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| Product | Description | |
|---|---|---|
| 1,2-Dioleoyl-sn-glycerol | ALN29882 is a glycerolipid located on the plasma membrane. It consists of two fatty acid chains covalently linked to a single glycerol molecule by means of an ester bond. 18:1 DG has been used as a source of diacylglycerol in the diacylglycerol O-acyltransferase 1 (DGAT1) assay. It is also used as a substrate in the DGAT-1 enzyme assay to evaluate compounds as potential inhibitors of DGAT-1. Suitable for lipoprotein overlay screening assays with the recombinant protein His-AtROP6. Uses: Scientific research. Group: Biochemical assay reagents. Alternative Names: sn-1,2-Dioleoylglycerol. CAS No. 24529-88-2. Pack Sizes: 5 mg; 10 mg; 25 mg. Product ID: HY-141572. |  |
| 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase | Requires Mg2+ for maximal activity. This enzyme is involved in the biosynthesis of vitamin K2 (menaquinone). In most anaerobes and all Gram-positive aerobes, menaquinone is the sole electron transporter in the respiratory chain and is essential for their survival. It had previously been thought that the products of the reaction were (1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate (SHCHC), pyruvate and CO2 but it is now known that two separate enzymes are involved: this enzyme and EC 4.2.99.20, 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase. Under basic conditions, the product can spontaneously lose pyruvate to form SHCHC. Group: Enzymes. Synonyms: SEPHCHC synthase; MenD. Enzyme Commission Number: EC 2.2.1.9. CAS No. 1112282-73-1. 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-2036; 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase; EC 2.2.1.9; 1112282-73-1; SEPHCHC synthase; MenD. Cat No: EXWM-2036. |  |
| aerobic carbon monoxide dehydrogenase | This enzyme, found in carboxydotrophic bacteria, catalyses the oxidation of CO to CO2 under aerobic conditions. The enzyme contains a binuclear Mo-Cu cluster in which the copper is ligated to a molybdopterin center via a sulfur bridge. The enzyme also contains two [2Fe-2S] clusters and FAD, and belongs to the xanthine oxidoreductase family. The CO2 that is produced is assimilated by the Calvin-Benson-Basham cycle, while the electrons are transferred to a quinone via the FAD site, and continue through the electron transfer chain to a dioxygen terminal acceptor. cf. EC 1.2.7.4, anaerobic carbon monoxide dehydrogenase. Group: Enzymes. Synonyms: MoCu-CODH; coxSML (gene names); molybdoenzyme carbon monoxide dehydrogenase. Enzyme Commission Number: EC 1.2.5.3. 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-1222; aerobic carbon monoxide dehydrogenase; EC 1.2.5.3; MoCu-CODH; coxSML (gene names); molybdoenzyme carbon monoxide dehydrogenase. Cat No: EXWM-1222. | |
| Alanine Aminotransferase from Human, Recombinant | Alanine transaminase (ALT) is a transaminase enzyme. It is also called alanine aminotransferase (ALAT) and was formerly called serum glutamate-pyruvate transaminase (SGPT) or serum glutamic-pyruvic transaminase (SGPT). ALT is found in plasma and in various body tissues, but is most common in the liver. It catalyzes the two parts of the alanine cycle. Serum ALT level, serum AST (aspartate transaminase) level, and their ratio (AST/ALT ratio) are commonly measured clinically as biomarkers for liver health. The tests are part of blood panels. Alanine aminotransferase human recombinant produced in e. coli is a homodimer, nonglycosylated, polypeptide chain containing 495a.a...inotransferase; pyruvate transaminase; pyruvate-alanine aminotransferase; pyruvate-glutamate transaminase. CAS No. 9000-86-6. Purity: Greater than 95.0% as determined by (a) Analysis by RP-HPLC. (b) Analysis by SDS-PAGE. ALT. Mole weight: 54,479 Da. Activity: 1,000 U/mg. Stability: AAT1 although stable at 10°C for 5 days, should be stored desiccated below -18°C. Please prevent freeze-thaw cycles. Appearance: Sterile liquid formulation. Source: E. coli. Species: Human. ALT1; Glutamic-pyruvic transaminase 1; GPT 1; Glutamic-alanine transaminase 1; AAT1; ALT; ALAT; SGPT; Alanine transaminase; alanine aminotransferase; GPT; β-alanine aminotransferase; alanine-α | |
| all-trans-nonaprenyl diphosphate synthase [geranylgeranyl-diphosphate specific] | Geranylgeranyl diphosphate is preferred over farnesyl diphosphate as allylic substrate. The plant Arabidopsis thaliana has two different enzymes that catalyse this reaction. SPS1 contributes to the biosynthesis of the ubiquinone side-chain while SPS2 supplies the precursor of the plastoquinone side-chains. Group: Enzymes. Synonyms: nonaprenyl diphosphate synthase (ambiguous); solanesyl diphosphate synthase (ambiguous); At-SPS2; At-SPS1; SPS1; SPS2. Enzyme Commission Number: EC 2.5.1.85. 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-2823; all-trans-nonaprenyl diphosphate synthase [geranylgeranyl-diphosphate specific]; EC 2.5.1.85; nonaprenyl diphosphate synthase (ambiguous); solanesyl diphosphate synthase (ambiguous); At-SPS2; At-SPS1; SPS1; SPS2. Cat No: EXWM-2823. | |
| amylo-α-1,6-glucosidase | This enzyme hydrolyses an unsubstituted glucose unit linked by an α(1?6) bond to an α(1?4) glucose chain. The enzyme activity found in mammals and yeast is in a polypeptide chain containing two active centres. The other activity is similar to that of EC 2.4.1.25 (4-α-glucanotransferase), which acts on the glycogen phosphorylase limit dextrin chains to expose the single glucose residues, which the 6-α-glucosidase activity can then hydrolyse. Together, these two activities constitute the glycogen debranching system. Group: Enzymes. Synonyms: amylo-1,6-glucosidase; dextrin 6-α-D-glucosidase; amylopectin 1,6-glucosidase; dextrin-1,6-glucosidase; glycogen phosphorylase-limit dextrin α-1,6-glucohydrolase. Enzyme Commission Number: EC 3.2.1.33. CAS No. 9012-47-9. 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-3896; amylo-α-1,6-glucosidase; EC 3.2.1.33; 9012-47-9; amylo-1,6-glucosidase; dextrin 6-α-D-glucosidase; amylopectin 1,6-glucosidase; dextrin-1,6-glucosidase; glycogen phosphorylase-limit dextrin α-1,6-glucohydrolase. Cat No: EXWM-3896. | |
| anaerobic carbon-monoxide dehydrogenase | This prokaryotic enzyme catalyses the reversible reduction of CO2 to CO. The electrons are transferred to redox proteins such as ferredoxin. In purple sulfur bacteria and methanogenic archaea it catalyses the oxidation of CO to CO2, which is incorporated by the Calvin-Benson-Basham cycle or released, respectively. In acetogenic and sulfate-reducing microbes it catalyses the reduction of CO2 to CO, which is incorporated into acetyl CoA by EC 2.3.1.169, CO-methylating acetyl CoA synthase, with which the enzyme forms a tight complex in those organisms. The enzyme contains five metal clusters per homodimeric enzyme: two nickel-iron-sulfur clusters called the C-Clusters, one [...-4S] clusters exist, presumably as part of the electron transfer chain. In purple sulfur bacteria the enzyme forms complexes with the Ni-Fe-S protein EC 1.12.7.2, ferredoxin hydrogenase, which catalyse the overall reaction: CO + H2O = CO2 + H2. cf. EC 1.2.5.3, aerobic carbon monoxide dehydrogenase. Group: Enzymes. Synonyms: Ni-CODH; carbon-monoxide dehydrogenase (ferredoxin). Enzyme Commission Number: EC 1.2.7.4. 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-1227; anaerobic carbon-monoxide dehydrogenase; EC 1.2.7.4; Ni-CODH; carbon-monoxide dehydrogenase (ferredoxin). Cat No: EXWM-1227. | |
| ATP Sulfurylase from S. cerevisiae, Recombinant | 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. Adenosine 5-triphosphate sulfurylase yeast recombinant produced in e. coli is a non-glycosylated, polypeptide chain containin...formed from aps and ppi. adenosine 5-triphosphate sulfurylase is purified by proprietary chromatographic techniques. Group: Enzymes. 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. CAS No. 9012-39-9. ATP-sulfurylase. Storage: at -20°C. Source: E. coli. Species: S. 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-1280. | |
| β-ketoacyl-[acyl-carrier-protein] synthase I | This enzyme is responsible for the chain-elongation step of dissociated (type II) fatty-acid biosynthesis, i.e. the addition of two C atoms to the fatty-acid chain. Escherichia coli mutants that lack this enzyme are deficient in unsaturated fatty acids. The enzyme can use fatty acyl thioesters of ACP (C2 to C16) as substrates, as well as fatty acyl thioesters of Co-A (C4 to C16). The substrate specificity is very similar to that of EC 2.3.1.179, β-ketoacyl-ACP synthase II, with the exception that the latter enzyme is far more active with palmitoleoyl-ACP (C16Δ9) as substrate, allowing the organism to regulate its fatty-acid composition with changes in temperature. Group: Enzymes. Synonyms: β-ketoa. Enzyme Commission Number: EC 2.3.1.41. CAS No. 9077-10-5. 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-2220; β-ketoacyl-[acyl-carrier-protein] synthase I; EC 2.3.1.41; 9077-10-5; β-ketoacyl-ACP synthase I; β-ketoacyl synthetase; β-ketoacyl-ACP synthetase; β-ketoacyl-acyl carrier protein synthetase; β-ketoacyl-[acyl carrier protein] synthase; β-ketoacylsynthase; condensing enzyme (ambiguous); 3-ketoacyl-acyl carrier protein synthase; fatty acid condensing enzyme; acyl-malonyl(acyl-carrier-protein)-c | |
| bile acid-CoA:amino acid N-acyltransferase | Also acts on CoA derivatives of other bile acids. Taurine and 2-fluoro-β-alanine can act as substrates, but more slowly. The enzyme can also conjugate fatty acids to glycine and can act as a very-long-chain acyl-CoA thioesterase. Bile-acid-amino-acid conjugates serve as detergents in the gastrointestinal tract, solubilizing long chain fatty acids, mono- and diglycerides, fat-soluble vitamins and cholesterol. This is the second enzyme in a two-step process leading to the conjugation of bile acids with amino acids; the first step is the conversion of bile acids into their acyl-CoA thioesters, which is catalysed by EC 6.2.1.7, cholate-CoA ligase. Group: Enzymes. Synonyms: glycine-taurine N-acyltransferase; amino acid N-choloyltransferase; BAT; glycine N-choloyltransferase; BACAT; cholyl-CoA glycine-taurine N-acyltransferase; cholyl-CoA:taurine N-acyltransferase. Enzyme Commission Number: EC 2.3.1.65. CAS No. 65979-40-0. 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-2245; bile acid-CoA:amino acid N-acyltransferase; EC 2.3.1.65; 65979-40-0; glycine-taurine N-acyltransferase; amino acid N-choloyltransferase; BAT; glycine N-choloyltransferase; BACAT; cholyl-CoA glycine-taurine N-acyltransferase; cholyl-CoA:taurine N-acyltransferase. Cat No: EXWM-2245. | |
| Biotinylated Transglutaminase from Human, Recombinant | This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a phosphate group as acceptor. Applications: Recombinant human transglutaminase is a homodimer (a2) composed of two chains held together by non covalent bonds. after activation of the zymogen by thrombin and ca2+ to its active form (a*2, factor xiiia), factor xiiia catalyzes the formation of covalent bridges (ε-(γ-glutamyl) lysine bonds) between fibrin units to increase the elasticity of the clot network. the resulting cross-linked fibrin is insoluble and resistant to lysis. Group: Enzymes. Synonyms: transglutamina... Lorand et al., Anal. Biochem. 44 (221-231). Appearance: Liquid. Storage: Store working aliquots at ≤ - 20°C. Avoid repeated freezing and thawing. Form: The transglutaminase is formulated in 10 mM Sodium Phosphate pH 8.0, 15 mM NaCl. Sample contains 50% glycerol. hFXIII is a Ca2+-dependent enzyme. Source: Insect cells. Species: Human. transglutaminase; EC 2.3.2.13; 80146-85-6; transglutaminase; Factor XIIIa; fibrinoligase; fibrin stabilizing factor; glutaminylpeptide γ-glutamyltransferase; polyamine transglutaminase; tissue transglutaminase; R-glutaminyl-peptide:amine γ-glutamyl transferase; protein-glutamine γ-glutamyltransferase; TG1. Pack: 50 | |
| [butirosin acyl-carrier protein]-L-glutamate ligase | Catalyses two steps in the biosynthesis of the side chain of the aminoglycoside antibiotics of the butirosin family. The enzyme adds one molecule of L-glutamate to a dedicated acyl-carrier protein, and following decarboxylation of the product by EC 4.1.1.95, L-glutamyl-[BtrI acyl-carrier protein] decarboxylase, adds a second L-glutamate molecule.Requires Mg2+ or Mn2+, and activity is enhanced in the presence of Mn2+. Group: Enzymes. Synonyms: [BtrI acyl-carrier protein]-L-glutamate ligase; BtrJ. Enzyme Commission Number: EC 6.2.1.39. 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-5697; [butirosin acyl-carrier protein]-L-glutamate ligase; EC 6.2.1.39; [BtrI acyl-carrier protein]-L-glutamate ligase; BtrJ. Cat No: EXWM-5697. | |
| cGMP-dependent protein kinase | CGMP is required to activate this enzyme. The enzyme occurs as a dimer in higher eukaryotes. The C-terminal region of each polypeptide chain contains the catalytic domain that includes the ATP and protein substrate binding sites. This domain catalyses the phosphorylation by ATP to specific serine or threonine residues in protein substrates. The enzyme also has two allosteric cGMP-binding sites (sites A and B). Binding of cGMP causes a conformational change that is associated with activation of the kinase. Group: Enzymes. Synonyms: 3':5'-cyclic GMP-dependent protein kinase; cGMP-dependent protein kinase Iβ; guanosine 3':5'-cyclic monophosphate-dependent protein kinase; PKG; PKG 1α; PKG 1β; PKG II; STK23. Enzyme Commission Number: EC 2.7.11.12. CAS No. 141588-27-4. 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-3131; cGMP-dependent protein kinase; EC 2.7.11.12; 141588-27-4; 3':5'-cyclic GMP-dependent protein kinase; cGMP-dependent protein kinase Iβ; guanosine 3':5'-cyclic monophosphate-dependent protein kinase; PKG; PKG 1α; PKG 1β; PKG II; STK23. Cat No: EXWM-3131. | |
| cholest-4-en-3-one 26-monooxygenase [(25S)-3-oxocholest-4-en-26-oate forming] | This enzyme, found in several bacterial pathogens, is involved in degradation of the host's cholesterol. It catalyses the hydroxylation of the C-26 carbon, followed by oxidation of the alcohol to the carboxylic acid via the aldehyde intermediate, initiating the degradation of the alkyl side-chain of cholesterol. The products are exclusively in the (25S) configuration. It is a two-component system consisting of a P-450 (heme thiolate) oxygenase (Cyp125) and a ferredoxin reductase (most likely KshB, which is also a part of EC 1.14.13.142, 3-ketosteroid 9α-monooxygenase). The enzyme also accepts cholesterol as a substrate. cf. EC 1.14.13.221, cholest-4-en-3-one 27-monooxygenase. Group: Enzymes. Synonyms: CYP125; CYP125A1; cholest-4-en-3-one 27-monooxygenase (misleading); cholest-4-en-3-one,NADH:oxygen oxidoreductase (26-hydroxyl. Enzyme Commission Number: EC 1.14.13.141. 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-0741; cholest-4-en-3-one 26-monooxygenase [(25S)-3-oxocholest-4-en-26-oate forming]; EC 1.14.13.141; CYP125; CYP125A1; cholest-4-en-3-one 27-monooxygenase (misleading); cholest-4-en-3-one,NADH:oxygen oxidoreductase (26-hydroxylating); cholest-4-en-3-one 26-monooxygenase (ambiguous). Cat No: EXWM-0741. | |
| cholesterol monooxygenase (side-chain-cleaving) | A heme-thiolate protein (cytochrome P-450). The reaction proceeds in three stages, with two hydroxylations at C-22 and C-20 preceding scission of the side-chain between carbons 20 and 22. The initial source of the electrons is NADPH, which transfers the electrons to the adrenodoxin via EC 1.18.1.6, adrenodoxin-NADP+ reductase. Group: Enzymes. Synonyms: cholesterol desmolase; cytochrome P-450scc; C27-side chain cleavage enzyme; cholesterol 20-22-desmolase; cholesterol C20-22 desmolase; cholesterol side-chain cleavage enzyme; cholesterol side-chain-cleaving enzyme; steroid 20-22 desmolase; steroid 20-22-lyase; CYP11A1 (gene name). Enzyme Commission Number: EC 1.14.15.6. CAS No. 37292-81-2, 440354-98-3. 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-0949; cholesterol monooxygenase (side-chain-cleaving); EC 1.14.15.6; 37292-81-2, 440354-98-3; cholesterol desmolase; cytochrome P-450scc; C27-side chain cleavage enzyme; cholesterol 20-22-desmolase; cholesterol C20-22 desmolase; cholesterol side-chain cleavage enzyme; cholesterol side-chain-cleaving enzyme; steroid 20-22 desmolase; steroid 20-22-lyase; CYP11A1 (gene name). Cat No: EXWM-0949. | |
| Creatine Kinase BB Fraction Human, Recombinant | Brain-type creatine kinase also known as CK-BB is a creatine kinase that in humans is encoded by the CKB gene. The protein encoded by this gene, CK-BB, consists of a homodimer of two identical brain-type CK-B subunits. BB-CK is a cytoplasmic enzyme involved in cellular energy homeostasis, with certain fractions of the enzyme being bound to cell membranes, ATPases, and a variety of ATP-requiring enzymes in the cell. > 90% (sds-page), liquid, recombinant, expressed in pichia pastoris. Applications: Human creatine kinase bb fraction has been used to investigate the survival benefit of the late percutaneous coronary intervention in patients after acute myocardial infarction. human creatine kinase bb fraction has also been used in a study to analyze protein oxidations and resultant loss of function. Group: Enzymes. Synonyms: CKB; creatine kinase, brain; CKBB; creatine kinase B-type; creatine kinase-B; creatine kinase B chain; B-CK; Brain-type creatine kinase; Creatine Kinase BB; CK-BB; BB-CK. Purity: > 90% (SDS-PAGE). CK. Stability: -70°C. Form: liquid. Source: Pichia pastoris. Species: Human. CKB; creatine kinase, brain; CKBB; creatine kinase B-type; creatine kinase-B; creatine kinase B chain; B-CK; Brain-type creatine kinase; Creatine Kinase BB; CK-BB; BB-CK. Cat No: NATE-0139. | |
| D-glutamyltransferase | The enzyme catalyses two reactions. The first is the transfer of a glutamyl residue from L- or D-glutamine to D-glutamate via a γ linkage, forming γ-glutamyl-D-glutamate, and the second is the transfer of additional glutamyl residues to the peptide, extending the polypeptide chain. Group: Enzymes. Synonyms: D-glutamyl transpeptidase; D-γ-glutamyl transpeptidase. Enzyme Commission Number: EC 2.3.2.1. CAS No. 9030-2-8. 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-2282; D-glutamyltransferase; EC 2.3.2.1; 9030-02-8; D-glutamyl transpeptidase; D-γ-glutamyl transpeptidase. Cat No: EXWM-2282. | |
| dimethyl-sulfide monooxygenase | The enzyme has lower activity with diethyl sulfide and other short-chain alkyl methyl sulfides. Its activity is stimulated by combined addition of FMN, and, after depletion of cations, of Mg2+ and Fe2+. The enzyme from Hyphomicrobium is a two component system that includes an FMN-dependent reductase subunit and a monooxygenase subunit. Group: Enzymes. Synonyms: dimethylsulfide monooxygenase. Enzyme Commission Number: EC 1.14.13.131. 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-0731; dimethyl-sulfide monooxygenase; EC 1.14.13.131; dimethylsulfide monooxygenase. Cat No: EXWM-0731. | |
| ditrans,polycis-polyprenyl diphosphate synthase [(2E,6E)-farnesyl diphosphate specific] | The enzyme is involved in biosynthesis of dolichol (a long-chain polyprenol) with a saturated α-isoprene unit, which serves as a glycosyl carrier in protein glycosylation. The yeast Saccharomyces cerevisiae has two different enzymes that catalyse this reaction. Rer2p synthesizes a well-defined family of polyprenols of 13-18 isoprene residues with dominating C80 (16 isoprene residues) extending to C120, while Srt1p synthesizes mainly polyprenol with 22 isoprene subunits. Largest Srt1p products reach C290. The enzyme from Arabidopsis thaliana catalyses the formation of polyprenyl diphosphates with predominant carbon number C120. Group: Enzymes. Synonyms: RER2; Rer2p; Rer2p Z-prenyltransferase; Srt1p; Srt2p Z-prenyltransferase; ACPT; dehydrodolichyl diphosphate synthase 1. Enzyme Commission Number: EC 2.5.1.87. 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-2825; ditrans,polycis-polyprenyl diphosphate synthase [(2E,6E)-farnesyl diphosphate specific]; EC 2.5.1.87; RER2; Rer2p; Rer2p Z-prenyltransferase; Srt1p; Srt2p Z-prenyltransferase; ACPT; dehydrodolichyl diphosphate synthase 1. Cat No: EXWM-2825. | |
| dynein ATPase | A multisubunit protein complex associated with microtubules. Hydrolysis of ATP provides energy for the movement of organelles (endosomes, lysosomes, mitochondria) along microtubules to the centrosome towards the microtubule's minus end. It also functions in the movement of eukaryotic flagella and cilia. It consists of two heavy chains (about 500 kDa), three-four intermediate chains (about 70 kDa) and four light chains (about 50 kDa). Group: Enzymes. Synonyms: dynein adenosine 5'-triphosphatase. Enzyme Commission Number: EC 3.6.4.2. 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-4704; dynein ATPase; EC 3.6.4.2; dynein adenosine 5'-triphosphatase. Cat No: EXWM-4704. | |
| Endo-β-N-acetylglucosaminidase from Arthrobacter protophormia, Recombinant | An Endoglycosidase is an enzyme that releases oligosaccharides from glycoproteins or glycolipids. It may also cleave polysaccharide chains between residues that are not the terminal residue, although releasing oligosaccharides from conjugated protein and lipid molecules is more common. It breaks the glycosidic bonds between two sugar monomer in the polymer. It is different from exoglycosidase that it does not do so at the terminal residue. Hence, it is used to release long carbohydrates from conjugated molecules. If an exoglycosidase were used, every monomer in the polymer would have to be removed, one by one from the chain, taking a long time. An endoglycosidase cleaves, giving a polymeric product. Group: Enzymes. Synonyms: Endoglycosidase; Endo-β-N-acetylglucosaminidase; EC 3.2.1.96; 231-791-2. Enzyme Commission Number: EC 3.2.1.96. CAS No. 37278-88-9. Purity: min 95% by SDS-PAGE. Endo-β-N-acetylglucosaminidase. Mole weight: 69 kDa. Source: E. coli. Species: Arthrobacter protophormia. Endoglycosidase; Endo-β-N-acetylglucosaminidase; EC 3.2.1.96; 231-791-2; Endo-A; Endo-β-N-Acetylglucosaminidase A. Cat No: NATE-1493. | |
| Endo-β-N-acetylglucosaminidase from Clostridium perfringens, Recombinant | An Endoglycosidase is an enzyme that releases oligosaccharides from glycoproteins or glycolipids. It may also cleave polysaccharide chains between residues that are not the terminal residue, although releasing oligosaccharides from conjugated protein and lipid molecules is more common. It breaks the glycosidic bonds between two sugar monomer in the polymer. It is different from exoglycosidase that it does not do so at the terminal residue. Hence, it is used to release long carbohydrates from conjugated molecules. If an exoglycosidase were used, every monomer in the polymer would have to be removed, one by one from the chain, taking a long time. An endoglycosidase cleaves, giving a polymeric product. Group: Enzymes. Synonyms: Endoglycosidase; Endo-β-N-acetylglucosaminidase; EC 3.2.1.96; 231-791-2. Enzyme Commission Number: EC 3.2.1.96. CAS No. 37278-88-9. Purity: > 95 % as judged by SDS-PAGE. Endo-β-N-acetylglucosaminidase. Storage: Store at 4°C (shipped at room temperature). Form: Supplied in 3.2 M ammonium sulphate. Source: Clostridium perfringens. Endoglycosidase; Endo-β-N-acetylglucosaminidase; EC 3.2.1.96; 231-791-2. Cat No: NATE-1203. | |
| Endoglycosidase F1 from Elizabethkingia miricola, Recombinant | An Endoglycosidase is an enzyme that releases oligosaccharides from glycoproteins or glycolipids. It may also cleave polysaccharide chains between residues that are not the terminal residue, although releasing oligosaccharides from conjugated protein and lipid molecules is more common. It breaks the glycosidic bonds between two sugar monomer in the polymer. It is different from exoglycosidase that it does not do so at the terminal residue. Hence, it is used to release long carbohydrates from conjugated molecules. If an exoglycosidase were used, every monomer in the polymer would have to be removed, one by one from the chain, taking a long time. An endoglycosida...ules. if an exoglycosidase were used, every monomer in the polymer would have to be removed, one by one from the chain, taking a long time. an endoglycosidase cleaves, giving a polymeric product. Group: Enzymes. Synonyms: Endoglycosidase; Endo F1; Endo-β-N-acetylglucosaminidase F1; Endoglycosidase F1 from Chryseobacterium meningosepticum; Endoglycosidase F1 from Elizabethkingia meningoseptica; Endoglycosidase F1 from Flavobacterium meningosepticum; Endoglycosidase F1; EC 3.2.1.96; 231-791-2. Enzyme Commission Number: EC 3.2.1.96. CAS No. 231-791-2. Endo-β-N-acetylglucosaminidase. Activity: > 16 U/mg, buffered aqueous solution. Storage: 2-8°C. Form: buf | |
| Endoglycosidase F2 from Elizabethkingia miricola, Recombinant | An Endoglycosidase is an enzyme that releases oligosaccharides from glycoproteins or glycolipids. It may also cleave polysaccharide chains between residues that are not the terminal residue, although releasing oligosaccharides from conjugated protein and lipid molecules is more common. It breaks the glycosidic bonds between two sugar monomer in the polymer. It is different from exoglycosidase that it does not do so at the terminal residue. Hence, it is used to release long carbohydrates from conjugated molecules. If an exoglycosidase were used, every monomer in the polymer would have to be removed, one by one from the chain, taking a long time. An endoglycosidase cleaves, giving a polymeric product. Group: Enzymes. Synonyms: EC 3.2.1.96; Elizabethkingia miricola; Endo-β-N-acetylglucosaminidase F2; Endo F2; Endoglycosidase F2 from Chryseobacterium meningosepticum; Endoglycosidase F2 from Elizabethkingia meningoseptica; Endoglyco. Enzyme Commission Number: EC 3.2.1.96. CAS No. 37278-88-9. Endo-β-N-acetylglucosaminidase. Activity: 20 units/mg. Storage: -20°C. Form: Aseptically filled solution in 10 mM sodium acetate, 25 mM sodium chloride, pH 4.5. Source: E. coli. Species: Elizabethkingia miricola. EC 3.2.1.96; Elizabethkingia miricola; Endo-β-N-acetylglucosaminidase F2; Endo F2; Endoglycosidase F2 from Ch | |
| Endoglycosidase F3 from Elizabethkingia miricola, Recombinant | An Endoglycosidase is an enzyme that releases oligosaccharides from glycoproteins or glycolipids. It may also cleave polysaccharide chains between residues that are not the terminal residue, although releasing oligosaccharides from conjugated protein and lipid molecules is more common. It breaks the glycosidic bonds between two sugar monomer in the polymer. It is different from exoglycosidase that it does not do so at the terminal residue. Hence, it is used to release long carbohydrates from conjugated molecules. If an exoglycosidase were used, every monomer in the polymer would have to be removed, one by one from the chain, taking a long time. An endoglycosidase cleaves, giving a polymeric product. Group: Enzymes. Synonyms: Endoglycosidase F3; Elizabethkingia miricola; Endo-β-N-. Enzyme Commission Number: EC 3.2.1.96. CAS No. 231-791-2. Endo-β-N-acetylglucosaminidase. Activity: 30 U/mg. Storage: 2-8°C. Form: Aseptically filled solution in 20 mM Tris-HCl, pH 7.5. Source: E. coli. Species: Elizabethkingia miricola. Endoglycosidase F3; Elizabethkingia miricola; Endo-β-N-acetylglucosaminidase F3; Endoglycosidase F3 from Elizabethkingia (Chryseobacterium/Flavobacterium) meningosepticum; EC 3.2.1.96; 231-791-2; Endo F3. Pack: Supplied with 5× Reaction Buffer, 250 mM sodium acetate, pH 4.5. Cat No: NATE-0216. | |
| γ-glutamyltransferase | The mammlian enzyme is part of the cell antioxidant defense mechanism. It initiates extracellular glutathione (GSH) breakdown, provides cells with a local cysteine supply and contributes to maintain intracelular GSH levels. The protein also has EC 3.4.19.13 (glutathione hydrolase) activity. The enzyme consists of two chains that are created by the proteolytic cleavage of a single precursor polypeptide. The N-terminal L-threonine of the C-terminal subunit functions as the active site for both the cleavage and the hydrolysis reactions. Group: Enzymes. Synonyms: glutamyl transpeptidase; α-glutamyl transpeptidase; γ-glutamyl peptidyltransferase; γ-glutamyl transpeptidase (ambiguous); γ-GPT; γ-GT; γ-GTP; L-γ-glutamyl. Enzyme Commission Number: EC 2.3.2.2. CAS No. 9046-27-9. γ-GT. 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-2293; γ-glutamyltransferase; EC 2.3.2.2; 9046-27-9; glutamyl transpeptidase; α-glutamyl transpeptidase; γ-glutamyl peptidyltransferase; γ-glutamyl transpeptidase (ambiguous); γ-GPT; γ-GT; γ-GTP; L-γ-glutamyl transpeptidase; L-γ-glutamyltransferase; L-glutamyltransferase; GGT (ambiguous); γ-glutamyltranspeptidase (ambiguous). Cat No: EXWM-2293. | |
| glutathione hydrolase | This protein also has EC 2.3.2.2 (γ-glutamyltransferase) activity. The enzyme consists of two chains that are created by the proteolytic cleavage of a single precursor polypeptide. The N-terminal L-threonine of the C-terminal subunit functions as the active site for both the cleavage and the hydrolysis reactions. The human enzyme also hydrolyses oxidized glutathione and leukotriene C4 with similar efficiency, while the mouse enzyme does not. Group: Enzymes. Synonyms: glutathionase; GGT (ambiguous); γ-glutamyltranspeptidase (ambiguous). Enzyme Commission Number: EC 3.4.19.13. 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-4085; glutathione hydrolase; EC 3.4.19.13; glutathionase; GGT (ambiguous); γ-glutamyltranspeptidase (ambiguous). Cat No: EXWM-4085. | |
| 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 human urokinase | Immobilized human two-chain HMW urokinase is ideal for the controlled activation of plasminogen to plasmin. After the activation is complete, the resin is simply removed and the reaction is quenched. May be used to immunopurify monoclonal and polyclonal antibodies directed against human urokinase. May be used repeatedly. Group: Enzymes. Synonyms: Urokinase; EC 3. 4. 21. 73; urokinase-type plasminogen activator; uPA; U-plasminogen activator; Cellular plasminogen activator; Urinary plasminogen activator. Enzyme Commission Number: EC 3. 4. 21. 73. Purity: >95% by SDS-PAGE analysis. Mole weight: 54000. Stability: 12 months from delivery. Storage: 4°C. Form: Resin. Source: Insect cell culture. Species: Human. Urokinase; EC 3. 4. 21. 73; urokinase-type plasminogen activator; uPA; U-plasminogen activator; Cellular plasminogen activator; Urinary plasminogen activator; Immobilized uPA; Immobilized urokinase. Cat No: NATE-1759. | |
| L-Aspartic Acid, non-animal | Aspartic acid (abbreviated as Asp or D; encoded by the codons [GAU and GAC]), also known as aspartate, is an α-amino acid that is used in the biosynthesis of proteins.[3] Similar to all other amino acids it contains an amino group and a carboxylic acid. Its α-amino group is in the protonated -NH+3 form under physiological conditions, while its α-carboxylic acid group is deprotonated ?COO? under physiological conditions. Aspartic acid has an acidic side chain (CH2COOH) which reacts with other amino acids, enzymes and proteins in the body. Under physiological conditions (pH 7.4) in proteins the side chain usually occurs as the negatively charged aspartate form, ?COO?. It is a non-essential amino acid in humans, meaning the body can synthesize it as needed.D-Aspartate is one of two D-amino acids commonly found in mammals. In proteins aspartate sidechains are often hydrogen bonded, often as asx turns or asx motifs, which often occur at the N-termini of alpha helices. Asp's L-isomer is one of the 22 proteinogenic amino acids, i.e., the building blocks of proteins. Asp (and glutamic acid) is classified as acidic, with a pKa of 3.9, however in a peptide this is highly dependent on the local environment (as with all amino acids), and could be as high as 14. Asp is pervasive in biosynthesis. Group: Biochemicals. Alternative Names: (S)-(+)-Aminosuccinic acid; (S)-Aminobutanedioic acid. Grades: Cell Culture Grade. CAS No. 56-84-8. Pack Sizes: 100g, 500g, 1Kg, 2.5Kg, 10Kg. Molecular Formula: C4H7NO4, Molecular Weight: 133.1. US Biological Life Sciences. |  Worldwide |
| L-rhamnose isomerase | Contains two divalent metal ions located at different metal-binding sites within the active site. The enzyme binds the closed ring form of the substrate and catalyses ring opening to generate a form of open-chain conformation that is coordinated to one of the metal sites. Isomerization proceeds via a hydride-shift mechanism. While the enzyme from the bacterium Escherichia coli is specific for L-rhamnose, the enzyme from the bacterium Pseudomonas stutzeri has broad substrate specificity and catalyses the interconversion of L-mannose and L-fructose, L-lyxose and L-xylulose, D-ribose and D-ribulose, and D-allose and D-psicose. Group: Enzymes. Synonyms: rhamnose isomerase; L-rhamnose ketol-isomerase. Enzyme Commission Number: EC 5.3.1.14. CAS No. 9023-84-1. 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-5455; L-rhamnose isomerase; EC 5.3.1.14; 9023-84-1; rhamnose isomerase; L-rhamnose ketol-isomerase. Cat No: EXWM-5455. | |
| matriptase | This trypsin-like integral-membrane serine peptidase has been implicated in breast cancer invasion and metastasis. The enzyme can activate hepatocyte growth factor/scattering factor (HGF/SF) by cleavage of the two-chain form at an Arg residue to give active α- and β-HGF, but It does not activate plasminogen, which shares high homology with HGF.The enzyme can also activate urokinase plasminogen activator (uPA), which initiates the matrix-degrading peptidase cascade. Belongs in peptidase family S1A. Group: Enzymes. Synonyms: serine protease 14; membrane-type serine protease 1; MT-SP1; prostamin; serine protease TADG-15; tumor-associated differentially-expressed gene 15 protein; ST14; breast cancer 80 kDa protease; epithin; serine endopeptidase SNC19. Enzyme Commission Number: EC 3.4.21.109. CAS No. 241475-96-7. 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-4104; matriptase; EC 3.4.21.109; 241475-96-7; serine protease 14; membrane-type serine protease 1; MT-SP1; prostamin; serine protease TADG-15; tumor-associated differentially-expressed gene 15 protein; ST14; breast cancer 80 kDa protease; epithin; serine endopeptidase SNC19. Cat No: EXWM-4104. | |
| myosin ATPase | Proteins of the contractile apparatus of muscle and nonmuscle cells; myosin molecule consists of two heavy chains (about 200 kDa) and two pairs of light chains (15-27 kDa). The head region of the heavy chain contains actin- and ATP-binding sites. ATP hydrolysis provides energy for actomyosin contraction. Group: Enzymes. Enzyme Commission Number: EC 3.6.4.1. 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-4699; myosin ATPase; EC 3.6.4.1. Cat No: EXWM-4699. | |
| NAD(P)H dehydrogenase (quinone) | A flavoprotein. The enzyme catalyses a two-electron reduction and has a preference for short-chain acceptor quinones, such as ubiquinone, benzoquinone, juglone and duroquinone. The animal, but not the plant, form of the enzyme is inhibited by dicoumarol. Group: Enzymes. Synonyms: menadione reductase; phylloquinone reductase; quinone reductase; dehydrogenase, reduced nicotinamide adenine dinucleotide (phosphate, quinone); DT-diaphorase; f. Enzyme Commission Number: EC 1.6.5.2. CAS No. 9032-20-6. 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-1591; NAD(P)H dehydrogenase (quinone); EC 1.6.5.2; 9032-20-6; menadione reductase; phylloquinone reductase; quinone reductase; dehydrogenase, reduced nicotinamide adenine dinucleotide (phosphate, quinone); DT-diaphorase; flavoprotein NAD(P)H-quinone reductase; menadione oxidoreductase; NAD(P)H dehydrogenase; NAD(P)H menadione reductase; NAD(P)H-quinone dehydrogenase; NAD(P)H-quinone oxidoreductase; NAD(P)H: (quinone-acceptor)oxidoreductase; NAD(P)H: menadione oxidoreductase; NADH-menadione reductase; naphthoquinone reductase; p-benzoquinone reductase; reduced NAD(P)H dehydrogenase; viologen accepting pyridine nucleotide oxidoreductase; vitamin K reductase; diaphorase; reduced nicotinamide-adenine dinucleotide (phosphate) dehy | |
| Native Bovine α-Chymotrypsinogen A | Chymotrypsinogen is a proteolytic enzyme and a precursor (zymogen) of the digestive enzyme chymotrypsin. It is a single polypetide chain consisting of 245 amino acid residues. It is synthesized in the acinar cells of the pancreas and stored inside membrane-bounded granules at the apex of the acinar cell. The cell is then stimulated by either a hormonal signal or a nerve impulse and the contents of the granules spill into a duct leading into the duodenum. Applications: The enzyme has been used in the non-invasive determination of solid-state protein conformation using near infrared (nir) spectroscopy. it has been used to study the partitioning of protein in polymer/polymer aqueous two-phase systems. the enzyme has also been used for self-interaction chromatography applications, to test the rapid measurement of protein osmotic second virial coefficients. in this technique, the protein is immobilized on chromatographic particles and its retention is measured using isocratic elution. Group: Zymogens. Synonyms: 9035-75-0; Chymotrypsinogen; α-Chymotrypsino. CAS No. 9035-75-0. Chymotrypsinogen A. Activity: > 40 units/mg solid. Storage: -20°C. Form: essentially salt-free, lyophilized powder. Source: Bovine Pancreas. Species: Bovine. 9035-75-0; Chymotrypsinogen; α-Chymotrypsinogen A; Chymotrypsinogen A; Chymotrypsin. Cat No: NATE-0748. | |
| Native Bovine Factor IXa β | Prepared from Bovine Factor IX by activation with Bovine Factor Xla, this Bovine Factor Xla is removed after activation. Complete activation is observed by SDS-PAGE. The Factor Xla activates FIX in a two-step reaction. In the first step, an internal Arg-Ala bond is cleaved, and in the second step, an Arg-Val bond is cleaved. The second cleavage leads to the liberation of an activation peptide from the NH2-terminal portion of the heavy chain to produce factor IXa&beta. Group: Enzymes. Synonyms: Bovine Factor IXa Beta; Factor IXa Beta; Factor Ixa. Factor IXa Beta. Mole weight: 43.9 kDa. Activity: 3096.00 PEU/mg. Storage: < -60°C. Source: Bovine. Species: Bovine. Bovine Factor IXa Beta; Factor IXa Beta; Factor Ixa. Cat No: NATE-0867. | |
| Native Bovine Trypsin Acetylated | Trypsin (EC 3.4.21.4) is a serine protease from the PA clan superfamily, found in the digestive system of many vertebrates, where it hydrolyses proteins. Trypsin is produced in the pancreas as the inactive protease trypsinogen. Trypsin cleaves peptide chains mainly at the carboxyl side of the amino acids lysine or arginine, except when either is followed by proline. It is used for numerous biotechnological processes. The process is commonly referred to as trypsin proteolysis or trypsinisation, and proteins that have been digested/treated with trypsin are said to have been trypsinized. The trypsin molecule has two domains: one is related to the enzyme active site and the trypt...e bacterial multidrug atp-binding cassette transporter. Group: Enzymes. Synonyms: α-trypsin; β-trypsin; cocoonase; parenzyme; parenzymol; tryptar; trypure; pseudotrypsin; tryptase; tripcellim; sperm receptor hydrolase; Alpha-trypsin; Beta-trypsin; EC 3.4.21.4; Trypsin; Acetyltrypsin. Enzyme Commission Number: EC 3.4.21.4. Trypsin. Activity: > 8,500 BAEE units/mg protein (biuret). Storage: -20°C. Source: Bovine pancreas. Species: Bovine. α-trypsin; β-trypsin; cocoonase; parenzyme; parenzymol; tryptar; trypure; pseudotrypsin; tryptase; tripcellim; sperm receptor hydrolase; Alpha-trypsin; Beta-trypsin; EC 3.4.21.4; Trypsin; Acetyltrypsin. Cat No: NATE-0720. | |
| Native Clostridium histolyticum Clostripain | Clostripain from Clostridium histolyticum is composed of two polypeptide chains, with molecular masses of 41.7 kDa and 15.4 kDa. Clostripain has a highly restricted substRate specificity for Arg-Xaa peptide bonds. Therefore, clostripain has been explored as a potential enzyme for protein sequencing purposes. It has also been studied as a catalyst for condensation of pharmaceutically important peptides containing Arg-Pro bonds. The isoelectric point of the enzyme is 4.8-4.9 (at 8°C), and optimum pH is 7.4~7.8 (against α-benzoyl-arginine ethyl ester). Group: Enzymes. Synonyms: clostridiopeptidase B; clostridium histolyticum proteinase B; α-clostridipain; clostridiopeptidase; Endoproteinase Arg-C; EC 3.4.22.8; 9028-00-6. Enzyme Commission Number: EC 3.4.22.8. CAS No. 9028-00-6. Kallikrein. Activity: > 20 units/mg solid. Storage: 2-8°C. Form: lyophilized powder. Source: Clostridium histolyticum. clostridiopeptidase B; clostridium histolyticum proteinase B; α-clostridipain; clostridiopeptidase; Endoproteinase Arg-C; EC 3.4.22.8; 9028-00-6. Cat No: NATE-0143. | |
| Native Hansenula 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. It employs one cofactor, FAD. Applications: Alcohol oxidase is used to catalyze the oxidation of short-chain, primary, aliphatic alcohols to their respective aldehydes. it may be used to study methanol metabolism is yeasts, such as candida, pichia, and hansenula. it is useful to study protein translocation into peroxisomes. Group: Enzymes. Synonyms: EC 1.1.3.13; 9073-63-6; alcohol oxidase; ethanol oxidase; Alcohol:oxygen oxidoreductase. Enzyme Commission Number: EC 1.1.3.13. CAS No. 9073-63-6. Mole weight: ~600 kDa. Activity: > 0.6 units/mg solid. Form: vacuum-dried powder. Source: Hansenula sp. EC 1.1.3.13; 9073-63-6; alcohol oxidase; ethanol oxidase; Alcohol:oxygen oxidoreductase. Cat No: NATE-0046. | |
| Native Human Cathepsin H | Cathepsin H is a protein that in humans is encoded by the CTSH gene. The protein encoded by this gene is a lysosomal cysteine proteinase important in the overall degradation of lysosomal proteins. It is composed of a dimer of disulfide-linked heavy and light chains, both produced from a single protein precursor. The encoded protein, which belongs to the peptidase C1 protein family, can act both as an aminopeptidase and as an endopeptidase. Increased expression of this gene has been correlated with malignant progression of prostate tumors. Two transcript variants encoding different isoforms have been found for this gene. Group: Enzymes. Synonyms: CTSH; cathepsin H; CPSB; ACC-4; ACC-5; ACC4; ACC5; CPSB; minichain. Purity: > 95% (SDS-PAGE). CTSH. Mole weight: 28 kDa. Storage: -40°C. Form: Liquid. Source: Human Liver. Species: Human. CTSH; cathepsin H; CPSB; ACC-4; ACC-5; ACC4; ACC5; CPSB; minichain. Cat No: NATE-0176. | |
| Native Human Creatine Kinase MM Fraction | 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: May be used as a control or calibrator in monitoring myoc...stoperative cardiac medical therapy in emergency coronary artery bypass grafting for acute myocardial infarction. creatine kinase mm fraction from human heart has also been used in a study to investigate the circadian dependence of infarct size and left ventricular function after st slevation myocardial infarction. Group: Enzymes. Synonyms: CKM; creatine kinase, muscle; CKMM; creatine kinase M-type; creatine kinase-M; creatine kinase M chain; M-CK; MM-CK. Activity: > 200 U/mg. Form: lyophilized powder. Source: Human heart. Species: Human. CKM; creatine kinase, muscle; CKMM; creatine kinase M-type; creatine kinase-M; creatine kinase M chain; M-CK; MM-CK. Cat No: NATE-0142. | |
| Native Human Elastase | Neutrophil elastase is a serine proteinase in the same family as chymotrypsin and has broad substrate specificity. Secreted by neutrophils and macrophages during inflammation, it destroys bacteria and host tissue. It also localizes to Neutrophil extracellular traps (NETs), via its high affinity for DNA, an unusual property for serine proteases. Leuk ocyte elastase is a 29 kda serine endoprotease of the proteinase s1 family. it exists as a single 238 amino acid-peptide chain with four disulfide bonds. it contains two or thee n-linked glycans of variable composition which account for its three major isoforms. Applications: Elastase from creative enzymes has been used to digest fibro...mal models. Group: Enzymes. Synonyms: ELANE; elastase; EC 3.4.21.37; leukocyte elastase; ELA2; elastase 2; neutrophil elaszym; serine elastase; lysosomal elastase; neutrophil elastase; polymorphonuclear leukocyte elastase; elaszym; granulocyte elastase. Enzyme Commission Number: EC 3.4.21.37. CAS No. 9004-6-2. ELA2. Mole weight: 29 kDa. Activity: > 50 units/mg protein (Bradford). Storage: -20°C. Form: Lyophilized from 0.05 M sodium acetate (pH 5.5) and 0.6 M NaCl. Source: Human leuk ocytes. Species: Human. ELANE; elastase; EC 3.4.21.37; leukocyte elastase; ELA2; elastase 2; neutrophil elaszym; serine elastase; lysosomal elastase; neutrophil elastase; polymorphonuclear leukocyte ela | |
| Native Human Factor IXa β | Prepared from Human Factor IX by activation with Bovine Factor XIa. This Bovine Factor XIa is removed after activation. Complete activation is observed by SDS-PAGE. The Factor XIa activates Factor IX in a two-step reaction. In the first step, an internal Arg-Ala bond is cleaved, and in the second step, an Arg-Val bond is cleaved. The second cleavage leads to the liberation of an activation peptide from the NH2-terminal portion of the heavy chain to produce Factor IXa&beta. Group: Enzymes. Synonyms: Human Factor IXa Beta; Factor IXa Beta; Factor IXa. Factor IXa Beta. Mole weight: 45 kDa. Activity: 12500.00 PEU/mg. Storage: < -60°C. Source: Human. Species: Human. Human Factor IXa Beta; Factor IXa Beta; Factor IXa. Cat No: NATE-0883. | |
| Native Mouse Creatine Kinase MM | 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. Group: Enzymes. Synonyms: CKM; creatine kinase, muscle; CKMM; creatine kinase M-type; creatine kinase-M; creatine kinase M chain; CK-MM. Purity: > 90% (SDS-PAGE). CK. Mole weight: 43 kDa. Storage: Store at -20° C. Form: Liquid, 50% Glycerol, 50 mM TrisCl, 2.5 mM b-mercaptoethanol, 0.05% NaN3. Source: Mouse Skeletal Muscle. Species: Mouse. CKM; creatine kinase, muscle; CKMM; creatine kinase M-type; creatine kinase-M; creatine kinase M chain; CK-MM. Cat No: NATE-1887. | |
| Native Mouse Endoproteinase Arg-C | An Endoglycosidase is an enzyme that releases oligosaccharides from glycoproteins or glycolipids. It may also cleave polysaccharide chains between residues that are not the terminal residue, although releasing oligosaccharides from conjugated protein and lipid molecules is more common. It breaks the glycosidic bonds between two sugar monomer in the polymer. It is different from exoglycosidase that it does not do so at the terminal residue. Hence, it is used to release long carbohydrates from conjugated molecules. If an exoglycosidase were used, every monomer in the polymer would have to be removed, one by one from the chain, taking a long time. An endoglycosidase cleaves, giving a polymeric product. Group: Enzymes. Synonyms: EC 3.4.21.35; glandular kallikrein; pancreatic kallikrein; submandibular. Enzyme Commission Number: EC 3.4.21.35. CAS No. 82047-85-6. Kallikrein. Storage: -20°C. Form: lyophilized powder. Source: Mouse submaxillary gland. Species: Mouse. EC 3.4.21.35; glandular kallikrein; pancreatic kallikrein; submandibular kallikrein; submaxillary kallikrein; kidney kallikrein; urinary kallikrein; kallikrein; salivary kallikrein; kininogenin; kininogenase; callicrein; glumorin; padreatin; padutin; kallidinogenase; bradykininogenase; depot-padutin; urokallikrein; dilminal D; onokrein P; 82047-85-6. Pack: vial of 5 μg. Cat No: NATE-0218. | |
| Native Porcine Creatine Kinase MM | 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. Mole weight: 43 kDa. Stability: 2 years. Storage: Store at -20°C. Form: Liquid; 50% Glycerol, 50 mM TrisCl, 2.5 mM b-mercaptoethanol, 0.05% NaN3. Source: Porcine Skeletal Muscle. Species: Porcine. CKM; creatine kinase, muscle; CKMM; creatine kinase M-type; creatine kinase-M; creatine kinase M chain; M-CK; MM-CK. Cat No: NATE-0959. | |
| Native Porcine Lipoamide Dehydrogenase | Lipoamide dehydrogenase (or diaphorase) catalyzes the following reaction: Lipoamide + NADH + H+ ? Dihydrolipoamide + NAD+. The enzyme occurs in mammalian and microbial cells and it catalyzes a number of reactions which involve NAD+ or NADH. Lipoamide dehydrogenase from porcine heart contains two polypeptide chains which are similar. It has two molecules of tightly bound flavin adenine dinucleotide (FAD). The molecular weight of the porcine heart enzyme is between 100,000 and 114,000. Group: Enzymes. Synonyms: NADH: lipoamide oxidoreductase; EC 1.6.4.3; Lipoamide Dehydrogenase; LD. Enzyme Commission Number: EC 1.6.4.3. LD. Mole weight: 100-114 kDa. Activity: 25 U/mg protein. Stability: Store at -20°C (-4°F). Form: Freeze-dried powder. Source: Porcine Heart. Species: Porcine. NADH: lipoamide oxidoreductase; EC 1.6.4.3; Lipoamide Dehydrogenase; LD. Cat No: NATE-0894. | |
| Native Pseudomonas fragi Acyl-CoA 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. Acs is an enzyme produced by microorganisms. this product shall be used for a diagnostics reagent. Applications: Useful in the enzymatic determination of fatty acid when coupled with acyl-coa oxidase. Group: Enzymes. Synonyms: EC 6.2.1.3; ACS; acyl-CoA synthetase; fatty acid thiokinase (long chain. Enzyme Commission Number: EC 6.2.1.3. CAS No. 9013-18-7. ACS3. Mole weight: 60 kDa (Sephadex G-150) SDS-PAGE 62 kDa. Activity: 2-8 U/mg. Stability: At least one year at-20°C. Appearance: White powder. Storage: Keep in freezer (-20°C to-80°C), dry place in well-closed containers and away from direct sun light). Form: Freeze dried powder. Source: Pseudomonas fragi. EC 6.2.1.3; ACS; acyl-CoA synthetase; fatty acid thiokinase (long chain); acyl-activating enzyme; palmitoyl-CoA synthase; lignoceroyl-CoA synthase; arachidonyl-CoA synthetase; ac | |
| 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 Rat Creatine Kinase MM | 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 Thermus flavus Malic Dehydrogenase | Malic dehydrogenase (MDH) exists as two isoforms within eukaryotic cells, one that is expressed in the mitochondria and functions in the TCA cycle and one in the cytoplasm that converts malate from the mitochondria back into oxaloacetate. Malic dehydrogenase from thermus flavus is stable and active at 90 oc. Applications: Malic dehydrogenase has been used in a study to assess electron transport chain activity in mit ochondria from human skeletal muscle. it has also been used in a study to investigate activities of enzymes and ammonia in serum of rats with fluoride hyperglycemia. Group: Enzymes. Synonyms: malic dehydrogenase; L-malate dehydrogenase; NAD-L-malate dehydrogenase; malic acid dehydrogenase; NAD-dependent malic dehydrogenase; NAD-malate dehydrogenase; NAD-malic deh. Enzyme Commission Number: EC 1.1.1.37. CAS No. 9001-64-3. MDH. Activity: > 50 units/mg solid. Storage: -20°C. Form: lyophilized powder; Contains dextran. Source: Thermus flavus. malic dehydrogenase; L-malate dehydrogenase; NAD-L-malate dehydrogenase; malic acid dehydrogenase; NAD-dependent malic dehydrogenase; NAD-malate dehydrogenase; NAD-malic dehydrogenase; malate (NAD) dehydrogenase; NAD-dependent malate dehydrogenase; NAD-specific malate dehydrogenase; NAD-linked malate dehydrogenase; MDH; L-malate-NAD+ oxidoreductase; EC 1.1.1.37; 9001-64-3. Cat No: NATE-0448. | |
| nicotinate dehydrogenase (cytochrome) | This two-component enzyme from Pseudomonas belongs to the family of xanthine dehydrogenases, but differs from most other members of this family. While most members contain an FAD cofactor, the large subunit of this enzyme contains three c-type cytochromes, enabling it to interact with the electron transfer chain, probably by delivering the electrons to a cytochrome oxidase. The small subunit contains a typical molybdopterin cytosine dinucleotide(MCD) cofactor and two [2Fe-2S] clusters. Group: Enzymes. Synonyms: nicotinic acid hydroxylase; nicotinate hydroxylase. Enzyme Commission Number: EC 1.17.2.1. 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-1085; nicotinate dehydrogenase (cytochrome); EC 1.17.2.1; nicotinic acid hydroxylase; nicotinate hydroxylase. Cat No: EXWM-1085. | |
| plus-end-directed kinesin ATPase | Microtubular motor protein, involved in organelle movement, in mitosis and meiosis. In contrast to dynein, it moves along microtubules towards the plus end. Composed of two heavy (α) chains (110 kDa) and two or more light (β) chains (65-75 kDa). Also hydrolyses GTP. Group: Enzymes. Synonyms: kinesin. Enzyme Commission Number: EC 3.6.4.4. 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-4706; plus-end-directed kinesin ATPase; EC 3.6.4.4; kinesin. Cat No: EXWM-4706. | |
| poly(3-hydroxybutyrate) depolymerase | Reaction also occurs with esters of other short-chain-length (C1-C5) hydroxyalkanoic acids (HA). There are two types of polymers: native (intracellular) granules are amorphous and have an intact surface layer; denatured (extracellular) granules either have no surface layer or a damaged surface layer and are partially crystalline. Group: Enzymes. Synonyms: PHB depolymerase; poly(3HB) depolymerase; poly[(R)-hydroxyalkanoic acid] depolymerase; poly(HA) depolymerase; poly(HASCL) depolymerase; poly[(R)-3-hydroxybutyrate] hydrolase. Enzyme Commission Number: EC 3.1.1.75. CAS No. 9014-11-3. 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-3503; poly(3-hydroxybutyrate) depolymerase; EC 3.1.1.75; 9014-11-3; PHB depolymerase; poly(3HB) depolymerase; poly[(R)-hydroxyalkanoic acid] depolymerase; poly(HA) depolymerase; poly(HASCL) depolymerase; poly[(R)-3-hydroxybutyrate] hydrolase. Cat No: EXWM-3503. | |
| Pro-Urokinase from Human, recombinant | Urokinase or Urokinase-type plasminogen activator (uPA) is a serine protease (EC 3.4.21.73). It is secreted as a single-chain zymogen, pro-Urokinase, possessing little or no intrinsic enzymatic activity. The single chain zymogen is converted into the active two chain enzyme (tcuPA) by cleavage of the bond between Lys157 and Ile158. After activation, Urokinase specifically cleaves the proenzyme plasminogen to form the active enzyme plasmin. The active plasmin then catalyzes the breakdown of fibrin polymers of blood clots. Urokinase is involved in a number of biological functions including fibrinolysis, embryogenesis, cell migration, tissue remodeling, ovulation, and wound healing. Additionally, it is a potent marker of invasion and metastasis in a variety of human cancers associated with breast, stomach, colon, bladder, ovary, brain and endometrium. Group: Enzymes. Synonyms: Single chain Urokinase-type plasminogen activator; s. Purity: > 90% by SDS-PAGE. Pro-Urokinase. Mole weight: 49.3 kDa. Activity: >1200 mU/mg. Storage: Stable at -80°C for at least 1 year as supplied. Store reconstituted aliquots at -80°C. Avoid repeated freeze and thaw cycles. Form: Lyophilized powder. Source: E. coli. Species: Human. Single chain Urokinase-type plasminogen activator; scuPA; Urokinase-type Plasminogen Activator uPA; PLAU; Pro-Urokinase. Cat No: NATE-1689. | |
| quinol-cytochrome-c reductase | The enzyme, often referred to as the cytochrome bc1 complex or complex III, is the third complex in the electron transport chain. It is present in the mitochondria of all aerobic eukaryotes and in the inner membranes of most bacteria. The mammalian enzyme contains cytochromes b-562, b-566 and c1, and a 2-iron ferredoxin. Depending on the organism and physiological conditions, the enzyme extrudes either two or four protons from the cytoplasmic to the non-cytoplasmic compartment (cf. EC 1.6.99.3, NADH dehydrogenase). Group: Enzymes. Synonyms: ubiquinol-cytochrome-c reductase; coenzyme Q-cytochrome c reductase; dihydrocoenzyme Q-cytochrome c reductase; reduced ubiquinone-cytochrome c reductase; complex III (mitocho. Enzyme Commission Number: EC 1.10.2.2. CAS No. 9027-3-6. 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-0474; quinol-cytochrome-c reductase; EC 1.10.2.2; 9027-03-6; ubiquinol-cytochrome-c reductase; coenzyme Q-cytochrome c reductase; dihydrocoenzyme Q-cytochrome c reductase; reduced ubiquinone-cytochrome c reductase; complex III (mitochondrial electron transport); ubiquinone-cytochrome c reductase; ubiquinol-cytochrome c oxidoreductase; reduced coenzyme Q-cytochrome c reductase; ubiquinone-cytochrome c oxidoreductase; reduced ubiquinone-cytochrome c oxido | |
| Recombinant Ketol-acid reductoisomerase from Mycobacterium tuberculosis | Ketol-acid reductoisomerase catalyzes two steps in the biosynthesis of branched-chain amino acids. Group: Enzymes. Synonyms: dihydroxyisovalerate dehydrogenase (isomerizing); acetohydroxy acid isomeroreductase; ketol acid reductoisomerase; alpha-keto-beta-hydroxylacyl reductoisomerase; 2-hydroxy-3-keto acid reductoisomerase; acetohydroxy acid reductoisomerase; acetolactate reductoisomerase; dihydroxyisovalerate (isomerizing) dehydrogenase; isomeroreductase; reductoisomerase; EC 1.1.1.86. Enzyme Commission Number: EC 1.1.1.86. CAS No. 9075-2-9. Purity: > 80 %. Ketol-acid reductoisomerase. Mole weight: 38 kDa. Appearance: Colourless clear liquid. Storage: Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C. Source: E. coli. Species: Mycobacterium tuberculosis. dihydroxyisovalerate dehydrogenase (isomerizing); acetohydroxy acid isomeroreductase; ketol acid reductoisomerase; alpha-keto-beta-hydroxylacyl reductoisomerase; 2-hydroxy-3-keto acid reductoisomerase; acetohydroxy acid reductoisomerase; acetolactate reductoisomerase; dihydroxyisovalerate (isomerizing) dehydrogenase; isomeroreductase; reductoisomerase; EC 1.1.1.86. Cat No: NATE-1016. | |
| (S)-2-hydroxy-acid oxidase | A flavoprotein (FMN). Exists as two major isoenzymes; the A form preferentially oxidizes short-chain aliphatic hydroxy acids, and was previously listed as EC 1.1.3.1, glycolate oxidase; the B form preferentially oxidizes long-chain and aromatic hydroxy acids. The rat isoenzyme B also acts as EC 1.4.3.2, L-amino-acid oxidase. Group: Enzymes. Synonyms: hydroxy-acid oxidase A; hydroxy-acid oxidase B; glycolate oxidase; L-2-hydroxy acid oxidase; hydroxyacid oxidase A; L-α-hydroxy acid oxidase. Enzyme Commission Number: EC 1.1.3.15. CAS No. 9028-71-1. 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-0397; (S)-2-hydroxy-acid oxidase; EC 1.1.3.15; 9028-71-1; hydroxy-acid oxidase A; hydroxy-acid oxidase B; glycolate oxidase; L-2-hydroxy acid oxidase; hydroxyacid oxidase A; L-α-hydroxy acid oxidase. Cat No: EXWM-0397. | |
| (S)-3-amino-2-methylpropionate transaminase | Also acts on β-alanine and other ω-amino acids having carbon chains between 2 and 5. The two enantiomers of the 2-methyl-3-oxopropanoate formed by the enzyme interconvert by enolization, so that this enzyme, together with EC 2.6.1.40, (R)-3-amino-2-methylpropionate-pyruvate transaminase, provide a route for interconversion of the enantiomers of 3-amino-2-methylpropanoate. Group: Enzymes. Synonyms: L-3-aminoisobutyrate transaminase; β-aminobutyric transaminase; L-3-aminoisobutyric aminotransferase; β-aminoisobutyrate-α-ketoglutarate transaminase. Enzyme Commission Number: EC 2.6.1.22. CAS No. 9031-95-2. 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-2862; (S)-3-amino-2-methylpropionate transaminase; EC 2.6.1.22; 9031-95-2; L-3-aminoisobutyrate transaminase; β-aminobutyric transaminase; L-3-aminoisobutyric aminotransferase; β-aminoisobutyrate-α-ketoglutarate transaminase. Cat No: EXWM-2862. | |
| short-chain acyl-CoA dehydrogenase | Contains FAD as prosthetic group. One of several enzymes that catalyse the first step in fatty acids β-oxidation. The enzyme catalyses the oxidation of saturated short-chain acyl-CoA thioesters to give a trans 2,3-unsaturated product by removal of the two pro-R-hydrogen atoms. The enzyme from beef liver accepts substrates with acyl chain lengths of 3 to 8 carbon atoms. The highest activity was reported with either butanoyl-CoA or pentanoyl-CoA. The enzyme from rat has only 10% activity with hexanoyl-CoA (compared to butanoyl-CoA) and no activity with octanoyl-CoA. cf. EC 1.3.8.7, medium-chain acyl-CoA dehydrogenase, EC 1.3.8.8, long-chain acyl-CoA dehydrogenase, and EC ...name). Enzyme Commission Number: EC 1.3.8.1. CAS No. 9027-88-7. 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-1405; short-chain acyl-CoA dehydrogenase; EC 1.3.8.1; 9027-88-7; butyryl-CoA dehydrogenase; butanoyl-CoA dehydrogenase; butyryl dehydrogenase; unsaturated acyl-CoA reductase; ethylene reductase; enoyl-coenzyme A reductase; unsaturated acyl coenzyme A reductase; butyryl coenzyme A dehydrogenase; short-chain acyl CoA dehydrogenase; short-chain acyl-coenzyme A dehydrogenase; 3-hydroxyacyl CoA reductase; butanoyl-CoA:(acceptor) 2,3-oxidoreductase; ACADS (gene name). Cat No: EXWM-1405. | |
| TDP-4-oxo-6-deoxy-α-D-glucose-3,4-oxoisomerase (dTDP-3-dehydro-6-deoxy-α-D-galactopyranose-forming) | The enzyme is involved in the biosynthesis of dTDP-3-acetamido-3,6-dideoxy-α-D-galactose. Four moieties of α-D-rhamnose and two moities of 3-acetamido-3,6-dideoxy-α-D-galactose form the repeating unit of the glycan chain in the S-layer of the bacterium Aneurinibacillus thermoaerophilus. Group: Enzymes. Synonyms: dTDP-6-deoxy-hex-4-ulose isomerase; TDP-6-deoxy-hex-4-ulose isomerase; FdtA. Enzyme Commission Number: EC 5.3.2.3. 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-5483; TDP-4-oxo-6-deoxy-α-D-glucose-3,4-oxoisomerase (dTDP-3-dehydro-6-deoxy-α-D-galactopyranose-forming); EC 5.3.2.3; dTDP-6-deoxy-hex-4-ulose isomerase; TDP-6-deoxy-hex-4-ulose isomerase; FdtA. Cat No: EXWM-5483. | |
| Tissue plasminogen activator from Human, Recombinant | Tissue plasminogen activator (abbreviated PLAT or tPA) is a secreted serine proteasewhich converts the proenzymeplasminogento plasmin, a fibrinolyticenzyme. Plasminogen is synthesized as a single chain which is cleaved by PLAT into the two chain disulfide linked plasmin. This enzyme plays a role in cell migrationand tissue remodeling. Increased enzymatic activity causes hyperfibrinolysis, which manifests as excessive bleeding; decreased activity leads to hypofibrinolysiswhich can result in thrombosisor embolism. Tissue plasminogen activator human recombinant produced in cho cells is a single, glycosylated polypeptide chain containing 527 amino acids and having a mol...0% as determined by (a) Analysis by RP-HPLC. (b) Analysis by SDS-PAGE. tPA. Mole weight: 59008.71 Da. Activity: 580,000 IU/mg. Stability: Lyophilized t-PA although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution tPA should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles. Appearance: Sterile Filtered White lyophilized (freeze-dried) powder. Source: CHO. Species: Human. Tissue-type plasminogen activator; EC 3.4.21.68; tPA; t-PA; t-plasminogen activator; TPA; T-PA. Cat No: NATE-0920. | |
| t-plasminogen activator | A peptidase of family S1 (trypsin family) from a wide variety of mammalian tissues, especially endothelial cells. Secreted as a single chain precursor which is cleaved to a two-chain form by plasmin. Activity is considerably enhanced by fibrin. Formerly included in EC 3.4.21.31 and EC 3.4.99.26. Group: Enzymes. Synonyms: tissue plasminogen activator; plasminogen activator, tissue-type; tissue-type plasminogen activator; tPA; t-PA. Enzyme Commission Number: EC 3.4.21.68. CAS No. 139639-23-9. tPA. 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-4159; t-plasminogen activator; EC 3.4.21.68; 139639-23-9; tissue plasminogen activator; plasminogen activator, tissue-type; tissue-type plasminogen activator; tPA; t-PA. Cat No: EXWM-4159. | |
| Transglutaminase from Mouse, Recombinant | This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a phosphate group as acceptor. Applications: Recombinant mouse transglutaminase is a homodimer (a2) composed of two chains held together by non covalent bonds. after activation of the zymogen by thrombin and ca2+ to its active form (a*2, factor xiiia), factor xiiia catalyzes the formation of covalent bridges (ε-(γ-glutamyl) lysine bonds) between fibrin units to increase the elasticity of the clot network. the resulting cross-linked fibrin is insoluble and resistant to lysis. Group: Enzymes. Synonyms: transglutaminase; EC ...ng to Lorand et al., Anal. Biochem. 44 (221-231)]. Appearance: Liquid. Storage: Store working aliquots at ≤ - 20°C. Avoid repeated freezing and thawing. Form: The transglutaminase is formulated in 10 mM Sodium Phosphate pH 8.0, 15 mM NaCl. Sample contains 50% glycerol. Biotinylated-transglutaminase is a Ca2+-dependent enzyme. Source: Insect cells. Species: Mouse. transglutaminase; EC 2.3.2.13; 80146-85-6; transglutaminase; Factor XIIIa; fibrinoligase; fibrin stabilizing factor; glutaminylpeptide γ-glutamyltransferase; polyamine transglutaminase; tissue transglutaminase; R-glutaminyl-peptide:amine γ-glutamyl transferase; protein-glutamine γ-glutamyltra | |
| u-plasminogen activator | Formed from the inactive precursor by action of plasmin or plasma kallikrein. Differs in structure from t-plasminogen activator (EC 3.4.21.68), and does not bind to fibrin. In peptidase family S1 (trypsin family). Formerly included in EC 3.4.21.31 and EC 3.4.99.26. Group: Enzymes. Synonyms: urokinase; urinary plasminogen activator; cellular plasminogen activator; urokinase-type plasminogen activator; double-chain urokinase-type plasminogen activator; two-chain urokinase-type plasminogen activator; urokinase plasminogen activator; uPA; u-PA; abbokinase; urinary esterase A. Enzyme Commission Number: EC 3.4.21.73. CAS No. 9039-53-6. uPA. 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-4165; u-plasminogen activator; EC 3.4.21.73; 9039-53-6; urokinase; urinary plasminogen activator; cellular plasminogen activator; urokinase-type plasminogen activator; double-chain urokinase-type plasminogen activator; two-chain urokinase-type plasminogen activator; urokinase plasminogen activator; uPA; u-PA; abbokinase; urinary esterase A. Cat No: EXWM-4165. | |
| Urokinase from Human, recombinant | Urokinase or Urokinase-type plasminogen activator (uPA) is a serine protease (EC 3.4.21.73). It is secreted as a single-chain zymogen, pro-Urokinase, possessing little or no intrinsic enzymatic activity. The single chain zymogen is converted into the active two chain enzyme (tcuPA) by cleavage of the bond between Lys157 and Ile158. After activation, Urokinase specifically cleaves the proenzyme plasminogen to form the active enzyme plasmin. The active plasmin then catalyzes the breakdown of fibrin polymers of blood clots. Urokinase is involved in a number of biological functions including fibrinolysis, embryogenesis, cell migration, tissue remodeling, ovulation, and wound healing. Additionally, it is a potent marker of invasion and metastasis in a variety of human cancers associated with breast, stomach, colon, bladder, ovary, brain and endometrium. Group: Enzymes. Synonyms: Two chain urokinase-type plasminogen acti. Enzyme Commission Number: EC 3.4.21.73. Purity: > 90% by SDS-PAGE. uPA. Mole weight: 49.3 kDa. Activity: >1500 mU/mg. Storage: Stable at -80°C for at least 1 year as supplied. Store reconstituted aliquots at -80°C. Avoid repeated freeze and thaw cycles. Form: Lyophilized powder. Source: E. coli. Species: Human. Two chain urokinase-type plasminogen activator; tcuPA; PLAU; ATF; UPA; URK; u-PA; BDPLT5; QPD; Urokinase. Cat No: NATE-1690. | |
| xylose isomerase | Contains two divalent metal ions, preferably magnesium, located at different metal-binding sites within the active site. The enzyme catalyses the interconversion of aldose and ketose sugars with broad substrate specificity. The enzyme binds the closed form of its sugar substrate (in the case of glucose, only the α anomer) and catalyses ring opening to generate a form of open-chain conformation that is coordinated to one of the metal sites. Isomerization proceeds via a hydride-shift mechanism. Group: Enzymes. Synonyms: D-xylose isomerase; D-xylose ketoisomerase; D-xylose ketol-isomerase. Enzyme Commission Number: EC 5.3.1.5. CAS No. 9023-82-9. Glucose Isomerase. 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-5476; xylose isomerase; EC 5.3.1.5; 9023-82-9; D-xylose isomerase; D-xylose ketoisomerase; D-xylose ketol-isomerase. Cat No: EXWM-5476. | |
| Bovine factor IX | The zymogen factor IX is a single chain vitamin K-dependent glycoprotein which is synthesized in the liver. The domain structure of factor IX is similar to that of the other vitamin K dependent coagulation factors. The NH2-terminal region contains 12 γ-carboxyglutamic acid (gla) residues which facilitate the calcium dependent binding of factor IX to negatively charged phospholipid surfaces. Two domains which are homologous to epidermal growth factor (EGF) span the region between the NH2-terminal gla domain and the activation peptide (Ala-146 to Arg-180).Factor IX is activated by either factor XIa or the factor VIIa/tissue factor/phospholipid complex. Cleavage at site A (see fig... activates factor X to factor Xa.Human factor IX is prepared from fresh frozen plasma by a combination of conventional procedures and immunoaffinity chromatography. Bovine factor IX is prepared from fresh citrated bovine plasma by a modification of the method described by Fujikawa et al. The purified proteins are supplied in 50% (vol/vol) glycerol/H2O and should be stored at -20°C. Purity is determined by SDS-PAGE analysis and activity is measured using a factor IX clotting assay. Group: Zymogens. CAS No. 9001-28-9. Purity: >95% by SDS-PAGE. Factor IX. Mole weight: 55400. Stability: 12 months. Storage: -20°C. Source: Bovine. Bovine factor IX; Factor IX. Pack: 100 ug. Cat No: CZY-003. | |
| Bovine Factor X | Factor X is a vitamin K-dependent protein zymogen which is synthesized in the liver and circulates in plasma as a two chain molecule linked by a disulfide bond. Prior to secretion into plasma, post-translational modifications produce 11 gamma-carboxyglutamic acid (gla) residues and a single b-hydroxyaspartic acid residue, which are located within the NH2-terminal light chain. The light chain also contains two epidermal growth factor (EGF) homology domains. The COOH-terminal heavy chain of factor X contains most of the carbohydrate moieties, as well as the latent serine protease domain. The activation of factor X is catalyzed by either the intrinsic factor Xase complex (factor IXa, fa...y of the prothrombinase complex. The first EGF homology domain contains a Ca2+ binding site which acts as a hinge to fold the EGF and GLA domains towards each other. This region of the molecule is involved in the recognition of cellular binding domains.Human factor X is isolated from fresh frozen human plasma by a combination of conventional techniques and immunoaffinity chromatography. In addition to the standard human factor X preparation, Gla-domainless human factor X is also available. Bovine factor X is isolated from fresh bovine plasma using a modification of the procedure reported by Bajaj et al. The purified zymogen is supplied in 50% (vol/vol) glycerol/H2O and should be store | |
| Bovine glu-Plasminogen | Plasminogen is a single chain glycoprotein zymogen which is synthesized in the liver and circulates in plasma at a concentration of approximately 2.4 uM. The plasminogen molecule contains 790 amino acids, 24 disulfide bridges, no free sulfhydryls and 5 regions of internal sequence homology, known as kringles, between Lys77 and Arg560. These five triple-looped, three disulfide bridged, kringle regions are homologous to the kringle domains in t-PA, u-PA and prothrombin. Plasminogen contains one high affinity (Kd=9x10-6M) and four low affinity (Kd=5x10-3M) lysine binding sites. The high affinity binding site resides within the first kringle region of plasminogen. The interaction of p...hich remain covalently associated by a disulfide bond.Native glu-plasminogen is prepared from fresh frozen human plasma by a modification of the procedure of Castellino, utilizing gel filtration and affinity chromatography. The two carbohydrate variants of glu-plasminogen (CHOI and CHOII) are isolated by gradient elution from lysine-Sepharose using the lysine analog, e-aminocaproic acid. The plasminogen is supplied in 50% (vol/vol) glycerol/H2O for storage at -20°C. Purity is determined by SDS-PAGE analysis. Group: Zymogens. Purity: >95% by SDS-PAGE. Plasminogen. Stability: 12 months. Storage: -20°C. Source: Bovine. Bovine glu-Plasminogen; Plasminogen. Pack: 1 mg. Cat No: CZY-015. | |
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