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| Product | Description | |
|---|---|---|
| leucine transaminase | A pyridoxal-phosphate protein. This enzyme differs from EC 2.6.1.42, branched-chain-amino-acid transaminase, in that it does not act on L-valine or L-isoleucine, although it does act on L-methionine. The mitochondrial form from rat liver differs in physical characteristics from the cytoplasmic form. Group: Enzymes. Synonyms: L-leucine aminotransferase; leucine 2-oxoglutarate transaminase; leucine aminotransferase; leucine-α-ketoglutarate transaminase. Enzyme Commission Number: EC 2.6.1.6. CAS No. 9030-37-9. 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-2901; leucine transaminase; EC 2.6.1.6; 9030-37-9; L-leucine aminotransferase; leucine 2-oxoglutarate transaminase; leucine aminotransferase; leucine-α-ketoglutarate transaminase. Cat No: EXWM-2901. |  |
| 2-aminohexanoate transaminase | A pyridoxal-phosphate protein. Also acts on L-leucine and, more slowly, on L-isoleucine, L-2-aminopentanoate and L-aspartate. Group: Enzymes. Synonyms: norleucine transaminase; norleucine (leucine) aminotransferase; leucine L-norleucine: 2-oxoglutarate aminotransferase. Enzyme Commission Number: EC 2.6.1.67. CAS No. 111310-35-1. 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-2908; 2-aminohexanoate transaminase; EC 2.6.1.67; 111310-35-1; norleucine transaminase; norleucine (leucine) aminotransferase; leucine L-norleucine: 2-oxoglutarate aminotransferase. Cat No: EXWM-2908. | |
| 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) | Contains thiamine diphosphate. It acts not only on 3-methyl-2-oxobutanaoate, but also on 4-methyl-2-oxopentanoate and (S)-3-methyl-2-oxopentanoate, so that it acts on the 2-oxo acids that derive from the action of transaminases on valine, leucine and isoleucine. It is a component of the multienzyme 3-methyl-2-oxobutanoate dehydrogenase complex in which multiple copies of it are bound to a core of molecules of EC 2.3.1.168, dihydrolipoyllysine-residue (2-methylpropanoyl)transferase, which also binds multiple copies of EC 1.8.1.4, dihydrolipoyl dehydrogenase. It does not act on free lipoamide or lipoyllysine, but only on the lipoyllysine residue in EC 2.3.1.168. Group: Enzymes. Synonyms: 2-oxoisocaproate dehydrogenase; 2-oxoisovalerate (lipoate) dehydrogenase; 3-methyl-2-oxobutanoate dehydrogenase (lipoamide); 3-methyl-2-oxobutanoate:lipoamide oxidoreductase (decarboxylating and acceptor-2-methylpropanoylating); α-keto-α-methylvalerate dehydrogenase; α. Enzyme Commission Number: EC 1.2.4.4. CAS No. 9082-72-8. 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-1219; 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring); EC 1.2.4.4; 9082-72-8; 2-oxoisocaproate dehydrogenase; 2-oxoisovalerate (lipo | |
| alanine-oxo-acid transaminase | A pyridoxal-phosphate protein. Group: Enzymes. Synonyms: L-alanine-α-keto acid aminotransferase; leucine-alanine transaminase; alanine-keto acid aminotransferase; alanine-oxo acid aminotransferase. Enzyme Commission Number: EC 2.6.1.12. CAS No. 9030-41-5. 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-2852; alanine-oxo-acid transaminase; EC 2.6.1.12; 9030-41-5; L-alanine-α-keto acid aminotransferase; leucine-alanine transaminase; alanine-keto acid aminotransferase; alanine-oxo acid aminotransferase. Cat No: EXWM-2852. | |
| Alanine-Valine transaminase (Crude Enzyme) | Branched chain aminotransferase is an aminotransferase enzyme which acts upon branched-chain amino acids. It uses largely α-ketoglutarate in forming branched chain α-keto acids and glutamate. The biological function of branched chain aminotransferases (BCAT) is to catalyse the synthesis or degradation of the branched chain amino acids leucine, isoleucine, and valine. In humans, branched chain amino acids are essential and are degraded by BCATs. This product with the indicated enzyme activity was briefly purified from engineered E. coli. Applications: Nutrition. Group: Enzymes. Synonyms: Transaminase B; branched-chain amino acid aminotransferase; branched-chain amino acid-glutamate Transaminase; branched-chain aminotransferase; L-branched chain amino acid aminotransferase; glutamate-branched-chain amino acid Transaminase. Enzyme Commission Number: EC 2.6.1.42. CAS No. 9054-65-3. Activity: Undetermined. Appearance: Clear to translucent yellow solution. Storage: at -20 °C or lower, for at least 1 month. Source: E. coli. Transaminase B; branched-chain amino acid aminotransferase; branched-chain amino acid-glutamate Transaminase; branched-chain aminotransferase; L-branched chain amino acid aminotransferase; glutamate-branched-chain amino acid Transaminase. Pack: 100ml. Cat No: NATE-1821. | |
| arginine-pyruvate transaminase | A pyridoxal-phosphate protein. While L-arginine is the best substrate, the enzyme exhibits broad substrate specificity, with L-lysine, L-methionine, L-leucine, L-ornithine and L-glutamine also able to act as substrates, but more slowly. Pyruvate cannot be replaced by 2-oxoglutarate as amino-group acceptor. This is the first catalytic enzyme of the arginine transaminase pathway for L-arginine utilization in Pseudomonas aeruginosa. This pathway is only used when the major route of arginine catabolism, i.e. the arginine succinyltransferase pathway, is blocked. Group: Enzymes. Synonyms: arginine:pyruvate transaminase; AruH; ATase. Enzyme Commission Number: EC 2.6.1.84. 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-2925; arginine-pyruvate transaminase; EC 2.6.1.84; arginine:pyruvate transaminase; AruH; ATase. Cat No: EXWM-2925. | |
| branched-chain-amino-acid transaminase | Also acts on L-isoleucine and L-valine, and thereby differs from EC 2.6.1.6, leucine transaminase, which does not. It also differs from EC 2.6.1.66, valine-pyruvate transaminase. Group: Enzymes. Synonyms: transaminase B; branched-chain amino acid aminotransferase; branched-chain amino acid-glutamate transaminase; branched-chain aminotransferase; L-branched chain amino acid aminotransferase; glutamate-branched-chain amino acid transaminase. Enzyme Commission Number: EC 2.6.1.42. CAS No. 9054-65-3. 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-2883; branched-chain-amino-acid transaminase; EC 2.6.1.42; 9054-65-3; transaminase B; branched-chain amino acid aminotransferase; branched-chain amino acid-glutamate transaminase; branched-chain aminotransferase; L-branched chain amino acid aminotransferase; glutamate-branched-chain amino acid transaminase. Cat No: EXWM-2883. | |
| Glutamate Dehydrogenase (NAD(P)) from E.coli, Recombinant | Glutamate dehydrogenase (GLDH) is an enzyme, present in most microbes and the mitochondria of eukaryotes, as are some of the other enzymes required for urea synthesis, that converts glutamate to α-ketoglutarate, and vice versa. In animals, the produced ammonia is usually used as a substrate in the urea cycle. Typically, the α-ketoglutarate to glutamate reaction does not occur in mammals, as glutamate dehydrogenase equilibrium favours the production of ammonia and α-ketoglutarate. Applications: Use recombinant glutamate dehydrogenase in diagnostic tests for the determination of ammonia, urea, l-glutamate, glutamate pyruvate transaminase and leucine aminopeptidase. Group: Enzymes. Synonyms: glu. CAS No. 9029-12-3. GLDH. Mole weight: ~2 200 kD for the associated enzyme with 8 subunits; 280 kD for one subunit. Activity: >80 U/mg. Stability: At +2 to +8°C within specification range for 12 months. Store dry. Appearance: White lyophilizate. Source: E.coli. glutamate dehydrogenase (NADP+); glutamic dehydrogenase; dehydrogenase; glutamate (nicotinamide adenine dinucleotide (phosphate)); glutamic acid dehydrogenase; L-glutamate dehydrogenase; L-glutamic acid dehydrogenase; NAD(P)-glutamate dehydrogenase; NAD(P)H-dependent glutamate dehydrogenase; glutamate dehydrogenase (NADP); EC 1.4.1.4; GLDH. Cat No: NATE-0981. | |
| tryptophan-phenylpyruvate transaminase | Valine, leucine and isoleucine can replace tryptophan as amino donor. Group: Enzymes. Synonyms: L-tryptophan-α-ketoisocaproate aminotransferase. Enzyme Commission Number: EC 2.6.1.28. CAS No. 37277-87-5. 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-2867; tryptophan-phenylpyruvate transaminase; EC 2.6.1.28; 37277-87-5; L-tryptophan-α-ketoisocaproate aminotransferase. Cat No: EXWM-2867. | |
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