302. | |
| Native Baker's yeast (S. cerevisiae) S-Acetyl-coenzyme A synthetase | Acetyl-coenzyme A synthetase catalyzes the production of acetyl-CoA. It is involved in histone acetylation in the nucleus. It may be involved in the growth of nonfermentable carbon sources such as glycerol. Acetyl-coenzyme A synthetase is induced by acetate, acetaldehyde and ethanol. Applications: S-acetyl-coenzyme a synthetase may be used to study various metabolic pathways, such as glycolysis, gluconeogenesis, pyruvate metabolism and co fixation. it may also be used in gene expression studies. Group: Enzymes. Synonyms: acetyl-CoA synthetase; acetyl activating enzyme; acetate thiokinase; acyl-activating enzyme; acetyl coenzyme A synthetase; acetic thiokinase; acetyl CoA ligase; acetyl C. Enzyme Commission Number: EC 6.2.1.1. CAS No. 9012-31-1. ACS. Activity: > 3 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing stabilizers as potassium phosphate, sucrose, and reduced glutathione. Source: Baker's yeast (S. cerevisiae). acetyl-CoA synthetase; acetyl activating enzyme; acetate thiokinase; acyl-activating enzyme; acetyl coenzyme A synthetase; acetic thiokinase; acetyl CoA ligase; acetyl CoA synthase; acetyl-coenzyme A synthase; short chain fatty acyl-CoA synthetase; short-chain acyl-coenzyme A synthetase; ACS; EC 6.2.1.1; 9012-31-1. Pack: Package size based on protein content. Cat No: NATE-0026. | |
| Native Bovine Angiotensin Converting Enzyme | 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; dipept...te buffer-300 mM NaCl, pH 8.3 at 37°C. Storage: Maintain at -20°C in undiluted aliquots for up to 12 months. Maintain at 4°C for up to one month. A decrease in activity may occur within prolonged storage at 4°C. Source: Bovine lung. Species: Bovine. 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 peptidyl dipeptidase; peptidyl dipept | |
| Native E. coli RNA Polymerase, Holoenzyme | E. coli RNA Polymerase, Holoenzyme is the core enzyme saturated with sigma factor 70. The Holoenzyme initiates RNA synthesis from sigma 70 specific bacterial and phage promoters. E. coli RNA Polymerase, Core Enzyme consists of 5 subunits designated α, α, β?, β, and &omega. The enzyme is free of sigma factor and does not recognize any specific bacterial or phage DNA promoters. The enzyme retains the ability to transcribe RNA from nonspecific initiation sequences. Addition of sigma factors will allow the enzyme to initiate RNA synthesis from specific bacterial and phage promoters. Applications: Rna synthesis from e. coli promoter transcription initiation studies in vitro translation with purexpress. Group: Enzymes. Synonyms: E. coli RNA Polymerase, Holoenzyme; E. coli RNA Polymerase; RNA Polymerase; RNAP; RNApol; DNA-dependent RNA polymerase. RNAP. Mole weight: 400 kDa. Storage: at -20°C. Form: 20 mM Tris-HCl, pH 7.5, 100 mM NaCl, 0.1 mM EDTA, 1 mM dithiothreitol (DTT) and 50% glycerol. Source: E. coli. E. coli RNA Polymerase, Holoenzyme; E. coli RNA Polymerase; RNA Polymerase; RNAP; RNApol; DNA-dependent RNA polymerase. Cat No: NATE-1262. | |
| Native Mammalian Ubiquitin Conjugating Enzyme Fractions | Ubiquitin-conjugating enzymes perform the second step in the ubiquitination reaction that targets a protein for degradation via the proteasome. The ubiquitination process covalently attaches ubiquitin, a short protein of 76 amino acids, to a lysine residue on the target protein. Once a protein has been tagged with one ubiquitin molecule, additional rounds of ubiquitination form a polyubiquitin chain that is recognized by the proteasome's 19S regulatory particle, triggering the ATP-dependent unfolding of the target protein that allows passage into the proteasome's 20S core particle, where proteases degrade the target into short peptide fragments for recycling by the cell. Applications: Ubiquitin conjugating enzyme fractions mammalian may be used in transferring the activated ubiquitin from e1 to the substrate through an additional high energy thiol ester intermediate e2-s-ubiquitin. ubiquitin-conjugating enzymes, also known as e2 enzymes and more rarely as ubiquitin-carrier enzymes, perform the second step in the ubiquitination reaction that targets a protein for degradation via the proteasome. Group: Enzymes. Synonyms: Ubiquitin con. Ubiquitin Conjugating Enzyme. Storage: -70°C. Source: Mammalian. Ubiquitin conjugating enzymes; Ubiquitin Conjugating Enzyme Fractions; E2 enzymes; ubiquitin-carrier enzymes. Cat No: NATE-0727. | |
| Native Porcine Angiotensin Converting Enzyme | 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. Ace is a monomer with molecular weight of ~170 kda ph range for activity: 7-8.5 temperature optimum: 37°c zinc is...-82-1. Angiotensin Converting Enzyme. Activity: > 10 units/mg protein (Bradford). Storage: -20°C. Form: Lyophilized powder containing Tris buffer salts. Source: Porcine kidney. Species: Porcine. 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 peptidyl dipeptidase; peptidyl dipeptidase-4; PDH; peptidyl dipeptide hydrolase; DCP. Cat N | |
| Native Pseudomonas sp. Acyl-coenzyme A Synthetase | The Long chain fatty acyl-CoA synthetase enzyme is a member of the ligase family that activates the breakdown of complex fatty acids. Long chain fatty acyl-CoA synthetase plays a crucial role in intermediary metabolism by catalyzing the formation of fatty acyl-CoA by a two-step process proceeding through an adenylated intermediate. It is an enzyme present in all organisms from bacteria to Humans. It catalyzes the pre-step reaction for β-oxidation of fatty acids or can be incorpoRated in phospholipids. Acyl coenzyme A synthetase proteins are involved in regulating and facilitating long-chain fatty acid transport in mammalian cells. Applications: Acyl-coenzyme a synthetase may be used to study fatty acid metabolism and lipid metabolism. it has been used to study its interaction with fatty acid transport proteins, which has been found to be involved in the efficient cellular uptake of long-chain fatty acids in adipocyte. Group: Enzymes. Synonyms: acyl-CoA synthetase; fatty acid thiokinase (long chain); acyl-activating. Enzyme Commission Number: EC 6.2.1.3. CAS No. 9013-18-7. ACS3. Activity: > 2 units/mg protein. Storage: -20°C. Source: Pseudomonas sp. acyl-CoA synthetase; fatty acid thiokinase (long chain); acyl-activating enzyme; palmitoyl-CoA synthase; lignoceroyl-CoA synthase; arachidonyl-CoA synthetase; acyl coenzyme A synt | |
| Native Rabbit Angiotensin Converting Enzyme | 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. Group: Enzymes. Synonyms: ACE; Angiotensin Converting Enzyme; EC 3.4.15.1; dip. Enzyme Commission Number: EC 3.4.15.1. CAS No. 9015-82-1. Angiotensin Converting Enzyme. Activity: > 2.0 units/mg protein (modified Warburg-Christian). Form: lyophilized powder. Source: Rabbit lung. Species: Rabbit. 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 peptidyl dipeptidase; peptidyl dipeptidase-4; PDH; peptidyl dipeptide hydrolase; DCP. Cat No: NATE-0015. | |
| Native Rabbit Pyruvate Kinase/Lactic Dehydrogenase enzymes | 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 Rat Angiotensin Converting Enzyme | 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 Russell's viper venom Factor V Activating Enzyme | 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 Streptococcus faecalis L-Tyrosine Decarboxylase Apoenzyme | 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 Trichoderma harzianum Lysing Enzymes | Native Trichoderma harzianum Lysing Enzymes. Contains β-glucanase, cellulase, protease, and chitinase activities. Applications: Used for yeast spheroplast transformation by hydrolyzing poly (1-3)-glucose of the yeast cell wall glucan. also used to retrieve dna plugs from agarose gels. Group: Enzymes. Synonyms: Lysing Enzymes; Glucanex. Lysing Enzymes. Form: lyophilized powder. Source: Trichoderma harzianum. Lysing Enzymes; Glucanex. Cat No: NATE-0428. | |
| Native Yeast Coenzyme A, Trilithium Salt | Coenzyme A (CoA, CoASH, or HSCoA) is a coenzyme, notable for its role in the synthesis and oxidation of fatty acids, and the oxidation of pyruvate in the citric acid cycle. All genomes sequenced to date encode enzymes that use coenzyme A as a substrate, and around 4% of cellular enzymes use it (or a thioester, such as acetyl-CoA) as a substrate. In humans, CoA biosynthesis requires cysteine, pantothenate, and adenosine triphosphate (ATP). Group: Coenzymes. Synonyms: Coenzyme A, Trilithium Salt; CoA-Li; 18439-24-2. CAS No. 18439-24-2. Purity: Determined by enzyme analysis with PTA* (> 75%) *PTA = Phosphotrasacetylase (LM) (EC 2.3.1.8.). CoA. Mole weight: 685.41. Storage: Keep tightly stoppered in the dark below 5°C. For Prolonged storage, keep below-20°C. Source: Yeast. Coenzyme A, Trilithium Salt; CoA-Li; 18439-24-2. Cat No: NATE-0146. | |
| 2,7-dihydroxy-5-methyl-1-naphthoate 7-O-methyltransferase | The enzyme from the bacterium Streptomyces carzinostaticus is involved in the biosynthesis of 2-hydroxy-7-methoxy-5-methyl-1-naphthoate. This compound is part of the enediyne chromophore of the antitumor antibiotic neocarzinostatin. In vivo the enzyme catalyses the regiospecific methylation at the 7-hydroxy group of its native substrate 2,7-dihydroxy-5-methyl-1-naphthoate. In vitro it also recognizes other dihydroxynaphthoic acids and catalyses their regiospecific O-methylation. Group: Enzymes. Synonyms: NcsB1; neocarzinostatin O-methyltransferase. Enzyme Commission Number: EC 2.1.1.303. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1911; 2,7-dihydroxy-5-methyl-1-naphthoate 7-O-methyltransferase; EC 2.1.1.303; NcsB1; neocarzinostatin O-methyltransferase. Cat No: EXWM-1911. | |
| 5'-Nucleotidase from Human, Recombinant | 5'-nucleotidase is an extracellular enzyme that converts nucleoside-5'-monophosphates to nucleosides with a substrate preference of AMP. Native 5'-nucleotidase is a GPI-anchored protein whose exporession is upregulated by hypoxia. 5'-nucleotidase has many functions in vivo including the generation of extracellular adenosine. 5'-Nucleotidase has various clinical significances. It is a key molecule in the regulation of cancer cells proliferation, migration and invasion in vitro tumor angiogenesis, and tumor immune escape in vivo. Due to this important role, the enzyme is a potential target for cancer research.1 It is also involved in salvage of extracellular nucleotides and...Enzyme Commission Number: EC 3.1.3.5. CAS No. 9027-73-0. Purity: >90% (SDS-PAGE). AMPase. Mole weight: ~61 kDa by SDS-PAGE (reducing). Activity: >15 U/mg. Storage: Store at -70°C. Form: Supplied as a solution containing Tris, NaCl, CaCl2, and 20% glycerol. Source: CHO cells. Species: Human. uridine 5'-nucleotidase; 5'-adenylic phosphatase; adenosine 5'-phosphatase; AMP phosphatase; adenosine monophosphatase; 5'-mononucleotidase; AMPase; UMPase; snake venom 5'-nucleotidase; thimidine monophosphate nucleotidase; 5'-AMPase; 5'-AMP nucleotidase; AMP phosphohydrolase; IMP 5'-nucleotidase; EC 3.1.3.5; CD73; NT5E; ecto-5'-nucleotidase. Pack: vial of 6-12 μg. Cat No: NATE-0795. | |
| acyl-lipid (n+3)-(Z)-desaturase (ferredoxin) | This plastidial enzyme is able to insert a cis double bond in monounsaturated fatty acids incorporated into glycerolipids. The enzyme introduces the new bond at a position 3 carbons away from the existing double bond, towards the methyl end of the fatty acid. The native substrates are oleoyl (18:1 Δ9) and (Z)-hexadec-7-enoyl (16:1 Δ7) groups attached to either position of the glycerol backbone in glycerolipids, resulting in the introduction of the second double bond at positions 12 and 10, respectively This prompted the suggestion that this is an ω6 desaturase. However, when acting on palmitoleoyl groups(16:1 Δ9), the enzyme introduces the second double bond at position 12 (ω4), indicating it is an (n+3) desaturase. cf. EC 1.14.19.34, acyl-lipid (9+3)-(E)-desaturase. Group: Enzymes. Synonyms: acyl-. Enzyme Commission Number: EC 1.14.19.23. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-0986; acyl-lipid (n+3)-(Z)-desaturase (ferredoxin); EC 1.14.19.23; acyl-lipid ω6-desaturase (ferredoxin); oleate desaturase (ambiguous); linoleate synthase (ambiguous); oleoyl-CoA desaturase (ambiguous); oleoylphosphatidylcholine desaturase (ambiguous); phosphatidylcholine desaturase (ambiguous); FAD6 (gene name). Cat No: EXWM-0986. | |
| anthranilate synthase | In some organisms, this enzyme is part of a multifunctional protein, together with one or more other components of the system for the biosynthesis of tryptophan [EC 2.4.2.18 (anthranilate phosphoribosyltransferase ), EC 4.1.1.48 (indole-3-glycerol-phosphate synthase), EC 4.2.1.20 (tryptophan synthase) and EC 5.3.1.24 (phosphoribosylanthranilate isomerase)]. The native enzyme in the complex uses either glutamine or, less efficiently, NH3. The enzyme separated from the complex uses NH3 only. Group: Enzymes. Synonyms: anthranilate synthetase; chorismate lyase; chorismate pyruvate-lyase (amino-accepting); TrpE. Enzyme Commission Number: EC 4.1.3.27. CAS No. 9031-59-8. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4907; anthranilate synthase; EC 4.1.3.27; 9031-59-8; anthranilate synthetase; chorismate lyase; chorismate pyruvate-lyase (amino-accepting); TrpE. Cat No: EXWM-4907. | |
| Carboxypeptidase B from Porcine, Recombinant | Carboxypeptidase B (or peptidyl-L-lysine (-L-arginine) hydrolase) catalyzes the hydrolysis of the basic amino acids, lysine, arginine, and ornithine from the C-terminal position of polypeptides. It has been shown to be a single polypeptide of 34 kDa Da. Trypsin is capable of converting native enzyme to the active enzyme, carboxypeptidase B II in vitro. The optimum pH is found to be 9.0. The enzyme may be used for sequence analysis by successive cleavage of C-terminal basic amino acids. It can also be used as a serum marker for the diagnosis of acute pancreatitis. Carboxypeptidase b (ec 3.4.17.2), also well known as protaminase, pancreatic procarboxy-peptidase b (pcpb), ... mature chain. the secreted cpb zymogen is converted to enzymatically active cpb by limited proteolysis by trypsin. Group: Enzymes. Synonyms: carboxypeptidase B; protaminase; CPB1; pancreatic carboxypeptidase B; tissue carboxypeptidase B; peptidyl-L-lysine [L-arginine]hydrolase; EC 3.4.17.2; 9025-24-5. Enzyme Commission Number: EC 3.4.17.2. Purity: >90% (SDS-PAGE test). Mole weight: About 35kDa (SDS-PAGE detection). Activity: >180U/mg. Appearance: White powder, lyophilized. Storage: Redissolved in 20% glycerol, 4°C, store at -20°C for long-term preservation, Avoid multiple freeze-thaw cycles. Form: Freeze dried powder. Source: Porcine. carboxypeptidase B; protaminase; C | |
| Carboxypeptidase-B from rat, Recombinant | Carboxypeptidase B, recombinant, is intended to use in highly regulated production processes at pharmaceutical companies. Carboxypeptidase B is a widely used metalloprotease, typically isolated from pancreas of different animals, that specifically releases arginine and lysine from the C-terminus of peptides and proteins. Roche has chemically synthesized a gene encoding for the amino acid sequence of the rat Carboxypeptidase B and has transformed the gene into the expression host Pichia pastoris, which expresses the recombinant Carboxypeptidase B as active protease with identical properties compared to the native Carboxypeptidase B. The product is manufactured according to...terial for the production of active pharmaceutical ingredients (api), i.e., insulin. Group: Enzymes. Synonyms: protaminase; pancreatic carboxypeptidase B; tissue carboxypeptidase B; peptidyl-L-lysine [L-arginine] hydrolase. Purity: >85%. CPB1. Activity: >210 U/mg. Stability: At -15 to -25°C within specification range for 24 months. Appearance: Clear, colorless to slightly yellowish solution. Storage: Tris/HCl, 33 mmol/l; ZnCl2, 0.1 mmol/l; pH 7.5-8.5 at +25°C. Source: Pichia pastoris. Species: Rat pancreas. carboxypeptidase B; protaminase; CPB1; pancreatic carboxypeptidase B; tissue carboxypeptidase B; peptidyl-L-lysine [L-arginine]hydrolase; EC 3.4.17.2; 9025-24-5. Cat N | |
| Carboxypeptidase-B rat, Recombinant | Carboxypeptidase B (or peptidyl-L-lysine (-L-arginine) hydrolase) catalyzes the hydrolysis of the basic amino acids, lysine, arginine, and ornithine from the C-terminal position of polypeptides. It has been shown to be a single polypeptide of 34 kDa Da. Trypsin is capable of converting native enzyme to the active enzyme, carboxypeptidase B II in vitro. The optimum pH is found to be 9.0. The enzyme may be used for sequence analysis by successive cleavage of C-terminal basic amino acids. It can also be used as a serum marker for the diagnosis of acute pancreatitis. Caspase 3 is synthesized as a 32 kda proenzyme. the active enzyme is a heterodimer of two large (17 kda) subunit...sponsible for rapidly metabolizing the c5a protein into c5a des-arg, with one less amino acid. Group: Enzymes. Synonyms: carboxypeptidase B; protaminase; CPB1; pancreatic carboxypeptidase B; tissue carboxypeptidase B; peptidyl-L-lysine [L-arginine]hydrolase; EC 3.4.17.2; 9025-24-5. Enzyme Commission Number: EC 3.4.17.2. CAS No. 9025-24-5. CPB1. Activity: 50-55 units/mg protein carboxypeptidase B. Storage: -20°C. Form: Lyophilized from 20 mM Tris, pH 8.0 + 50 mM NaCl. Source: E. coli. Species: Rat. carboxypeptidase B; protaminase; CPB1; pancreatic carboxypeptidase B; tissue carboxypeptidase B; peptidyl-L-lysine [L-arginine]hydrolase; EC 3.4.17.2; 9025-24-5. Cat No: NATE-0153. | |
| Caspase-9 (Active) from Human, Recombinant | The expressed caspase-9 spontaneously undergoes autoprocessing to yield the subunits characteristic of the native enzyme. Active enzyme purified from E. coliThis product is useful in screening caspase inhibitors for pharmaceutical Applications. Group: Enzymes. Synonyms: CASP9; APAF-3; APAF3; ICE-LAP6; MCH6; PPP1R56; Caspase-9 (Active); Caspase-9. Purity: 90% (SDS-PAGE). Caspase 9. Activity: ~400 units/mg. Appearance: Lyophilized Powder. Storage: -80°C. Source: E. coli. Species: Human. CASP9; APAF-3; APAF3; ICE-LAP6; MCH6; PPP1R56; Caspase-9 (Active); Caspase-9. Cat No: NATE-0816. | |
| cathepsin T | Degrades azocasein and denatured hemoglobin; the only native protein on which it has been shown to act is tyrosine aminotransferase. Group: Enzymes. Enzyme Commission Number: EC 3.4.22.24. CAS No. 77464-86-9. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4198; cathepsin T; EC 3.4.22.24; 77464-86-9. Cat No: EXWM-4198. | |
| Chemically modified Cholesterol Oxidase from Brevibacterium species | Oxidoreductase that catalyzes the interconversion of cholesterol to cholest-4-en-3-one. Rely on the proven diagnostic quality of this product. Applications: Use cholesterol oxidase in diagnostic tests for the determination of cholesterol in combination with cholesterol esterase. Group: Enzymes. Synonyms: Cholesterol-O2 oxidoreductase; 3 beta-Hydroxy steroid oxidoreductase; 3β-hydroxysteroid: oxygen oxidoreductase; cholesterol: oxygen oxidoreductase; cholesterol oxidase. CHOD. Mole weight: 60 kD (native and SDS). Activity: 10-20 U/mg lyophilizate. Stability: At -15 to -25°C within specification range for 12 months. Store dry. Protect from light. Appearance: Yellow lyophilizate. Storage: No decrease in activity over 6 weeks at +35°C. Source: Brevibacterium species. Cholesterol-O2 oxidoreductase; 3 beta-Hydroxy steroid oxidoreductase; 3β-hydroxysteroid: oxygen oxidoreductase; cholesterol: oxygen oxidoreductase; cholesterol oxidase; EC 1.1.3.6. Cat No: DIA-284. | |
| Creatine Kinase MB Isoenzyme Type-2 from Human, Recombinant | CK-MB Type II possesses the naturally occurring carboxy-terminal amino acid lysine. This occurs during a myocardial infarct (MI or heart attack) when CK-MB Type II is released from damaged heart muscle, and the C-terminal lysine is cleaved in the blood stream, thus creating CK-MB Type I. This difference can be exploited in diagnosis of an MI. Ckmbitii human recombinant produced in pichia pastoris is a glycosylated polypeptide chain having an identical amino acid sequence compared to the native enzyme, purified under non-denaturing conditions and reacts with polyclonal antibodies to mb isoenzyme in elisa. the ckmbitii is purified by proprietary chromatographic techniques. Group: Enzymes. Synonyms: Creatine Kinase MB Isoenzyme Type-II; Creatine Kinase MB Isoenzyme Type-2; CKMBT2; CKMBITII; CKMBII; CKMB. Purity: Greater than 95.0% as determined by (a) Analysis by RP-HPLC. (b) Analysis by SDS-PAGE. CK. Activity: 892 IU/mg. Stability: CKMBITII although stable at 15°C for 7 days, should be stored below -18°C. Please prevent freeze-thaw cycles. Appearance: Sterile Filtered colourless liquid formulation. Source: Pichia Pastoris. Species: Human. Creatine Kinase MB Isoenzyme Type-II; Creatine Kinase MB Isoenzyme Type-2; CKMBT2; CKMBITII; CKMBII; CKMB. Cat No: NATE-0819. | |
| Creatine Kinase MM Isoenzyme Type-3 from Human, Recombinant | Creatine Kinase MM is a cytoplasmic enzyme involved in energy homeostasis and is an important serum marker for myocardial infarction. The encoded protein reversibly catalyzes the transfer of phosphate between ATP and various phosphogens such as creatine phosphate. It acts as a homodimer in striated muscle as well as in other tissues, and as a heterodimer with a similar brain isozyme in heart. The encoded protein is a member of the ATP:guanido phosphotransferase protein family. Ckmt3 human recombinant produced in pichia pastoris is a glycosylated polypeptide chain having an identical amino acid sequence compared to the native enzyme, purified under non-denaturing conditions and reacts with polyclonal antibodies to mm isoenzyme in elisa.the ckmt3 is purified by proprietary chromatographic techniques. Group: Enzymes. Synonyms: Creatine kin. Enzyme Commission Number: EC 2.7.3.2. Purity: Greater than 95.0% as determined by (a) Analysis by RP-HPLC. (b) Analysis by SDS-PAGE. CK. Activity: 500 IU/mg. Stability: CKMT3 although stable at 15°C for 7 days, should be stored below -18°C. lease prevent freeze-thaw cycles. Appearance: Sterile Filtered colourless liquid formulation. Source: Pichia Pastoris. Species: Human. Creatine kinase M-type; EC 2.7.3.2; Creatine kinase M chain; M-CK; CKM; CKMM; CKMMITIII; CKMMT3. Cat No: NATE-0821. | |
| Dipeptidyl Peptidase IV from Human, Recombinant | Native DPPIV is a ubiquitous type II transmembrane glycoprotein and a serine protease of the S9 prolyl-oligopeptidase family. In vivo, it is synthesized with a signal peptide, which functions as the membrane anchoring domain. There is an 88% sequence homology between the human and porcine kidney enzymes. Both exist as homodimers with a subunit molecular weight of ~30 kDa. The high mannose 100 kDa DPPIV precursor is processed in the Golgi to yield a 124 kDa heavily N-and O-linked mature glycoprotein. It is then sorted to the apical membrane through the concerted action of both N-and O-linked glycans and its association with lipid microdomains. The porcine enzyme contai...zyme from creative enzymes has been used to study the lc-ms (liquid chromatography-mass spectrometry) based assay method for dpp-iv inhibitor screening and substrate discovery. Group: Enzymes. Synonyms: EC 3.4.14.5; 54249-88-6; DPPIV; DPP4; dipeptidyl aminopeptidase IV; Xaa-Pro-dipeptidyl-aminopeptidase; Gly-Pro naphthylamidase; postproline dipeptidyl aminopeptidase IV; lymphocyte antigen CD26; glycoprotein GP110; dipeptidyl peptidase IV; glycylproline aminopeptidase; glycylproline aminopeptidase; X-prolyl dipeptidyl aminopeptidase; pep X; leukocyte antigen CD26; glycylprolyl dipeptidylaminopeptidase; dipeptidyl-peptide hydrolase; glycylprolyl aminopeptidase; dipeptidy | |
| Glycerol-3-phosphate oxidase from Pediococcus sp. | In enzymology, a glycerol-3-phosphate oxidase (EC 1.1.3.21) is an enzyme that catalyzes the chemical reaction: sn-glycerol 3-phosphate + O2 ? glycerone phosphate + H2O2. Thus, the two substrates of this enzyme are sn-glycerol 3-phosphate and O2, whereas its two products are glycerone phosphate and H2O2. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with oxygen as acceptor. This enzyme participates in glycerophospholipid metabolism. It employs one cofactor, FAD. Native glycerol-3-phosphate oxidase (ec 1.1.3.21) was purified from streptococcus sp. Group: Enzymes. Synonyms: glycerol-3-phosphate oxidase; EC 1.1.3.21; sn-glycerol-3-phosphate: oxygen 2-oxidoreductase; glycerol phosphat. Enzyme Commission Number: EC 1.1.3.21. CAS No. 9046-28-0. Activity: 40 U/mg-solid or more (containing approx. 60% of stabilizers). Appearance: Yellowish powder. Storage: Store in tightly closed containers, desiccated, protected from light, at-20°C. Form: Freeze dried powder. Source: Pediococcus sp. glycerol-3-phosphate oxidase; EC 1.1.3.21; sn-glycerol-3-phosphate: oxygen 2-oxidoreductase; glycerol phosphate oxidase; glycerol-1-phosphate oxidase; glycerol phosphate oxidase; L-alpha-glycerophosphate oxidase; alpha-glycerophosphate oxidase; L-alpha-glycerol-3-phosphate oxidase. Cat No: DIA-154. | |
| Granzyme B from Mouse, Recombinant | Granzyme B, a 247 amino acid polypeptide, contains a leader sequence, which is cleaved by a signal peptidase and a two amino acid prodomain, which is cleaved by the lysosomal cysteine protease DPPI. The recombinant granzyme B is expressed in Pichia pastoris as the mature form and appears on SDS-PAGE as a triplet (~34, 32, and 30 kDa) due to three different glycosylations. Granzyme B, a serine protease, is the most prominent granzyme in a family of 11 found in the cytotoxic granules. The granzymes enter the target cell with the assistance of perforin, a critical molecule of the cytotoxic granules. In the target cell, the granzymes act on specific substrates involved with the cell death via apoptosis. > 90% (sds-page), recombinant, expressed in pichia pastoris, buffered aqueous solution. pichia expressed recombinant granzyme b has the advantage over native granzyme b as the latter can be purified only in limited amounts, and over e. coli and vaccinia virus expressed enzymes that failed to generate soluble active enzyme. Group: Enzymes. Synonyms: g. CAS No. 143180-74-9. Granzyme B. Mole weight: 28.9 kDa. Activity: > 10,000 units/mg protein. Storage: -70°C. Form: buffered aqueous solution. Source: Pichia pastoris. Species: Mouse. granzyme B; CTLA1; CCPII; cytotoxic cell proteinase-1; granzyme G; granzyme H; CCP1 proteinase; GzmB. Cat No: NATE-0333. | |
| Heparinase I | This enzyme selectively cleaves highly sulfated polysaccharide chains containing 1-4 linkages between N-sulfated glucaoamine and 2-O-sulfated iduronic acid. It cleaves heparin sulfate but only to a limited extent in the sulfated zone. It also cleaves the antithrombin III pentasaccharide unit in the heparin molecule. Optimum pH 7.0-7.6. Stabilised with 0.2-0.4% BSA, 0.22 μm sterile filtered and dispensed into sterile tubes/vials. Synonyms: Native Flavobacterium Heparinum Heparinase I; EC 4.2.2.7; Heparinase I; Heparin Eliminase; Heparinase; Heparin Lyase; Heparinase I From Bacteroides Eggerthii, Recombinant. Grades: 95%. CAS No. 9025-39-2. Mole weight: 42.8 kDa. |  |
| Immobilized human plasmin | We have immobilized human Lys plasmin on agarose resin by coupling of primary amines. Plasmin retains catalytic activity when coupled and may be used to efficiently activate single-chain tPA and uPA to the two-chain form. It may also be used to convert plasminogen from its native Glu form to the Lys form by removing the first 77 amino acids. Group: Enzymes. Synonyms: fibrinase; fibrinolysin; actase; serum tryptase; thrombolysin; plasmin; EC 3. 4. 21. 7; 9001-90-5; PLG. Enzyme Commission Number: EC 3. 4. 21. 7. Purity: >95% by SDS-PAGE analysis. Mole weight: 85000. Stability: 12 months from delivery. Storage: 4°C. Form: Resin. Source: Human plasma. Species: Human. fibrinase; fibrinolysin; actase; serum tryptase; thrombolysin; plasmin; EC 3. 4. 21. 7; 9001-90-5; PLG; Immobilized plasmin. Cat No: NATE-1757. | |
| Immobilized Proteinase K on G3m | Proteinase K is an unspecific serine protease with strong proteolytic activity on denatured (in SDS) and high molecular weight native proteins. It cleaves peptide bonds mostly after the carboxyl group of N-substituted hydrophobic, aliphatic and aromatic amino acids. G3m: 25 ug proteinase K immobilized on matrix G3m per CR-column. 0.7 mAnson units immobilized per CR-column. This CR-column cuts at least 370 ug BSA per application. Nr. 5 Storage buffer: 50 mM Tris/HCl, pH 7. 5Nr. 16 Reaction buffer: 50 mM Tris/HCl, 5 mM NaCl, pH 8. 0Nr. 17 Washing buffer: 50 mM Tris/HCl, 1. 0 M NaCl, pH 8. 0The columns are more active in 0.1% SDS and at 40°C. Also active in PBS buffer (20 mM Na-phosphate, 150 mM NaCl at pH 7. 6). Group: Enzymes. Synonyms: Tritirachium alkaline proteinase; Tritirachium album serine proteinase; proteinase K; Tritirachium album proteinase K; endopeptidase K; EC 3. 4. 21. 64; 39450-01-6. Enzyme Commission Number: EC 3. 4. 21. 64. Purity: Chromatographically purified, free of ribo- and deoxyribonucleases. Storage: 4 °C. Source: Tritirachium album. Tritirachium alkaline proteinase; Tritirachium album serine proteinase; proteinase K; Tritirachium album proteinase K; endopeptidase K; EC 3. 4. 21. 64; 39450-01-6; Immobilized Proteinase K. Cat No: NATE-1768. | |
| microbial collagenase | Six species of metalloendopeptidase acting on native collagen can be isolated from the medium of Clostridium histolyticum. Class I has forms α (68 kDa), β (115 kDa) and γ (79 kDa); class II has Δ (100 kDa), ε (110 kDa) and ζ (125 kDa). The two classes are immunologically crossreactive, but have significantly different sequences, and different specificities such that their actions on collagen are complementary. The enzymes also act as peptidyl-tripeptidases. Variants of the enzyme have been purified from Bacillus cereus, Empedobacter collagenolyticum, Pseudomonas marinoglutinosa, and species of Vibrio, Vibrio B-30 (ATCC 21250) and V. alginolyticu...ase-8; matirx metalloproteinase-18; interstitial collagenase. Enzyme Commission Number: EC 3.4.24.3. CAS No. 9001-12-1. Collagenase. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4311; microbial collagenase; EC 3.4.24.3; 9001-12-1; Clostridium histolyticum collagenase; clostridiopeptidase A; collagenase A; collagenase I; Achromobacter iophagus collagenase; collagenase; aspergillopeptidase C; nucleolysin; azocollase; metallocollagenase; soycollagestin; Clostridium histolyticum proteinase A; clostridiopeptidase II; MMP-8; clostridiopeptidase I; collagen peptidase; collagen protease; collagenase MM | |
| Native Aerococcuss viridans Lactate Oxidase | Native Aerococcuss viridans Lactate Oxidase. Native lactate oxidase (ec 1.13.12.4) was purified from aerococcuss viridans. Group: Enzymes. Synonyms: lactate 2-monooxygenase; EC 1.13.12.4; (S)-lactate: oxygen 2-oxidoreductase (decarboxylating); lactate oxidative decarboxylase; lactate oxidase; lactic oxygenase; lactate oxygenase; lactic oxidase; L-lactate monooxygenase; lactate monooxygenase; L-lactate-2-monooxygenase. Enzyme Commission Number: EC 1.13.12.4. CAS No. 9028-72-2. Lactate oxidase. Activity: > 20 U/mg. Appearance: Yellowish powder. Storage: Store in tightly closed containers, desiccated, protected from light, at-20°C. Form: Freeze dried powder. Source: Aerococcuss viridans. lactate 2-monooxygenase; EC 1.13.12.4; (S)-lactate: oxygen 2-oxidoreductase (decarboxylating); lactate oxidative decarboxylase; lactate oxidase; lactic oxygenase; lactate oxygenase; lactic oxidase; L-lactate monooxygenase; lactate monooxygenase; L-lactate-2-monooxygenase. Cat No: DIA-156. | |
| Native Aerococcuss viridans Pyruvate oxidase | In enzymology, a pyruvate oxidase (EC 1.2.3.3) is an enzyme that catalyzes the chemical reaction: pyruvate + phosphate + O2 <-> acetyl phosphate + CO2 + H2O2. The 3 substrates of this enzyme are pyruvate, phosphate, and O2, whereas its 3 products are acetyl phosphate, CO2, and H2O2. Native pyruvate oxidase (ec 1.2.3.3) was purified from aerococcuss viridans. Applications: Useful for enzymatic determination of ast and alt. Group: Enzymes. Synonyms: pyruvate oxidase; EC 1.2.3.3; pyruvate: oxygen 2-oxidoreductase (phosphorylating); pyruvic oxidase; phosphate-dependent pyruvate oxidase. Enzyme Commission Number: EC 1.2.3.3. CAS No. 9001-96-1. Pyruvate oxidase. Activity: > 25 U/mg. Appearance: Yellowish powder. Storage: Store in tightly closed containers, desiccated, protected from light, at-20°C. Form: Freeze dried powder. Source: Aerococcuss viridans. pyruvate oxidase; EC 1.2.3.3; pyruvate: oxygen 2-oxidoreductase (phosphorylating); pyruvic oxidase; phosphate-dependent pyruvate oxidase. Cat No: DIA-169. | |
| Native Alginate Lyase | In enzymology, a poly (beta-D-mannuronate) lyase (EC 4.2.2.3) is an enzyme that catalyzes the chemical reaction:Eliminative cleavage of polysaccharides containing beta-D-mannuronate residues to give oligosaccharides with 4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl groups at their ends. This enzyme belongs to the family of lyases, specifically those carbon-oxygen lyases acting on polysaccharides. This enzyme participates in fructose and mannose metabolism. Applications: Alginate lyase is used to break down alginate or alginic acid and to reduce viscosity. it is useful during follicle isolation, encapsulation, and culture. Group: Enzymes. Synonyms: alginate lyase I; alginate lyase; alginase I; alginase II; alginase; poly (β-D-1,4-mannuronide) lyase; EC 4.2.2.3; 9024-15-1. Enzyme Commission Number: EC 4.2.2.3. CAS No. 9024-15-1. Alginate lyase. Activity: > 10,000 units/g solid. Storage: 2-8°C. Form: powder. alginate lyase I; alginate lyase; alginase I; alginase II; alginase; poly (β-D-1,4-mannuronide) lyase; EC 4.2.2.3; 40591-57-9. Cat No: NATE-0050. | |
| Native α-lytic protease | Alpha-lytic protease (aLP) is an alternative specificity protease for proteomics applications. This protease cleaves after T, A, S, and V residues. It geneRates peptides of similar average length as trypsin. aLP was first isolated from the myxobacterium Lysobacter enzymogenes. The pro-form of aLP is 397 amino acids long. In its mature form, aLP is 198 amino acids long. Its tertiary structural core resembles those of pancreatic serine proteases. Group: Enzymes. Synonyms: Alpha-lytic protease; myxobacter α-lytic proteinase; α-lytic proteinase; α-lytic protease; Mycobacterium sorangium α-lytic proteinase; Myxobacter 495 α-lytic proteinase; Alp. α-LP. Storage: -70°C. Form: Supplied as a solution in 10 mM sodium acetate buffer, pH 5.0. Alpha-lytic protease; myxobacter α-lytic proteinase; α-lytic proteinase; α-lytic protease; Mycobacterium sorangium α-lytic proteinase; Myxobacter 495 α-lytic proteinase; Alp. Cat No: NATE-0052. | |
| Native Arthrobacter globiformis Choline oxidase | In enzymology, a choline oxidase (EC 1.1.3.17) is an enzyme that catalyzes the chemical reaction choline + O2<-> betaine aldehyde + H2O2. Thus, the two substrates of this enzyme are choline and O2, whereas its two products are betaine aldehyde and H2O2. Native choline oxidase (ec 1.1.3.17) was purified from arthrobacter globiformis. Group: Enzymes. Synonyms: choline oxidase; EC 1.1.3.17; choline: oxygen 1-oxidoreductase. Enzyme Commission Number: EC 1.1.3.17. CAS No. 9028-67-5. Choline Oxidase. Activity: 8-20 U/mg. Appearance: Yellow amorphous powder. Storage: Store in tightly closed containers, desiccated, protected from light, at-20°C. Form: Freeze dried powder. Source: Arthrobacter globiformis. choline oxidase; EC 1.1.3.17; choline: oxygen 1-oxidoreductase. Cat No: DIA-139. | |
| Native Arthrobacter luteus Zymolyase | Native Arthrobacter luteus Zymolyase. Group: Enzymes. Synonyms: Zymolyase. Zymolyase. Activity: 20U/mg. Stability: Stable for one year at 4°C. Storage: -20°C. Form: Lyophilized powder. Source: Arthrobacter luteus. Zymolyase. Cat No: NATE-0739. | |
| Native Arthrobacter sp. acyl-CoA oxidase | In enzymology, an acyl-CoA oxidase (EC 1.3.3.6) is an enzyme that catalyzes the chemical reaction acyl-CoA + O2<-> trans-2, 3-dehydroacyl-CoA + H2O2. Thus, the two substrates of this enzyme are acyl-CoA and O2, whereas its two products are trans-2, 3-dehydroacyl-CoA and H2O2. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-CH group of donor with oxygen as acceptor. This enzyme participates in 3 metabolic pathways: fatty acid metabolism, polyunsaturated fatty acid biosynthesis, and ppar signaling pathway. It employs one cofactor, FAD. Native acyl-coa oxidase (ec 1.3.3.6) was purified from arthrobacter sp. Group: Enzymes. Synonyms: acyl-CoA oxidase; EC 1.3.3.6; fatty acyl-CoA oxidase; acyl coenzyme A oxidase; and fatty acyl-coenzyme A oxidase. Enzyme Commission Number: EC 1.3.3.6. CAS No. 61116-22-1. Acyl-CoA oxidase. Activity: > 20 U/mg. Storage: Store in tightly closed containers, desiccated, protected from light, at-20°C. Form: Yellowish Freeze dried powder. Source: Arthrobacter sp. acyl-CoA oxidase; EC 1.3.3.6; fatty acyl-CoA oxidase; acyl coenzyme A oxidase; and fatty acyl-coenzyme A oxidase. Cat No: DIA-121. | |
| Native Arthrobacter sp. Tyramine Oxidase | Amine oxidases (AO) are enzymes that catalyze the oxidation of a wide range of biogenic amines including many neurotransmitters, histamine and xenobiotic amines. There are two classes of amine oxidases: flavin-containing (EC 1.4.3.4) and copper-containing (EC 1.4.3.6). Copper-containing AO act as a disulphide-linked homodimer. They catalyse the oxidation of primary amines to aldehydes, with the subsequent release of ammonia and hydrogen peroxide, which requires one copper ion per subunit and topaquinone as cofactor: RCH2NH2 + H2O + O2 <-> RCHO + NH3 + H2O2. The 3 substrates of this enzyme are primary amines (RCH2NH2), H2O, and O2, whereas its 3 products are RCHO, NH3, and H2O2. Native tyramine oxidase (ec 1.4.3.4) was purified from arthrobacter sp. Applications: Useful for enzymatic determiantion of leucine aminopeptidase. Group: Enzymes. Synonyms: Tyramine Oxidase; TOD; EC 1.4.3.6. Enzyme Commission Number: EC 1.4.3.6. CAS No. 9001-53-0. Tyramine Oxidase. Activity: > 3 U/mg. Appearance: White to light brown powder. Storage: Store in tightly closed containers, desiccated, protected from light, at-20°C. Form: Freeze dried powder. Source: Arthrobacter sp. Tyramine Oxidase; TOD; EC 1.4.3.6. Cat No: DIA-158. | |
| Native Aspergillus japonicus Pectolyase | Pectolyase catalyzes the eliminative cleavage of a-(1-4)-Dgalacturonan methyl ester to give oligosaccharides with 4-deoxy-6-O-methyl-a-D-galact-4-enuronosyl groups at their non-reducing ends. It contain two types of pectinase, endopolygalacturonase, endo-pectin lyase and a maceration stimulating factora. Applications: Used in plant protoplast preparation to digest cell wall prior to organelle isolation. pectolyase p5936 (pel1) is a natural mixed pectolyase produced by the fungus aspergillus japonicus used to digest components (endopolygalacturonate and pectin) of plant cell walls. treatment of cell walls with pectolyase can be used to destablilize the cell walls for organelle isolation or to modify the elasticity of the cell walls. Group: Enzymes. Synonyms: polygalacturonase; pectin depolymerase; pectinase; endopolygalacturonase; pectolase;. Enzyme Commission Number: EC 3.2.1.15. CAS No. 9033-35-6. Pectinase. Activity: > 0.3 units/mg solid. Storage: -20°C. Form: lyophilized powder. Source: Aspergillus japonicus. polygalacturonase; pectin depolymerase; pectinase; 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; EC 3.2.1.15; PEL1. Cat No: NATE-0540. | |
| Native Bacillus cereus Phospholipase C | Phospholipase C is an enzyme with system name phosphatidylcholine cholinephosphohydrolase. This enzyme catalyses the following chemical reaction: a phosphatidylcholine + H2O<-> 1, 2-diacyl-sn-glycerol + phosphocholine. The bacterial enzyme is a zinc protein. It also acts on sphingomyelin and phosphatidylinositol. Native phospholipase c (ec 3.1.4.3) was purified from bacillus cereus. Applications: Useful for enzymatic determination of lecithin. Group: Enzymes. Synonyms: Phospholipase C; EC 3.1.4.3; lipophosphodiesterase I; Clostridium welchii alpha-toxin; Clostridium oedematiens beta-and gamma-toxins; lipophosphodiesterase C; phosphatidase C; heat-labile hemolysin; alpha-toxin. Enzyme Commission Number: EC 3.1.4.3. CAS No. 9001-86-9. Phospholipase C. Activity: > 30 U/mg. Appearance: White to brownish powder. Storage: Store in tightly closed containers, desiccated, protected from light, at-20°C. Form: Freeze dried powder. Source: Bacillus cereus. Phospholipase C; EC 3.1.4.3; lipophosphodiesterase I; Clostridium welchii alpha-toxin; Clostridium oedematiens beta-and gamma-toxins; lipophosphodiesterase C; phosphatidase C; heat-labile hemolysin; alpha-toxin. Cat No: DIA-163. | |
| Native Bacillus licheniformis Alkaline Protease | Proteinase catabolizes proteins by hydrolysis of peptide bonds. Proteases are inactivated by serine active-site inhibitors, such as phenylmethylsulfonyl fluoride (PMSF) and diisopropylfluorophosphate. Subtilisin a is a member of the serine s8 endoproteinase family. it has broad specificity with a preference for a large uncharged residue in the p1 position. it hydrolyzes native and denatured proteins, and is active under alkaline conditions. Applications: The enzyme has been used to optimize release of all mitochondrial populations from homogenized ventricular tissue of rat heart.1 it has also been used in the pre-hybridisation treatment of formalin fixed, paraffin wax...ex); MCP; proteasome; large multicatalytic protease; multicatalytic proteinase; proteasome organelle; alkaline protease; 26S protease; triCorn proteinase; triCorn protease; EC 3.4.25.1. Enzyme Commission Number: EC 3.4.25.1. CAS No. 140879-24-9. Alkaline Protease. Mole weight: 27 Kda. Activity: 7.0-14.0 units/mg. Form: lyophilized powder. Source: Bacillus licheniformis. ingensin; macropain; multicatalytic endopeptidase complex; prosome; multicatalytic proteinase (complex); MCP; proteasome; large multicatalytic protease; multicatalytic proteinase; proteasome organelle; alkaline protease; 26S protease; triCorn proteinase; triCorn protease; EC 3.4.25.1. Cat No: NATE-0444. | |
| Native Bacillus licheniformis Protease | Protease catabolizes proteins by hydrolysis of peptide bonds. Proteases are inactivated by serine active-site inhibitors, such as phenylmethylsulfonyl fluoride (PMSF) and diisopropylfluorophosphate. Protease is a serine endoproteinase with a broad specificity towards native and denatured proteins, and is active under alkaline conditions. It is active in some organic solvents such as dry octane. The enzyme is found to be stable at ph 8-10, retaining activity of up to 90% for 24 hours. it shows maximum activity at temperatures between 55-60°c. Applications: The product has been used with other enzymes for in situ proteolysis to produce crystals suitable for structure determi...f bacillus licheniformis. it is a serine endoproteinase with a broad specificity towards native and denatured proteins, and is active under alkaline conditions. Group: Enzymes. Synonyms: Protease; 9014-01-1; Subtilisin A; EC 3.4.21.62; Alcalase. Enzyme Commission Number: EC 3.4.21.62. CAS No. 9001-92-7. Protease. Mole weight: Subtilisin is a non-glycosylated single polypeptide chain without disulfide bonds and has a molecular weight of 27 KDa. Activity: Type VIII, 7-15 units/mg solid; Type I, > 2.4 U/g. Form: Type VIII, lyophilized powder; Type I, aqueous solution. Source: Bacillus licheniformis. Protease; 9014-01-1; Subtilisin A; EC 3.4.21.62; Alcalase. Cat No: NATE-0633. | |
| Native Bacillus megaterium Diaphorase (NADH) | In enzymology, a NADPH dehydrogenase is an enzyme that catalyzes In enzymology, a NAD (P)H dehydrogenase (quinone) (EC 1.6.5.2) is an enzyme that catalyzes the chemical reaction NAD (P)H + H+ + a quinone<-> NAD (P)+ + a hydroquinone. The 4 substrates of this enzyme are NADH, NADPH, H+, and quinone, whereas its 3 products are NAD+, NADP+, and hydroquinone. Native diaphorase (ec 1.6.5.2) was purified from bacillus megaterium. Applications: Useful for enzymatic determination of reduced nad. Group: Enzymes. Synonyms: EC 1.6.99.3; cytochrome c reductase; type 1 dehydrogenase; beta-NADH dehydrogenase dinucleotide; diaphorase; dihydrocodehydr. Enzyme Commission Number: EC 1.6.99.3. CAS No. 9079-67-8. Diaphorase. Activity: 30-60 U/mg. Appearance: Yellow dried powder. Storage: Store in tightly closed containers, desiccated, protected from light, at-20°C. Form: Freeze dried powder. Source: Bacillus megaterium. EC 1.6.99.3; cytochrome c reductase; type 1 dehydrogenase; beta-NADH dehydrogenase dinucleotide; diaphorase; dihydrocodehydrogenase I dehydrogenase; dihydronicotinamide adenine dinucleotide dehydrogenase; diphosphopyridine diaphorase; DPNH diaphorase; NADH diaphorase; NADH hydrogenase; NADH oxidoreductase; NADH-menadione oxidoreductase; reduced diphosphopyridine nucleotide diaphorase; Beta-NADH dehydrogenase dinucleotide. Cat No: DIA-142. | |
| Native Bacillus sp. Glucose-6-phosphate dehydrogenase | Glucose-6-phosphate dehydrogenase (G6PD or G6PDH) (EC 1.1.1.49) is a cytosolic enzyme that catalyzes the chemical reaction:D-glucose 6-phosphate + NADP+ <-> 6-phospho-D-glucono-1,5-lactone + NADPH + H+. This enzyme is in the pentose phosphate pathway, a metabolic pathway that supplies reducing energy to cells (such as erythrocytes) by maintaining the level of the co-enzyme nicotinamide adenine dinucleotide phosphate (NADPH). Native glucose-6-phosphate dehydrogenase (ec 1.1.1.49) was purified from bacillus sp. Applications: Useful for enzymatic determination of glucose or atp when coupled with hexokinase. Group: Enzymes. Synonyms: Glucose-6-phosphate dehydrogenase; G6PD; G6PDH; Glucose-6-phosphate dehydrogenase (NADP(+)); EC 1.1.1.49; Glucose-6-phosphate 1-dehydrogenase; Glucose-6-phosph. Enzyme Commission Number: EC 1.1.1.49. CAS No. 9001-40-5. Glucose-6-phosphate dehydrogenase. Mole weight: 104 kDa dalton (two subunits of approx. 55 kDa). Activity: > 200 U/mg. Appearance: White/off white powder. Storage: Store in tightly closed containers, desiccated, protected from light, at-20°C. Form: Freeze dried powder. Source: Bacillus sp. Glucose-6-phosphate dehydrogenase; G6PD; G6PDH; Glucose-6-phosphate dehydrogenase (NADP(+)); EC 1.1.1.49; Glucose-6-phosphate 1-dehydrogenase; Glucose-6-phosphate dehydrogenase; GPD. Cat No: DIA-143. | |
| Native Bacillus sp. Glutamine synthetase | Glutamine synthetase (GS) (EC 6.3.1.2) is an enzyme that plays an essential role in the metabolism of nitrogen by catalyzing the condensation of glutamate and ammonia to form glutamine: Glutamate + ATP + NH3 ? Glutamine + ADP + phosphate. Glutamine Synthetase uses ammonia produced by nitrate reduction, amino acid degradation, and photorespiration. The amide group of glutamate is a nitrogen source for the synthesis of glutamine pathway metabolites. Native glutamine synthetase (ec 6.3.1.2) was purified from bacillus sp. Applications: Useful for the determination of ammonia and atp in clinical analysis. Group: Enzymes. Synonyms: Glutamine synthetase; GS; EC 6.3.1.2; Glutamate-ammonia ligase. Enzyme Commission Number: EC 6.3.1.2. CAS No. 9023-70-5. GS. Activity: > 15 U/mg. Appearance: White to pale brown powder. Storage: Store in tightly closed containers, desiccated, protected from light, at-20°C. Form: Freeze dried powder. Source: Bacillus sp. Glutamine synthetase; GS; EC 6.3.1.2; Glutamate-ammonia ligase. Cat No: DIA-155. | |
| Native Bacillus stearothermophilus Phosphoglucose isomerase | Glucose-6-phosphate isomerase is an enzyme that catalyzes the conversion of glucose-6-phosphate into fructose 6-phosphate in the second step of glycolysis. The human variant of this enzyme is encoded by the GPI gene. Native glucose-6-phosphate isomerase (ec 5.3.1.9) was purified from bacillus stearothermophilus. Group: Enzymes. Synonyms: Glucose-6-phosphate isomerase; phosphoglucose isomerase; phosphohexose isomerase; EC 5.3.1.9; phosphohexomutase; oxoisomerase; hexosephosphate isomerase; phosphosaccharomutase; phosphoglucoisomerase; phosphohexoisomerase; glucose phosphate isomerase; hexose phosphate isomerase; D-glucose-6-phosphate ketol-isomerase. Enzyme Commission Number: EC 5.3.1.9. CAS No. 9001-41-6. PGI. Activity: > 250 U/mg. Appearance: White powder. Storage: Store in tightly closed containers, desiccated, protected from light, at-20°C. Form: Freeze dried powder. Source: Bacillus stearothermophilus. Glucose-6-phosphate isomerase; phosphoglucose isomerase; phosphohexose isomerase; EC 5.3.1.9; phosphohexomutase; oxoisomerase; hexosephosphate isomerase; phosphosaccharomutase; phosphoglucoisomerase; phosphohexoisomerase; glucose phosphate isomerase; hexose phosphate isomerase; D-glucose-6-phosphate ketol-isomerase. Cat No: DIA-162. | |
| Native Bacillus subtilis Bilirubin oxidase | In enzymology, a bilirubin oxidase (EC 1.3.3.5) is an enzyme that catalyzes the chemical reaction 2 bilirubin + O2<-> 2 biliverdin + 2 H2O. Thus, the two substrates of this enzyme are bilirubin and O2, whereas its two products are biliverdin and H2O. This enzyme belongs to the family of oxidoreductases, to be specific those acting on the CH-CH group of donor with oxygen as acceptor. This enzyme participates in porphyrin and chlorophyll metabolism. Native bilirubin oxidase (ec 1.3.3.5) was purified from bacillus subtilis. Applications: Useful for enzymatic determination of bilirubin and for eliminating the interference of bilirubin in diagnostic assays. Group: Enzymes. Synonyms: bilirubin oxidase M-1; bilirubin oxidase; EC 1.3.3.5; bilirubin: oxygen oxidoreductase. Enzyme Commission Number: EC 1.3.3.5. CAS No. 80619-01-8. Bilirubin Oxidase. Activity: > 1.2 U/mg. Storage: Store in tightly closed containers, desiccated, protected from light, at-20°C. Form: Freeze dried powder. Source: Bacillus subtilis. bilirubin oxidase M-1; bilirubin oxidase; EC 1.3.3.5; bilirubin: oxygen oxidoreductase. Cat No: DIA-129. | |
| Native Bacillus subtilis Diacetinase | Native Bacillus subtilis Diacetinase. Applications: Used in the formulation of lipase testing reagents. Group: Enzymes. Synonyms: Diacetinase; EC 3.1.1-. Enzyme Commission Number: E.C.3.1.1-. Diacetinase. Activity: 0.228 U/mg-0.633 U/mg liquid. Appearance: Colourless to Yellowish solution. Form: Liquid. Source: Bacillus subtilis. Diacetinase; EC 3.1.1-. Cat No: NATE-0187. | |
| Native Bovine β(1-3,4)-Galactosidase | Hydrolyzes non-reducing terminal galactose β(1-3) and β(1-4) linkages. Can be used in conjunction with other β-galactosidases for exoglycosidase sequencing. Applications: The enzyme has applications in the analysis of a wide variety of glycoconjugates. it is particularly useful for ensuring the complete removal of β(1-3) and β(1-4)-linked non-reducing terminal galactose residues of oligosaccharides. gal β(1-6) glcnac is hydrolyzed more slowly, however this linkage is not normally encountered in native complex glycans. this activity towards β(1-3) and β(1-4)-linked galactose contrasts with that of our other β-galactosidases whi...tose residues. 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: ~68 kD. Form: 20 mM sodium Citrate phosphate, 150 mM NaCl (pH 4.0). Source: Bovine testis. Species: Bovine. β(1-3,4)-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-0973. | |
| Native Bovine Deoxyribonuclease II | Deoxyribonuclease II, also called as acid DNAse, hydrolyzes deoxyribonucleotide linkages in native and denatured DNA yielding products with 3'-phosphates. In vitro, its optimum pH range is 4.5-5.0. It also acts upon p-nitrophenyl-phosphodiesters at pH 5.6-5.9. The molecular weight is approximately 38 kDa Da. Applications: Dnase ii from creative enzymes has been used in the dissociation medium during the preparation of embryonic cardiac myocytes from rat heart. deoxyribonuclease ii from bovine spleen has been used in a study that conducted a partial purification of deoxyribonucleases from eggs and liver of xenopus laevis. deoxyribonuclease ii from bovine spleen has also been used in a study to investigate nucleic acid and protein synthesis of splenic lymphocytes. Group: Enzymes. Synonyms: DNASE2; deoxyribonuclease II; EC 3.1.22.1; 9025-64-3; DNase II; pancreatic DNase II; deoxyribonucleate 3'-nucleotidohydrolase; DNase II; pancreati. Enzyme Commission Number: EC 3.1.22.1. CAS No. 9025-64-3. DNASE2. Activity: > 1,000 units/mg protein. Storage: -20°C. Form: essentially salt-free, lyophilized powder. Source: Bovine spleen. Species: Bovine. DNASE2; deoxyribonuclease II; EC 3.1.22.1; 9025-64-3; DNase II; pancreatic DNase II; deoxyribonucleate 3'-nucleotidohydrolase; DNase II; pancreatic DNase II; acid deoxyribonuclease; acid Dnase. Cat No: NATE-0201. | |
| Native Bovine Lactoperoxidase | Lactoperoxidase catalyzes the oxidation of iodide to iodine by hydrogen peroxide. This activity provides a gentle, specific alternative to chloramine T for the radioiodination of proteins and DNA. Group: Enzymes. Synonyms: lactoperoxidase; guaiacol peroxidase; plant peroxidase; Japanese radish peroxidase; horseradish peroxidase (HRP); soybean peroxidase (SBP); extensin peroxidase; heme peroxidase; oxyperoxidase; protoheme peroxidase; pyrocatechol peroxidase; scopoletin peroxidase; Coprinus cinereus peroxidase; Arthromyces ramosus peroxidase; EC 1.11. Enzyme Commission Number: EC 1.11.1.7. CAS No. 9003-99-0. Peroxidase. Activity: Type I, > 50 units/mg protein; Type II, > 150 units/mg; Type III, > 200 units/mg protein; Type IV, > 80 units/mg protein. Storage: -20°C. Form: Type I, ammonium sulfate suspension, Suspension in 3.2 M (NH4)2SO4 pH approx. 7.0; Type II, Type IV, lyophilized powder; Type III, lyophilized powder (essentially salt-free). Source: Bovine milk. Species: Bovine. lactoperoxidase; guaiacol peroxidase; plant peroxidase; Japanese radish peroxidase; horseradish peroxidase (HRP); soybean peroxidase (SBP); extensin peroxidase; heme peroxidase; oxyperoxidase; protoheme peroxidase; pyrocatechol peroxidase; scopoletin peroxidase; Coprinus cinereus peroxidase; Arthromyces ramosus peroxidase; EC 1.11.1.7; 9003-99-0; LPO; SPO. Cat No: NATE-0418. | |
| Native Bovine Mucopolysaccharidase | Native Bovine Mucopolysaccharidase. Creative enzymes, is a leading producer of high potency hyaluronidase and mucopolysaccharidase and supplies the diagnostics industry. we extract hyaluronidase and mucopolysaccharidase from either bovine or ovine testes using multiple precipitation, fractionation, and filtration steps. creative enzymes products are not intended for use in pharmaceutical applications. Applications: In anti-cellulite preparations / promotion of topical drug absorption / local anesthesia / dispersion and dissipation of fluids and edema /in tissue and cell dissociation. Group: Enzymes. Synonyms: Mucopolysaccharidase; 37326-33-3; Hyaluronate 4-glycanohydrolase. CAS No. 9031-30-5. Mucopolysaccharidase. Activity: > 40 U/mg. Storage: Store at <-15°C. Form: A freeze-dried material. Source: Bovine testes. Species: Bovine. Mucopolysaccharidase; 37326-33-3; Hyaluronate 4-glycanohydrolase. Cat No: NATE-0463. | |
| Native Bovine Phosphodiesterase II | Phosphodiesterase (PDE) is any enzyme that is used to breaks phosphodiester bonds. The enzyme acts on poly (A), poly (U), and poly (I). Native DNA and poly (C) are quite resistant to the action of this enzyme. Hydrolyzes RNA, RNA-Core, 3'-alkyl-and 3'-aryl-nucleoside phosphates, and polydeoxyribonucleotides with 3'-phosphate end groups to 3'-mononucleotides. Polynucleotides having 5'-phosphomonoester end groups are not attacked. Applications: Phosphodiesterase (pde) is any enzyme that is used to breaks phosphodiester bonds. it is a membrane-bound glycoprotein that is used to catalyze the hydrolysis of various nucleotide polyphosphates. phosphodiesterase ii has been used in t...yloxobutyl (pob) base adducts from dna. furthermore, it has been used along with micr oc occal endonuclease to hydrolyze purified dna to 3-nucleoside monophosphates. Group: Enzymes. Synonyms: 3'-exonuclease; spleen phosphodiesterase; 3'-nucleotide phosphodiesterase; phosphodiesterase II; spleen exonuclease; EC 3.1.16.1; 9068-54-6; PDE2. Enzyme Commission Number: EC 3.1.16.1. CAS No. 9068-54-6. PDE. Activity: > 5.0 units/mg protein. Storage: -20°C. Form: lyophilized powder. Source: Bovine spleen. Species: Bovine. 3'-exonuclease; spleen phosphodiesterase; 3'-nucleotide phosphodiesterase; phosphodiesterase II; spleen exonuclease; EC 3.1.16.1; 9068-54-6; PDE2. Cat No: NATE-0518. | |
| Native Bovine Protein Kinase G Iα | Protein Kinase G 1a is a native isoform of protein kinase G type I (cGK-I) isolated from bovine lung. It is a serine-threonine protein kinase found naturally in high concentrations in the cerebellar Purkinje cells, smooth muscle cells, and human platelets. > 95% (sds-page), buffered aqueous glycerol solution. Group: Enzymes. Synonyms: Protein Kinase G Iα; PKG Iα; cGK Iα; cyclic Guanosine Monophosphate Protein Kinase I α; EC 2.7.1.37; PKG1A; cGMP-dependent protein kinase. Enzyme Commission Number: EC 2.7.1.37. Purity: >95% (SDS-PAGE). PKC. Mole weight: mol wt 74 kDa (monomer). Stability: -20°C. Form: buffered aqueous glycerol solution. Source: bovine lung. Species: Bovine. Protein Kinase G Iα; PKG Iα; cGK Iα; cyclic Guanosine Monophosphate Protein Kinase I α; EC 2.7.1.37; PKG1A; cGMP-dependent protein kinase. Cat No: NATE-0579. | |
| Native Bovine Ribonuclease B | Native RNase BS generated by subtilisin digestion of native RNase B comprising of amino acid residues 21-124 of RNase B, is sensitive to PNGase F digestion. Intramolecular N-glycans of bovine pancreatic RNase B function like chaperone. RNase B is found to be much faster than RNase A, while RNase A is liable to aggregate during regeneration. The stimulatory effect of Asn-oligosaccharide (which corresponds to the most predominant sugar chain of RNase B) reveals that the N-glycans of RNase B facilitates the transformation of bulky intermediates into folded, compact species. Group: Enzymes. Synonyms: Pancreatic ribonucleases; EC 3.1.27. glycoproteins; ribonucleate 3'-pyrimidino-oligonucleotidohydrolase; 9001-99-4. Enzyme Commission Number: EC 3.1.27.5. CAS No. 9001-99-4. Purity: > 80% (SDS-PAGE). Rnase. Activity: > 50 Kunitz units/mg protein. Storage: -20°C. Source: Bovine pancreas. Species: Bovine. Pancreatic ribonucleases; EC 3.1.27.5; RNase; RNase I; RNase B; pancreatic RNase; ribonuclease I; endoribonuclease I; ribonucleic phosphatase; alkaline ribonuclease; ribonuclease; gene S glycoproteins; Ceratitis capitata alkaline ribonuclease; SLSG glycoproteins; gene S locus-specific glycoproteins; S-genotype-asssocd. glycoproteins; ribonucleate 3'-pyrimidino-oligonucleotidohydrolase; 9001-99-4. Pack: Package size based on protein content. Cat No: NATE-0656. | |
| Native Bovine Trypsin & Chymotrypsin Mixtures | Native Bovine Trypsin & Chymotrypsin Mixtures. Creative enzymes is a world leading producer of trypsin / chymotrypsin mixtures. trypsin and chymotrypsin are extracted from bovine pancreas and pancreatic juices using multiple precipitation, fractionation, and filtration steps. creative enzymes products are not intended for use in pharmaceutical applications. Applications: In combination with chymotrypsinogen and ribonuclease it is used to formulate anti-inflammatory tablets /treatment of wounds (internal and external) / mixtures of trypsin and chymotrypsin in different ratios frequently are used in digestive aids and food. Group: Enzymes. Synonyms: Trypsin & Chymotrypsin. Trypsin-Chymotrypsin. Activity: >1000 :1000 NF U/mg. Storage: Store at <-15°C. Source: Bovine pancreas. Species: Bovine. Trypsin & Chymotrypsin. Cat No: NATE-0719. | |
| Native Caldariomyces fumago Chloroperoxidase | Chloroperoxidase (CPO) is a 42 kDa Da extracellular heme glycoenzyme containing ferriprotoporphyrin IX as the prosthetic group. CPO is secreted from fungus and exhibits a broad spectrum of chemical reactivities. It is a peroxide-dependent chlorinating enzyme. It also catalyzes peroxidase-, catalase-and cytochrome P450-type reactions of dehydrogenation, H2O2 decomposition and oxygen insertion, respectively. The enzyme has magnetic and spectroscopic properties similar to that of cyctochrome P-450. CPO from the fungus Caldariomyces fumago has the capacity to chlorinate aromatic hydrocarbons, including polycyclic aromatic hydrocarbons (PAHs). Applications: A useful alternative to lactoperoxidase for 131i ion labeling studies, for bromination of proteins, and for cl labeling of macromolecules in long-term isolation procedures. Group: Enzymes. Synonyms: Chloroperoxidase; CPO; Vanadium halopero. Enzyme Commission Number: EC 1.11.1.10. CAS No. 9055-20-3. CPO. Activity: 1,000-2,000 units/mg protein (E1%/280); > 3,000 units/mL; >10,000 U/mL. Storage: 2-8°C. Form: buffered aqueous suspension. Purified suspension in 0.1 M sodium phosphate solution, pH approx. 4.5. Source: Caldariomyces fumago. Chloroperoxidase; CPO; Vanadium haloperoxidase; EC 1.11.1.10; 9055-20-3; Chloride Peroxidase; Chloride:hydrogen-peroxide oxidoreductase. Cat No: NATE-0156. | |
| Native Candida sp. Alcohol oxidase | In enzymology, an alcohol oxidase (EC 1.1.3.13) is an enzyme that catalyzes the chemical reaction a primary alcohol + O2 <-> an aldehyde + H2O2. Thus, the two substrates of this enzyme are primary alcohol and O2, whereas its two products are aldehyde and H2O2. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with oxygen as acceptor. Native alcohol oxidase (ec 1.1.3.13) was purified from candida sp. Applications: Useful for enzymatic determination of blood alcohol. Group: Enzymes. Synonyms: ethanol oxidase; alcohol oxidase; EC 1.1.3.13; Methanol oxidase; 9073-63-6. Enzyme Commission Number: EC 1.1.3.13. CAS No. 9073-63-6. Alcohol Oxidase. Activity: 7~20 U/mg. Storage: Store in tightly closed containers, desiccated, protected from light, at-20°C. Form: Light yellow powder. Source: Candida sp. ethanol oxidase; alcohol oxidase; EC 1.1.3.13; Methanol oxidase; 9073-63-6. Cat No: DIA-123. | |
| Native Clostridium histolyticum Collagenase | Collagenases are endopeptidases that digest native collagen in the triple helix region. Collagens are the major fibrous component of animal extracellular connective tissue. Bacterial collagenases differ from vertebrate collagenases in that they exhibit broader substrate specificity (Peterkofsky 1982, Birkedal-Hansen 1987). Unlike animal collagenases that split collagen in its native triple-helical conformation (Woolley et al. 1975, Gross et al. 1974), bacterial collagenase is unique because it can degrade both water-insoluble native collagens and water-soluble denatured ones. It can attack almost all collagen types, and is able to make multiple cleavages within triple h...ations needing to avoid introduction of animal derived pathogens into bioprocessing procedures. Group: Enzymes. Synonyms: EC 3.4.24.3; Collagenase; Clostridiopeptidase A; Clostridium histolyticum collagenase; collagenase A; collagenase I; Achromobacter iophagus collagenase; aspergillopeptidase C; nucleolysin; Collagenase, Type 1; Collagenase, Type 2; Collagenase, Type 3; Collagenase, Type 4; Collagenase, Type 5. Enzyme Commission Number: EC 3.4.24.3. CAS No. 9001-12-1. Collagenase. Mole weight: 68 to 130 kDa. Activity: Type 1 > 125 units per mg; Type 2 > 125 units per mg; Type 3 > 100 units per mg; Type 4 > 160 units per mg; Type 5 > 450 units per mg. Stability: This pro | |
| Native Clostridium kluyveri Diaphorase | Native Clostridium kluyveri Diaphorase. Applications: Diaphorase from clostridium kluyveri, or lipoyl dehydrogenase, has been used in a study to assess the protein-protein interactions in assembly of lipoic acid on the 2-oxoacid dehydrogenases of aerobic metabolism. lipoyl dehydrogenase has also been used in a study to investigate the redox regulation of tyrosine nitration and 3-nitrotyrosine reduction by antioxidants. Group: Enzymes. Synonyms: dehydrolipoate dehydrogenase; diaphorase; dihydrolipoamide dehydrogenase; dihydrolipoamide:NAD+ oxidoreductase; dihydrolipoic dehydrogenase; dihydrothioctic dehydrogenase; lipoamide dehydrogenase (NADH); lipoamide oxidoreductase (NADH); lipoamide reductase; lipo. Enzyme Commission Number: EC 1.8.1.4. CAS No. 9001-18-7. Diaphorase. Activity: 3.0-20.0 units/mg protein (biuret). Storage: Store at -20°C. Form: Lyophilized powder. Source: Clostridium kluyveri. dehydrolipoate dehydrogenase; diaphorase; dihydrolipoamide dehydrogenase; dihydrolipoamide:NAD+ oxidoreductase; dihydrolipoic dehydrogenase; dihydrothioctic dehydrogenase; lipoamide dehydrogenase (NADH); lipoamide oxidoreductase (NADH); lipoamide reductase; lipoamide reductase (NADH); lipoate dehydrogenase; lipoic acid dehydrogenase; lipoyl dehydrogenase; dihydrolipoyl dehydrogenase; EC 1.8.1.4; 9001-18-7; Lipoamide Dehydrogenase. Cat No: NATE-0875. | |
| Native Clostridium sp. Diaphorase | Native Clostridium sp. Diaphorase. Applications: This enzyme is useful for colorimetric determination of nad(p)h and many dehydrogenases when coupled with various dyes which act as hydrogen acceptors from nad(p)h. Group: Enzymes. Synonyms: Diaphorase; EC 1.6.99.-. Enzyme Commission Number: EC 1.6.99.-. Diaphorase. Mole weight: 24 kDa. Activity: Grade? 30U/mg-solid or more (containing approx. 15% of stabilizers). Stability: Stable at-20°C for at least one year. Appearance: Yellowish amorphous powder, lyophilized. Form: Freeze dried powder. Source: Clostridium sp. Diaphorase; EC 1.6.99.-. Cat No: DIA-187. | |
| Native Cucurbita sp. L-ascorbate oxidase | In enzymology, a L-ascorbate oxidase (EC 1.10.3.3) is an enzyme that catalyzes the chemical reaction2 L-ascorbate + O2 ? 2 dehydroascorbate + 2 H2O. Thus, the two substrates of this enzyme are L-ascorbate and O2, whereas its two products are dehydroascorbate and H2O. Native l-ascorbate oxidase (ec 1.10.3.3) was purified from acremonium sp. Applications: This enzyme is useful for enzymatic determination of ascorbic acid and for eliminating the interference of ascorbic acid in clinical analysis. Group: Enzymes. Synonyms: ascorbase; ascorbic acid oxidase; ascorbate oxidase; ascorbic oxidase; ascorbate dehydrogenase; L-ascorbic acid oxidase; AAO; L-ascorbate: O2 oxidoreductase; AA oxidase; EC 1.10.3.3; 9029-44-1; L-ascorbate oxidase. Enzyme Commission Number: EC 1.10.3.3. CAS No. 9029-44-1. Activity: 200U/mg. Appearance: Light blue amorphous powder, lyophilized. Storage: Store in tightly closed containers, desiccated, protected from light, at-20°C. Form: Light blue lyophilized powder. Source: Cucurbita sp. ascorbase; ascorbic acid oxidase; ascorbate oxidase; ascorbic oxidase; ascorbate dehydrogenase; L-ascorbic acid oxidase; AAO; L-ascorbate: O2 oxidoreductase; AA oxidase; EC 1.10.3.3; 9029-44-1; L-ascorbate oxidase. Cat No: DIA-124. | |
| Native E. coli 1-5-Anhydroglucitol-6-Phosphate Dehydrogenase | Native E. coli 1-5-Anhydroglucitol-6-Phosphate Dehydrogenase. Ag6pdhii is an enzyme produced by microorganisms. this product shall be used for a diagnostics reagent. Applications: Useful for enzymatic determination of 1,5-ag. Group: Enzymes. Synonyms: AG6PDHII; EC 1.1.1.140; 1-5-Anhydroglucitol-6-Phosphate Dehydrogenase. Enzyme Commission Number: EC 1.1.1.140. CAS No. 37250-69-4. AG6PDHII. Mole weight: 78 kDa (TSK gel G 3000 SWXL gel filtration); 40 kDa (SDS-PAGE). Activity: > 20 U/mg. Stability: Stable for 1 years under the freezing condition (-80°C). Appearance: White powder. Storage: Storage at-80°C in the presence of a desiccant is recommended. Form: Freeze dried powder. Source: Escherichia coli. AG6PDHII; EC 1.1.1.140; 1-5-Anhydroglucitol-6-Phosphate Dehydrogenase. Cat No: NATE-0039. | |
| Native Equine Spleen Apoferritin | Native apo-ferritin from equine spleen is a native protein shell of ferritin molecule lacking iron. Group: Enzymes. Synonyms: Ferritin, Apo-; Apoferritin; Ferritin; Apo-Ferritin; Apo ferritin. CAS No. 9013-31-4. Purity: 0.95. Storage: Store at -20° C. Form: Freeze-dried powder. Source: Equine Spleen. Species: Equine. Ferritin, Apo-; Apoferritin; Ferritin; Apo-Ferritin; Apo ferritin. Cat No: NATE-1873. | |
| Native Flavobacterium heparinum Heparinase I | In enzymology, a heparin lyase (EC 4.2.2.7) is an enzyme that catalyzes the chemical reaction: Eliminative cleavage of polysaccharides containing 1,4-linked D-glucuronate or L-iduronate residues and 1,4-alpha-linked 2-sulfoamino-2-deoxy-6-sulfo-D-glucose residues to give oligosaccharides with terminal 4-deoxy-alpha-D-gluc-4-enuronosyl groups at their non-reducing ends. This enzyme belongs to the family of lyases, specifically those carbon-oxygen lyases acting on polysaccharides. Group: Enzymes. Synonyms: EC 4.2.2.7; Heparinase I; 9025-39-2; heparin eliminase; heparinase; heparin lyase. Enzyme Commission Number: EC 4.2.2.7. CAS No. 9025-39-2. Heparinase. Mole weight: mol wt 42.8 kDa. Activity: > 200 units/mg protein (enzyme + BSA). Storage: -20°C. Source: Flavobacterium heparinum. EC 4.2.2.7; Heparinase I; 9025-39-2; heparin eliminase; heparinase; heparin lyase. Cat No: NATE-0338. | |
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