Creative Enzymes - Products
Enzyme manufacturing for life science research and medicines, food, alcohol, fabric, paper etc. Uses include: drug discovery, cancer and infectious disease research, microbiology and personalized medicine.
| Product | Description | |
|---|---|---|
| glutamate N-acetyltransferase | Also has some hydrolytic activity on acetyl-L-ornithine, but the rate is 1% of that of transferase activity. Group: Enzymes. Synonyms: ornithine transacetylase; α-N-acetyl-L-ornithine:L-glutamate N-acetyltransferase; acetylglutamate synthetase; acetylglutamate-acetylornithine transacetylase; acetylglutamic synthetase; acetylglutamic-acetylornithine transacetylase; acetylornithinase; acetylornithine glutamate acetyltransferase; glutamate acetyltransferase; N-acetyl-L-glutamate synthetase; N-acetylglutamate synthase; N-acetylglutamate synthetase; ornithine acetyltransferase; 2-N. Enzyme Commission Number: EC 2.3.1.35. CAS No. 37257-14-0. 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-2213; glutamate N-acetyltransferase; EC 2.3.1.35; 37257-14-0; ornithine transacetylase; α-N-acetyl-L-ornithine:L-glutamate N-acetyltransferase; acetylglutamate synthetase; acetylglutamate-acetylornithine transacetylase; acetylglutamic synthetase; acetylglutamic-acetylornithine transacetylase; acetylornithinase; acetylornithine glutamate acetyltransferase; glutamate acetyltransferase; N-acetyl-L-glutamate synthetase; N-acetylglutamate synthase; N-acetylglutamate synthetase; ornithine acetyltransferase; 2-N-acetyl-L-ornithine:L-glutamate N-acetyltransferase. Cat No: EXWM-2213. |  |
| glutamate-prephenate aminotransferase | A pyridoxal-phosphate protein. Aspartate can also act as the amino donor, but more slowly (cf. EC 2.6.1.78, aspartate-prephenate aminotransferase). The enzyme from higher plants shows a marked preference for prephenate as substrate compared to pyruvate, phenylpyruvate or 4-hydroxyphenylpyruvate. Group: Enzymes. Synonyms: prephenate transaminase (ambiguous); PAT (ambiguous); L-glutamate:prephenate aminotransferase. Enzyme Commission Number: EC 2.6.1.79. 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-2919; glutamate-prephenate aminotransferase; EC 2.6.1.79; prephenate transaminase (ambiguous); PAT (ambiguous); L-glutamate:prephenate aminotransferase. Cat No: EXWM-2919. | |
| glutamate-putrescine ligase | Forms part of a novel bacterial putrescine utilization pathway in Escherichia coli. Group: Enzymes. Synonyms: γ-glutamylputrescine synthetase; YcjK. Enzyme Commission Number: EC 6.3.1.11. CAS No. 914090-78-1. 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-5714; glutamate-putrescine ligase; EC 6.3.1.11; 914090-78-1; γ-glutamylputrescine synthetase; YcjK. Cat No: EXWM-5714. | |
| glutamate racemase | A pyridoxal-phosphate protein. Group: Enzymes. Enzyme Commission Number: EC 5.1.1.3. CAS No. 9024-8-2. 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-5381; glutamate racemase; EC 5.1.1.3; 9024-08-2. Cat No: EXWM-5381. | |
| glutamate synthase (ferredoxin) | Binds a [3Fe-4S] cluster as well as FAD and FMN. The protein is composed of two domains, one hydrolysing L-glutamine to NH3 and L-glutamate (cf. EC 3.5.1.2, glutaminase), the other combining the produced NH3 with 2-oxoglutarate to produce a second molecule of L-glutamate. The NH3 is channeled through a 24 ? channel in the active protein. No hydrolysis of glutamine takes place without ferredoxin and 2-oxoglutarate being bound to the protein. Group: Enzymes. Synonyms: ferredoxin-dependent glutamate synthase; ferredoxin-glutamate synthase; glutamate synthase (ferredoxin-dependent). Enzyme Commission Number: EC 1.4.7.1. CAS No. 62213-56-3. 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-1487; glutamate synthase (ferredoxin); EC 1.4.7.1; 62213-56-3; ferredoxin-dependent glutamate synthase; ferredoxin-glutamate synthase; glutamate synthase (ferredoxin-dependent). Cat No: EXWM-1487. | |
| glutamate synthase (NADH) | A flavoprotein (FMN). Group: Enzymes. Synonyms: glutamate (reduced nicotinamide adenine dinucleotide) synthase; NADH: GOGAT; L-glutamate synthase (NADH); L-glutamate synthetase; NADH-glutamate synthase; NADH-dependent glutamate synthase; glutamate synthase (NADH2). Enzyme Commission Number: EC 1.4.1.14. CAS No. 65589-88-0. 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-1447; glutamate synthase (NADH); EC 1.4.1.14; 65589-88-0; glutamate (reduced nicotinamide adenine dinucleotide) synthase; NADH: GOGAT; L-glutamate synthase (NADH); L-glutamate synthetase; NADH-glutamate synthase; NADH-dependent glutamate synthase; glutamate synthase (NADH2). Cat No: EXWM-1447. | |
| glutamate synthase (NADPH) | Binds FMN, FAD, 2 [4Fe-4S] clusters and 1 [3Fe-4S] cluster. The reaction takes place in the opposite direction to that shown. The protein is composed of two subunits, α and &beta. The α subunit is composed of two domains, one hydrolysing L-glutamine to NH3 and L-glutamate (cf. EC 3.5.1.2, glutaminase), the other combining the produced NH3 with 2-oxoglutarate to produce a second molecule of L-glutamate (cf. EC 1.4.1.4, glutamate dehydrogenase [NADP+]). The β subunit transfers electrons to the cosubstrate. The NH3 is channeled through a 31 ? channel in the active protein. In the absence of the β subunit, coupling between the two domains of the α subunit.mmission Number: EC 1.4.1.13. CAS No. 37213-53-9. 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-1446; glutamate synthase (NADPH); EC 1.4.1.13; 37213-53-9; glutamate (reduced nicotinamide adenine dinucleotide phosphate) synthase; L-glutamate synthase; L-glutamate synthetase; glutamate synthetase (NADP); NADPH-dependent glutamate synthase; glutamine-ketoglutaric aminotransferase; NADPH-glutamate synthase; NADPH-linked glutamate synthase; glutamine amide-2-oxoglutarate aminotransferase (oxidoreductase, NADP); L-glutamine:2-oxoglutarate aminotransferase, NADPH oxidizing; GOGAT. Cat No: EXWM-1446. | |
| glutamate-tRNAGln ligase | When this enzyme acts on tRNAGlu, it catalyses the same reaction as EC 6.1.1.17, glutamate-tRNA ligase. It has, however, diminished discrimination, so that it can also form glutamyl-tRNAGln. This relaxation of specificity has been found to result from the absence of a loop in the tRNA that specifically recognizes the third position of the anticodon. This accounts for the ability of this enzyme in, for example, Bacillus subtilis, to recognize both tRNA1Gln (UUG anticodon) and tRNAGlu (UUC anticodon) but not tRNA2Gln (CUG anticodon). The ability of this enzyme to recognize both tRNAGlu and one of the tRNAGln isoacceptors derives from their sharing a major identity element, a hypermodified derivative of U34 (5-methylaminomethyl-2-thiouridine). The glutamyl-tRNAGln is not used in protein synthesis until it is converted by EC 6.3.5.7, glutaminyl-tRNA synthase (glutamine-hydrolysing), into glutaminyl-tRNAGln. Group: Enzymes. Synonyms: nondiscriminating glutamyl-tRNA synthetase. Enzyme Commission Number: EC 6.1.1.24. CAS No. 9068-76-2. 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-5656; glutamate-tRNAGln ligase; EC 6.1.1.24; 9068-76-2; nondiscriminating glutamyl-tRNA synthetase. Cat No: EXWM-5656. | |
| glutamate-tRNA ligase | This enzyme belongs to the family of ligases, to be specific those forming carbon-oxygen bonds in aminoacyl-tRNA and related compounds. This enzyme participates in 3 metabolic pathways: glutamate metabolism, porphyrin and chlorophyll metabolism, and aminoacyl-trna biosynthesis. Group: Enzymes. Synonyms: glutamyl-tRNA synthetase; glutamyl-transfer ribonucleate synthetase; glutamyl-transfer RNA synthetase; glutamyl-transfer ribonucleic acid synthetase; glutamate-tRNA synthetase; glutamic acid translase. Enzyme Commission Number: EC 6.1.1.17. CAS No. 9068-76-2. 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-5648; glutamate-tRNA ligase; EC 6.1.1.17; 9068-76-2; glutamyl-tRNA synthetase; glutamyl-transfer ribonucleate synthetase; glutamyl-transfer RNA synthetase; glutamyl-transfer ribonucleic acid synthetase; glutamate-tRNA synthetase; glutamic acid translase. Cat No: EXWM-5648. | |
| glutaminase | Glutaminase (EC 3.5.1.2, glutaminase I, L-glutaminase, glutamine aminohydrolase) is an amidohydrolase enzyme that generates glutamate from glutamine. Glutaminase has tissue-specific isoenzymes. Glutaminase has an important role in glial cells. Group: Enzymes. Synonyms: glutaminase I; L-glutaminase; glutamine aminohydrolase. Enzyme Commission Number: EC 3.5.1.2. CAS No. 9001-47-2. Glutaminase. 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-4409; glutaminase; EC 3.5.1.2; 9001-47-2; glutaminase I; L-glutaminase; glutamine aminohydrolase. Cat No: EXWM-4409. | |
| glutamin-(asparagin-)ase | The enzyme from the bacterium Achromobacter hydrolyses L-asparagine at 0.8 of the rate of L-glutamine; the D-isomers are also hydrolysed, but more slowly. cf. EC 3.5.1.2, glutaminase and EC 3.5.1.1, asparaginase. Group: Enzymes. Synonyms: glutaminase-asparaginase; ansB (gene name); L-asparagine/L-glutamine amidohydrolase; L-ASNase/L-GLNase. Enzyme Commission Number: EC 3.5.1.38. CAS No. 39335-03-0. 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-4426; glutamin-(asparagin-)ase; EC 3.5.1.38; 39335-03-0; glutaminase-asparaginase; ansB (gene name); L-asparagine/L-glutamine amidohydrolase; L-ASNase/L-GLNase. Cat No: EXWM-4426. | |
| glutamine-fructose-6-phosphate transaminase (isomerizing) | Although the overall reaction is that of a transferase, the mechanism involves the formation of ketimine between fructose 6-phosphate and a 6-amino group from a lysine residue at the active site, which is subsequently displaced by ammonia (transamidination). Group: Enzymes. Synonyms: hexosephosphate aminotransferase; glucosamine-6-phosphate isomerase (glutamine-forming); glutamine-fructose-6-phosphate transaminase (isomerizing); D-fructose-6-phosphate amidotransferase; glucosaminephosphate isomerase; glucosamine 6-phosphate synthase; GlcN6P synthase. Enzyme Commission Number: EC 2.6.1.16. CAS No. 9030-45-9. 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-2856; glutamine-fructose-6-phosphate transaminase (isomerizing); EC 2.6.1.16; 9030-45-9; hexosephosphate aminotransferase; glucosamine-6-phosphate isomerase (glutamine-forming); glutamine-fructose-6-phosphate transaminase (isomerizing); D-fructose-6-phosphate amidotransferase; glucosaminephosphate isomerase; glucosamine 6-phosphate synthase; GlcN6P synthase. Cat No: EXWM-2856. | |
| glutamine N-acyltransferase | Phenylacetyl-CoA and (indol-3-yl)acetyl-CoA, but not benzoyl-CoA, can act as acyl donors. Not identical with EC 2.3.1.13 glycine N-acyltransferase or EC 2.3.1.71 glycine N-benzoyltransferase. Group: Enzymes. Enzyme Commission Number: EC 2.3.1.68. CAS No. 9030-00-6. 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-2248; glutamine N-acyltransferase; EC 2.3.1.68; 9030-00-6. Cat No: EXWM-2248. | |
| glutamine N-phenylacetyltransferase | This enzyme belongs to the family of transferases, specifically those acyltransferases transferring groups other than aminoacyl groups. This enzyme participates in tyrosine metabolism and phenylalanine metabolism. Group: Enzymes. Synonyms: glutamine phenylacetyltransferase; phenylacetyl-CoA:L-glutamine N-acetyltransferase. Enzyme Commission Number: EC 2.3.1.14. CAS No. 9030-00-6. 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-2078; glutamine N-phenylacetyltransferase; EC 2.3.1.14; 9030-00-6; glutamine phenylacetyltransferase; phenylacetyl-CoA:L-glutamine N-acetyltransferase. Cat No: EXWM-2078. | |
| glutamine-phenylpyruvate transaminase | A pyridoxal-phosphate protein. L-Methionine, L-histidine and L-tyrosine can act as donors. The enzyme has little activity on pyruvate and glyoxylate (cf. EC 2.6.1.15 glutamine-pyruvate transaminase). Group: Enzymes. Synonyms: glutamine transaminase K; glutamine-phenylpyruvate aminotransferase. Enzyme Commission Number: EC 2.6.1.64. CAS No. 68518-06-9. 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-2905; glutamine-phenylpyruvate transaminase; EC 2.6.1.64; 68518-06-9; glutamine transaminase K; glutamine-phenylpyruvate aminotransferase. Cat No: EXWM-2905. | |
| glutamine-pyruvate transaminase | A pyridoxal-phosphate protein. L-Methionine can act as donor; glyoxylate can act as acceptor. Group: Enzymes. Synonyms: glutaminase II; L-glutamine transaminase L; glutamine-oxo-acid transaminase. Enzyme Commission Number: EC 2.6.1.15. CAS No. 9030-44-8. 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-2855; glutamine-pyruvate transaminase; EC 2.6.1.15; 9030-44-8; glutaminase II; L-glutamine transaminase L; glutamine-oxo-acid transaminase. Cat No: EXWM-2855. | |
| glutamine-scyllo-inositol transaminase | A pyridoxal-phosphate protein. Group: Enzymes. Synonyms: glutamine scyllo-inosose aminotransferase; L-glutamine-keto-scyllo-inositol aminotransferase; glutamine-scyllo-inosose transaminase; L-glutamine-scyllo-inosose transaminase. Enzyme Commission Number: EC 2.6.1.50. CAS No. 9033-3-8. 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-2892; glutamine-scyllo-inositol transaminase; EC 2.6.1.50; 9033-03-8; glutamine scyllo-inosose aminotransferase; L-glutamine-keto-scyllo-inositol aminotransferase; glutamine-scyllo-inosose transaminase; L-glutamine-scyllo-inosose transaminase. Cat No: EXWM-2892. | |
| glutamine synthetase | Glutamine synthetase, which catalyses the incorporation of ammonium into glutamate, is a key enzyme of nitrogen metabolism found in all domains of life. Several types have been described, differing in their oligomeric structures and cofactor requirements. Group: Enzymes. Synonyms: glutamate-ammonia ligase; glutamylhydroxamic synthetase; L-glutamine synthetase; GS. Enzyme Commission Number: EC 6.3.1.2. CAS No. 9023-70-5. GS. 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-5722; glutamine synthetase; EC 6.3.1.2; 9023-70-5; glutamate-ammonia ligase; glutamylhydroxamic synthetase; L-glutamine synthetase; GS. Cat No: EXWM-5722. | |
| [glutamine synthetase]-adenylyl-L-tyrosine phosphorylase | This bacterial enzyme removes an adenylyl group from a modified tyrosine residue of EC 6.3.1.2, glutamine synthetase. The enzyme is bifunctional, and also performs the adenylation of this residue (cf. EC 2.7.7.42, [glutamine synthetase] adenylyltransferase). The two activities are present on separate domains. Group: Enzymes. Synonyms: adenylyl-[glutamine-synthetase]-deadenylase; [L-glutamate:ammonia ligase (ADP-forming)]-O4-(5'-adenylyl)-L-tyrosine:phosphate adenylyltransferase; [glutamate-ammonia ligase]-adenylyl-L-tyrosine phosphorylase. Enzyme Commission Number: EC 2.7.7.89. 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-3302; [glutamine synthetase]-adenylyl-L-tyrosine phosphorylase; EC 2.7.7.89; adenylyl-[glutamine-synthetase]-deadenylase; [L-glutamate:ammonia ligase (ADP-forming)]-O4-(5'-adenylyl)-L-tyrosine:phosphate adenylyltransferase; [glutamate-ammonia ligase]-adenylyl-L-tyrosine phosphorylase. Cat No: EXWM-3302. | |
| [glutamine synthetase] adenylyltransferase | This bacterial enzyme adenylates a tyrosine residue of EC 6.3.1.2, glutamine synthetase. The enzyme is bifunctional, and also catalyses a reaction that removes the adenyl group from the modified tyrosine residue (cf. EC 2.7.7.89, [glutamine synthetase]-adenylyl-L-tyrosine phosphorylase). The two activities are present on separate domains. Group: Enzymes. Synonyms: glutamine-synthetase adenylyltransferase; ATP:glutamine synthetase adenylyltransferase; adenosine triphosphate:glutamine synthetase adenylyltransferase; ATP:[L-glutamate:ammonia ligase (ADP-forming)] adenylyltransferase; ATP:[L-glutamate:ammonia ligase (ADP-forming)]-L-tyrosine adenylyltransferase; [glutamate-ammonia-ligase] adenylyltransferase. Enzyme Commission Number: EC 2.7.7.42. CAS No. 9077-66-1. 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-3254; [glutamine synthetase] adenylyltransferase; EC 2.7.7.42; 9077-66-1; glutamine-synthetase adenylyltransferase; ATP:glutamine synthetase adenylyltransferase; adenosine triphosphate:glutamine synthetase adenylyltransferase; ATP:[L-glutamate:ammonia ligase (ADP-forming)] adenylyltransferase; ATP:[L-glutamate:ammonia ligase (ADP-forming)]-L-tyrosine adenylyltransferase; [glutamate-ammonia-ligase] adenylyltransferase. Cat No: EXWM-3254. | |
| Glutamine Synthetase from Human, recombinant | GLUL also known as Glutamine synthetase. It is a trimetallic enzyme containing two divalent cation sites and one monovalent cation site per subunit. GLUL is able to regulate intracellular concentrations of glutamate and catalyzes the synthesis of glutamine form glutamate and ammonia. It is ubiquitously expressed in the human and plays a major role for many metabolic pathways such as cell proliferation, inhibition of apoptosis, and cell signaling. Recombinant Human GLUL was expressed in E.coli and purified by using conventional chromatography techniques. Group: Enzymes. Synonyms: Glutamine synthetase; GS; EC 6.3.1.2; Glutamate-ammonia ligase; GLNS; PIG43; PIG59; GLUL. Enzyme Commission Number: EC 6.3.1.2. CAS No. 9023-70-5. Purity: > 85% by SDS-PAGE. GS. Mole weight: 42 kDa. Activity: > 2.000 pmol/min/ug. Storage: Can be stored at 4°C short term (1-2 weeks). For long term storage, aliquot and store at -70°C. Avoid repeated freezing and thawing cycles. Form: Liquid. Source: E. coli. Species: Human. Glutamine synthetase; GS; EC 6.3.1.2; Glutamate-ammonia ligase; GLNS; PIG43; PIG59; GLUL. Cat No: NATE-1675. | |
| glutamine-tRNA ligase | This enzyme belongs to the family of ligases, to be specific those forming carbon-oxygen bonds in aminoacyl-tRNA and related compounds. This enzyme participates in glutamate metabolism and aminoacyl-trna biosynthesis. Group: Enzymes. Synonyms: glutaminyl-tRNA synthetase; glutaminyl-transfer RNA synthetase; glutaminyl-transfer ribonucleate synthetase; glutamine-tRNA synthetase; glutamine translase; glutamate-tRNA ligase; glutaminyl ribonucleic acid; GlnRS. Enzyme Commission Number: EC 6.1.1.18. CAS No. 9075-59-6. 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-5649; glutamine-tRNA ligase; EC 6.1.1.18; 9075-59-6; glutaminyl-tRNA synthetase; glutaminyl-transfer RNA synthetase; glutaminyl-transfer ribonucleate synthetase; glutamine-tRNA synthetase; glutamine translase; glutamate-tRNA ligase; glutaminyl ribonucleic acid; GlnRS. Cat No: EXWM-5649. | |
| glutaminyl-peptide cyclotransferase | Involved in the formation of thyrotropin-releasing hormone and other biologically active peptides containing N-terminal pyroglutamyl residues. The enzyme from papaya also acts on glutaminyl-tRNA. Group: Enzymes. Synonyms: glutaminyl-tRNA cyclotransferase; glutaminyl cyclase; glutaminyl-transfer ribonucleate cyclotransferase. Enzyme Commission Number: EC 2.3.2.5. CAS No. 37257-21-9. 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-2305; glutaminyl-peptide cyclotransferase; EC 2.3.2.5; 37257-21-9; glutaminyl-tRNA cyclotransferase; glutaminyl cyclase; glutaminyl-transfer ribonucleate cyclotransferase. Cat No: EXWM-2305. | |
| glutaminyl-tRNA synthase (glutamine-hydrolysing) | In systems lacking discernible glutamine-tRNA ligase (EC 6.1.1.18), glutaminyl-tRNAGln is formed by a two-enzyme system. In the first step, a nondiscriminating ligase (EC 6.1.1.24, glutamate-tRNAGln ligase) mischarges tRNAGln with glutamate, forming glutamyl-tRNAGln. The glutamyl-tRNAGln is not used in protein synthesis until the present enzyme converts it into glutaminyl-tRNAGln (glutamyl-tRNAGlu is not a substrate for this reaction). Ammonia or asparagine can substitute for the preferred substrate glutamine. Group: Enzymes. Synonyms: Glu-AdT; Glu-tRNAGln amidotransferase; glutamyl-tRNAGln amidotransferase; Glu-tRNAGln:L-glutamine amido-ligase (ADP-forming). Enzyme Commission Number: EC 6.3.5.7. CAS No. 52232-48-1. 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-5810; glutaminyl-tRNA synthase (glutamine-hydrolysing); EC 6.3.5.7; 52232-48-1; Glu-AdT; Glu-tRNAGln amidotransferase; glutamyl-tRNAGln amidotransferase; Glu-tRNAGln:L-glutamine amido-ligase (ADP-forming). Cat No: EXWM-5810. | |
| glutamyl aminopeptidase | Ca2+-activated and generally membrane-bound. A zinc-metallopeptidase in family M1 (membrane alanyl aminopeptidase family). Group: Enzymes. Synonyms: aminopeptidase A; aspartate aminopeptidase; angiotensinase A; glutamyl peptidase; Ca2+-activated glutamate aminopeptidase; membrane aminopeptidase II; antigen BP-1/6C3 of mouse B lymphocytes; L-aspartate aminopeptidase; angiotensinase A2. Enzyme Commission Number: EC 3.4.11.7. CAS No. 9074-83-3. 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-4028; glutamyl aminopeptidase; EC 3.4.11.7; 9074-83-3; aminopeptidase A; aspartate aminopeptidase; angiotensinase A; glutamyl peptidase; Ca2+-activated glutamate aminopeptidase; membrane aminopeptidase II; antigen BP-1/6C3 of mouse B lymphocytes; L-aspartate aminopeptidase; angiotensinase A2. Cat No: EXWM-4028. | |
| glutamyl endopeptidase | From Staphylococcus aureus strain V8. In appropriate buffer the specificity is restricted to Glu?. In peptidase family S1 (trypsin family). Group: Enzymes. Synonyms: V8 proteinase; endoproteinase Glu-C; staphylococcal serine proteinase. Enzyme Commission Number: EC 3.4.21.19. CAS No. 137010-42-5. V8 Protease. 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-4118; glutamyl endopeptidase; EC 3.4.21.19; 137010-42-5; V8 proteinase; endoproteinase Glu-C; staphylococcal serine proteinase. Cat No: EXWM-4118. | |
| glutamyl endopeptidase II | From Streptomyces griseus. A peptidase of family S1 (trypsin family). Inhibited by [Leu18?Glu]-modified turkey ovomucoid third domain. Group: Enzymes. Synonyms: GluSGP. Enzyme Commission Number: EC 3.4.21.82. CAS No. 137010-42-5. 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-4174; glutamyl endopeptidase II; EC 3.4.21.82; 137010-42-5; GluSGP. Cat No: EXWM-4174. | |
| glutamyl-tRNA reductase | This enzyme forms part of the pathway for the biosynthesis of 5-aminolevulinate from glutamate, known as theC5 pathway.The route shown in the diagram is used in most eubacteria, and in all archaebacteria, algae and plants. However, in the α-proteobacteria, EC 2.3.1.37, 5-aminolevulinate synthase, is used in an alternative route to produce the product 5-aminolevulinate from succinyl-CoA and glycine. This route is found in the mitochondria of fungi and animals, organelles that are considered to be derived from an endosymbiotic α-proteobacterium. Although higher plants do not possess EC 2.3.1.37, the protistan Euglena gracilis possesses both the C5 pathway and EC 2.3.1.37. Group: Enzymes. Enzyme Commission Number: EC 1.2.1.70. CAS No. 119940-26-0. 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-1172; glutamyl-tRNA reductase; EC 1.2.1.70; 119940-26-0. Cat No: EXWM-1172. | |
| glutarate-CoA ligase | GTP or ITP can act instead of ATP. Group: Enzymes. Synonyms: glutaryl-CoA synthetase; glutaryl coenzyme A synthetase. Enzyme Commission Number: EC 6.2.1.6. CAS No. 9023-68-1. 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-5708; glutarate-CoA ligase; EC 6.2.1.6; 9023-68-1; glutaryl-CoA synthetase; glutaryl coenzyme A synthetase. Cat No: EXWM-5708. | |
| glutarate-semialdehyde dehydrogenase | This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is glutarate-semialdehyde:NAD+ oxidoreductase. This enzyme is also called glutarate semialdehyde dehydrogenase. This enzyme participates in lysine degradation. Group: Enzymes. Synonyms: glutarate semialdehyde dehydrogenase. Enzyme Commission Number: EC 1.2.1.20. CAS No. 9028-99-3. 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-1126; glutarate-semialdehyde dehydrogenase; EC 1.2.1.20; 9028-99-3; glutarate semialdehyde dehydrogenase. Cat No: EXWM-1126. | |
| glutaryl-7-aminocephalosporanic-acid acylase | Forms 7-aminocephalosporanic acid, a key intermediate in the synthesis of cephem antibiotics. It reacts only weakly with cephalosporin C. Group: Enzymes. Synonyms: 7β-(4-carboxybutanamido)cephalosporanic acid acylase; cephalosporin C acylase; glutaryl-7-ACA acylase; CA; GCA; GA; cephalosporin acylase; glutaryl-7-aminocephalosporanic acid acylase; GL-7-ACA acylase. Enzyme Commission Number: EC 3.5.1.93. CAS No. 56645-46-6. 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-4485; glutaryl-7-aminocephalosporanic-acid acylase; EC 3.5.1.93; 56645-46-6; 7β-(4-carboxybutanamido)cephalosporanic acid acylase; cephalosporin C acylase; glutaryl-7-ACA acylase; CA; GCA; GA; cephalosporin acylase; glutaryl-7-aminocephalosporanic acid acylase; GL-7-ACA acylase. Cat No: EXWM-4485. | |
| glutaryl-CoA dehydrogenase (acceptor) | The enzyme contains FAD. The anaerobic, sulfate-reducing bacterium Desulfococcus multivorans contains two glutaryl-CoA dehydrogenases: a decarboxylating enzyme (EC 1.3.8.6), and a nondecarboxylating enzyme (this entry). The two enzymes cause different structural changes around the glutaconyl carboxylate group, primarily due to the presence of either a tyrosine or a valine residue, respectively, at the active site. Group: Enzymes. Synonyms: GDHDes; nondecarboxylating glutaryl-coenzyme A dehydrogenase; nondecarboxylating glutaconyl-coenzyme A-forming GDH; glutaryl-CoA dehydrogenase (non-decarboxylating). Enzyme Commission Number: EC 1.3.99.32. 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-1434; glutaryl-CoA dehydrogenase (acceptor); EC 1.3.99.32; GDHDes; nondecarboxylating glutaryl-coenzyme A dehydrogenase; nondecarboxylating glutaconyl-coenzyme A-forming GDH; glutaryl-CoA dehydrogenase (non-decarboxylating). Cat No: EXWM-1434. | |
| glutaryl-CoA dehydrogenase (ETF) | Contains FAD. The enzyme catalyses the oxidation of glutaryl-CoA to glutaconyl-CoA (which remains bound to the enzyme), and the decarboxylation of the latter to crotonyl-CoA (cf. EC 4.1.1.70, glutaconyl-CoA decarboxylase). FAD is the electron acceptor in the oxidation of the substrate, and its reoxidation by electron-transfer flavoprotein completes the catalytic cycle. The anaerobic, sulfate-reducing bacterium Desulfococcus multivorans contains two glutaryl-CoA dehydrogenases: a decarboxylating enzyme (this entry), and a non-decarboxylating enzyme that only catalyses the oxidation to glutaconyl-CoA (EC 1.3.99.32). Group: Enzymes. Synonyms: glutaryl coenzyme A dehydrogenase; glutaryl-CoA:(acceptor) 2,3-oxidoreductase (decarboxylating); glutaryl-CoA dehydrogenase. Enzyme Commission Number: EC 1.3.8.6. CAS No. 37255-38-2. 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-1413; glutaryl-CoA dehydrogenase (ETF); EC 1.3.8.6; 37255-38-2; glutaryl coenzyme A dehydrogenase; glutaryl-CoA:(acceptor) 2,3-oxidoreductase (decarboxylating); glutaryl-CoA dehydrogenase. Cat No: EXWM-1413. | |
| Glutaryl coenzyme A lithium salt | Glutaryl coenzyme A is an intermediate in the metabolism (catabolism) of the amino acids lysine and tryptophan. Glutaryl CoA is used as a substrate to study the specificity and kinetics of glutaryl-CoA dehydrogenases. Applications: An intermediate in the metabolism (catabolism) of the amino acids lysine and tryptophan. Group: Coenzymes. Synonyms: Glutaryl CoA. CAS No. 103192-48-9. Purity: ≥90%. Mole weight: 881.63. Appearance: Powder. Form: Solid. Glutaryl CoA; Glutaryl coenzyme A lithium salt; 103192-48-9. Cat No: COEC-053. | |
| glutathione amide-dependent peroxidase | This enzyme, which has been characterized from the proteobacterium Marichromatium gracile, is a chimeric protein, containing a peroxiredoxin-like N-terminus and a glutaredoxin-like C terminus. The enzyme has peroxidase activity towards hydrogen peroxide and several small alkyl hydroperoxides, and is thought to represent an early adaptation for fighting oxidative stress. The glutathione amide disulfide produced by this enzyme can be restored to glutathione amide by EC 1.8.1.16 (glutathione amide reductase). Group: Enzymes. Enzyme Commission Number: EC 1.11.1.17. 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-0498; glutathione amide-dependent peroxidase; EC 1.11.1.17. Cat No: EXWM-0498. | |
| glutathione amide reductase | A dimeric flavoprotein (FAD). The enzyme restores glutathione amide disulfide, which is produced during the reduction of peroxide by EC 1.11.1.17 (glutathione amide-dependent peroxidase), back to glutathione amide (it catalyses the reaction in the opposite direction to that shown). The enzyme belongs to the family of flavoprotein disulfide oxidoreductases, but unlike other members of the family, which are specific for NADPH, it prefers NADH. Group: Enzymes. Synonyms: GAR. Enzyme Commission Number: EC 1.8.1.16. 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-1642; glutathione amide reductase; EC 1.8.1.16; GAR. Cat No: EXWM-1642. | |
| glutathione-CoA-glutathione transhydrogenase | This enzyme belongs to the family of oxidoreductases, specifically those acting on a sulfur group of donors with a disulfide as acceptor. This enzyme participates in cysteine metabolism and glutathione metabolism. Group: Enzymes. Synonyms: glutathione-coenzyme A glutathione disulfide transhydrogenase; glutathione-coenzyme A glutathione disulfide transhydrogenase; glutathione coenzyme A-glutathione transhydrogenase; glutathione:coenzyme A-glutathione transhydrogenase; coenzyme A:oxidized-glutathione oxidoreductase; coenzyme A:glutathione-disulfide oxidoreductase. Enzyme Commission Number: EC 1.8.4.3. CAS No. 37256-48-7. 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-1671; glutathione-CoA-glutathione transhydrogenase; EC 1.8.4.3; 37256-48-7; glutathione-coenzyme A glutathione disulfide transhydrogenase; glutathione-coenzyme A glutathione disulfide transhydrogenase; glutathione coenzyme A-glutathione transhydrogenase; glutathione:coenzyme A-glutathione transhydrogenase; coenzyme A:oxidized-glutathione oxidoreductase; coenzyme A:glutathione-disulfide oxidoreductase. Cat No: EXWM-1671. | |
| glutathione-cystine transhydrogenase | This enzyme belongs to the family of oxidoreductases, specifically those acting on a sulfur group of donors with a disulfide as acceptor. The systematic name of this enzyme class is glutathione:cystine oxidoreductase. Other names in common use include GSH-cystine transhydrogenase, and NADPH-dependent GSH-cystine transhydrogenase. This enzyme participates in cysteine metabolism and glutathione metabolism. Group: Enzymes. Synonyms: GSH-cystine transhydrogenase; NADPH-dependent GSH-cystine transhydrogenase. Enzyme Commission Number: EC 1.8.4.4. CAS No. 37256-49-8. 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-1672; glutathione-cystine transhydrogenase; EC 1.8.4.4; 37256-49-8; GSH-cystine transhydrogenase; NADPH-dependent GSH-cystine transhydrogenase. Cat No: EXWM-1672. | |
| glutathione dehydrogenase (ascorbate) | This enzyme belongs to the family of oxidoreductases, specifically those acting on a sulfur group of donors with a quinone or similar compound as acceptor. This enzyme participates in 3 metabolic pathways: ascorbate and aldarate metabolism, glutamate metabolism, and glutathione metabolism. Group: Enzymes. Synonyms: dehydroascorbic reductase; dehydroascorbic acid reductase; glutathione dehydroascorbate reductase; DHA reductase dehydroascorbate reductase; GDOR; glutathione:dehydroascorbic acid oxidoreductase. Enzyme Commission Number: EC 1.8.5.1. CAS No. 9026-38-4. 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-1676; glutathione dehydrogenase (ascorbate); EC 1.8.5.1; 9026-38-4; dehydroascorbic reductase; dehydroascorbic acid reductase; glutathione dehydroascorbate reductase; DHA reductase dehydroascorbate reductase; GDOR; glutathione:dehydroascorbic acid oxidoreductase. Cat No: EXWM-1676. | |
| glutathione-disulfide reductase | A dimeric flavoprotein (FAD); activity is dependent on a redox-active disulfide in each of the active centres. Group: Enzymes. Synonyms: glutathione reductase; glutathione reductase (NADPH); NADPH-glutathione reductase; GSH reductase; GSSG reductase; NADPH-GSSG reductase; glutathione S-reductase; NADPH:oxidized-glutathione oxidoreductase. Enzyme Commission Number: EC 1.8.1.7. CAS No. 9001-48-3. GR. 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-1651; glutathione-disulfide reductase; EC 1.8.1.7; 9001-48-3; glutathione reductase; glutathione reductase (NADPH); NADPH-glutathione reductase; GSH reductase; GSSG reductase; NADPH-GSSG reductase; glutathione S-reductase; NADPH:oxidized-glutathione oxidoreductase. Cat No: EXWM-1651. | |
| glutathione γ-glutamylcysteinyltransferase | This enzyme belongs to the family of transferases, specifically the aminoacyltransferases. Group: Enzymes. Synonyms: phytochelatin synthase; γ-glutamylcysteine dipeptidyl transpeptidase. Enzyme Commission Number: EC 2.3.2.15. CAS No. 125390-02-5. 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-2288; glutathione γ-glutamylcysteinyltransferase; EC 2.3.2.15; 125390-02-5; phytochelatin synthase; γ-glutamylcysteine dipeptidyl transpeptidase. Cat No: EXWM-2288. | |
| glutathione-homocystine transhydrogenase | The reactions catalysed by this enzyme and by others in this subclass may be similar to those catalysed by EC 2.5.1.18 glutathione transferase. Group: Enzymes. Enzyme Commission Number: EC 1.8.4.1. CAS No. 9029-40-7. 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-1664; glutathione-homocystine transhydrogenase; EC 1.8.4.1; 9029-40-7. Cat No: EXWM-1664. | |
| 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. | |
| glutathione oxidase | A flavoprotein (FAD). Also acts, more slowly, on L-cysteine and several other thiols. Group: Enzymes. Enzyme Commission Number: EC 1.8.3.3. CAS No. 55467-56-6. 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-1660; glutathione oxidase; EC 1.8.3.3; 55467-56-6. Cat No: EXWM-1660. | |
| glutathione peroxidase | A protein containing a selenocysteine residue. Steroid and lipid hydroperoxides, but not the product of reaction of EC 1.13.11.12 lipoxygenase on phospholipids, can act as acceptor, but more slowly than H2O2 (cf. EC 1.11.1.12 phospholipid-hydroperoxide glutathione peroxidase). Group: Enzymes. Synonyms: GSH peroxidase; selenium-glutathione peroxidase; reduced glutathione peroxidase. Enzyme Commission Number: EC 1.11.1.9. CAS No. 9013-66-5. GSH-Px. 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-0511; glutathione peroxidase; EC 1.11.1.9; 9013-66-5; GSH peroxidase; selenium-glutathione peroxidase; reduced glutathione peroxidase. Cat No: EXWM-0511. | |
| Glutathione reductase from E. coli, Recombinant | Glutathione reductase (GR) is a crucial flavoenzyme in the antioxidant defense system. Reduced glutathione (GSH) is used by glutathione peroxidase to detoxify hydrogen peroxide and in the precess is converted to oxidized glutathione (GSSG). The GSSG is then recycled back to GSH by glutathione reductase (GR) using NADPH that is then converted to NADP+. The regenerated GSH is then available to detoxify more hydrogen peroxide. The enzyme uses FAD as a cofactor. GR and glutathione peroxidase may inhibit lipid peroxidation by functioning as antioxidant enzymes in sperm. Glutathione reductase shares a structural motif with a number of other proteins including aspartyl prote.e; GSSG reductase; NADPH-GSSG reductase; glutathione S-reductase; NADPH:oxidized-glutathione oxidoreductase. Enzyme Commission Number: EC 1.8.1.7. CAS No. 9001-48-3. Purity: >95% as judged by SDS-PAGE. GR. Mole weight: 49.5 kDa. Activity: 35 U/mg protein, 98 U/ml. Storage: Glutathione reductase should be stored at 4 °C or and will remain stable up to 3 years if stored as specified. Form: 3.2 M ammonium sulphate. Source: E. coli. Species: E. coli. GR; glutathione reductase; glutathione reductase (NADPH); NADPH-glutathione reductase; GSH reductase; GSSG reductase; NADPH-GSSG reductase; glutathione S-reductase; NADPH:oxidized-glutathione oxidoreductase. Cat No: NATE-1574. | |
| Glutathione Reductase from Human, Recombinant | Glutathione reductase enzyme is a homodimeric enzyme containing 1 FAD molecule and 1 NADPH binding domain per subunit., Both human GR (hGR) and Plasmodium falciparum GR (PfGR) are essential for the survival of the malaria parasite within the human erythrocyte. Thus, this enzyme may be used for studies of candidate anti-malaria reagents. Group: Enzymes. Synonyms: glutathione-disulfide reductase; glutathione reductase; glutathione reductase (NADPH); NADPH-glutathione reductase; GSH reductase; GSSG reductase; NADPH-GSSG reductase; glutathione S-reductase; NADPH:oxidized-glutathione oxidoreductase; EC 1.8.1.7; 9001-48-3; GR. Enzyme Commission Number: EC 1.8.1.7. CAS No. 9001-48-3. GR. Activity: > 10 units/mg protein. Storage: -20°C. Form: buffered aqueous solution; Solution containing 25 mM Tris-HCl, pH 7.4, 1 mM EDTA, and 50% (v/v) glycerol. Source: E. coli. Species: Human. glutathione-disulfide reductase; glutathione reductase; glutathione reductase (NADPH); NADPH-glutathione reductase; GSH reductase; GSSG reductase; NADPH-GSSG reductase; glutathione S-reductase; NADPH:oxidized-glutathione oxidoreductase; EC 1.8.1.7; 9001-48-3; GR. Cat No: NATE-0320. | |
| Glutathione S-Transferase from E.coli, Recombinant | Glutathione S-transferases (GSTs), previously known as ligandins, comprise a family of eukaryotic and prokaryotic phase II metabolic isozymes best known for their ability to catalyze the conjugation of the reduced form of glutathione (GSH) to xenobiotic substrates for the purpose of detoxification. The GST family consists of three superfamilies:the cytosolic, mitochondrial, and microsomal--also known as MAPEG--proteins. Members of the GST superfamily are extremely diverse in amino acid sequence, and a large fraction of the sequences deposited in public databases are of unknown function. The Enzyme Function Initiative (EFI) is using GSTs as a model superfamily to iden.ferase. Mole weight: 26kDa. Activity: >20 units/mg. Stability: Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles. Form: Sterile Filtered clear solution in Phosphate Buffered Saline pH 7.4. Source: E.coli. Species: E.coli. Glutathione S-transferases; GSTs; GST; Glutathione S-alkenetransferase; Glutathione S-alkyltransferase; Glutathione S-aralkyltransferase; Glutathione S-aryltransferase; Glutathione S-epoxidetransferase; RX:Glutathione R-transferase; EC 2.5.1.18; 50812-37-8. Cat No: NATE-1945. | |
| Glutathione S-Transferase, Recombinant | Glutathione S-transferases (GSTs), previously known as ligandins, comprise a family of eukaryotic and prokaryotic phase II metabolic isozymes best known for their ability to catalyze the conjugation of the reduced form of glutathione (GSH) to xenobiotic substrates for the purpose of detoxification. The GST family consists of three superfamilies:the cytosolic, mitochondrial, and microsomalalso known as MAPEGproteins. Members of the GST superfamily are extremely diverse in amino acid sequence, and a large fraction of the sequences deposited in public databases are of unknown function. The Enzyme Function Initiative (EFI) is using GSTs as a model superfamily to identify new.erase; Glutathione S-aryltransferase; Glutathione S-epoxidetransferase; RX:Glutathione R-transferase; EC 2.5.1.18; 50812-37-8. Enzyme Commission Number: EC 2.5.1.18. Purity: >90% (SDS-PAGE test). Mole weight: About 26kDa (SDS-PAGE detection). Activity: 30 u/mg. Appearance: White powder, lyophilized or colorless liquid. Storage: 4°C, store at -20°C for long-term preservation. Form: Freeze dried powder. Glutathione S-transferases; GSTs; GST; Glutathione S-alkenetransferase; Glutathione S-alkyltransferase; Glutathione S-aralkyltransferase; Glutathione S-aryltransferase; Glutathione S-epoxidetransferase; RX:Glutathione R-transferase; EC 2.5.1.18; 50812-37-8. Cat No: NATE-1141. | |
| glutathione synthase | This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-amino-acid ligases (peptide synthases). This enzyme participates in glutamate metabolism and glutathione metabolism. Group: Enzymes. Synonyms: glutathione synthetase; GSH synthetase. Enzyme Commission Number: EC 6.3.2.3. CAS No. 9023-62-5. 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-5746; glutathione synthase; EC 6.3.2.3; 9023-62-5; glutathione synthetase; GSH synthetase. Cat No: EXWM-5746. | |
| Glutathione Synthase 1 (Crude Enzyme) | This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-amino-acid ligases (peptide synthases). This product with the indicated enzyme activity was briefly purified from engineered E.coli. Applications: Biotechnology; analysis; synthesis. Group: Enzymes. Synonyms: glutathione synthetase; GSH synthetase. Enzyme Commission Number: EC 6.3.2.3. CAS No. 9023-62-5. Activity: Undetermined. Appearance: Clear to translucent yellow solution. Storage: at -20 °C or lower, for at least 1 month. Source: E. coli. glutathione synthetase; GSH synthetase. Pack: 100ml. Cat No: NATE-1860. | |
| Glutathione Synthase 2 (Crude Enzyme) | This enzyme belongs to the family of ligases, specifically those forming carbon-nitrogen bonds as acid-D-amino-acid ligases (peptide synthases). This product with the indicated enzyme activity was briefly purified from engineered E.coli. Applications: Biotechnology; analysis; synthesis. Group: Enzymes. Synonyms: glutathione synthetase; GSH synthetase. Enzyme Commission Number: EC 6.3.2.3. CAS No. 9023-62-5. Activity: Undetermined. Appearance: Clear to translucent yellow solution. Storage: at -20 °C or lower, for at least 1 month. Source: E. coli. glutathione synthetase; GSH synthetase. Pack: 100ml. Cat No: NATE-1861. | |
| glutathione thiolesterase | This enzyme belongs to the family of hydrolases, specifically those acting on thioester bonds. The systematic name of this enzyme class is S-acylglutathione hydrolase. This enzyme is also called citryl-glutathione thioesterhydrolase. Group: Enzymes. Synonyms: citryl-glutathione thioesterhydrolase. Enzyme Commission Number: EC 3.1.2.7. CAS No. 9025-99-4. 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-3570; glutathione thiolesterase; EC 3.1.2.7; 9025-99-4; citryl-glutathione thioesterhydrolase. Cat No: EXWM-3570. | |
| glutathione transferase | A group of enzymes of broad specificity. R may be an aliphatic, aromatic or heterocyclic group; X may be a sulfate, nitrile or halide group. Also catalyses the addition of aliphatic epoxides and arene oxides to glutathione, the reduction of polyol nitrate by glutathione to polyol and nitrile, certain isomerization reactions and disulfide interchange. Group: Enzymes. Synonyms: glutathione S-transferase; glutathione S-alkyltransferase; glutathione S-aryltransferase; S-(hydroxyalkyl)glutathione lyase; glutathione S-aralkyltransferase; glutathione S-alkyl transferase; GST. Enzyme Commission Number: EC 2.5.1.18. CAS No. 50812-37-8. Glutathione S-Transferase. 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-2754; glutathione transferase; EC 2.5.1.18; 50812-37-8; glutathione S-transferase; glutathione S-alkyltransferase; glutathione S-aryltransferase; S-(hydroxyalkyl)glutathione lyase; glutathione S-aralkyltransferase; glutathione S-alkyl transferase; GST. Cat No: EXWM-2754. | |
| glutathionylspermidine amidase | Spermidine is numbered so that atom N-1 is in the amino group of the aminopropyl part of the molecule. The enzyme from Escherichia coli is bifunctional and also catalyses the glutathionylspermidine synthase (EC 6.3.1.8) reaction, resulting in a net hydrolysis of ATP. Group: Enzymes. Synonyms: glutathionylspermidine amidohydrolase (spermidine-forming). Enzyme Commission Number: EC 3.5.1.78. CAS No. 171040-71-4. 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-4469; glutathionylspermidine amidase; EC 3.5.1.78; 171040-71-4; glutathionylspermidine amidohydrolase (spermidine-forming). Cat No: EXWM-4469. | |
| glutathionylspermidine synthase | Requires magnesium ions. Involved in the synthesis of trypanothione in trypanosomatids. The enzyme from Escherichia coli is bifunctional and also catalyses the glutathionylspermidine amidase (EC 3.5.1.78) reaction, resulting in a net hydrolysis of ATP. Group: Enzymes. Synonyms: glutathione:spermidine ligase (ADP-forming). Enzyme Commission Number: EC 6.3.1.8. CAS No. 9077-9-2. 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-5728; glutathionylspermidine synthase; EC 6.3.1.8; 9077-09-2; glutathione:spermidine ligase (ADP-forming). Cat No: EXWM-5728. | |
| glutinol synthase | The enzyme from Kalanchoe daigremontiana also gives traces of other triterpenoids. Group: Enzymes. Enzyme Commission Number: EC 5.4.99.49. 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-5591; glutinol synthase; EC 5.4.99.49. Cat No: EXWM-5591. | |
| glyceollin synthase | A heme-thiolate protein (P-450). Glyceollins II and III are formed from 2-dimethylallyl-(6aS,11aS)-3,6a,9-trihydroxypterocarpan whereas glyceollin I is formed from the 4-isomer. Group: Enzymes. Enzyme Commission Number: EC 1.14.13.85. 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-0893; glyceollin synthase; EC 1.14.13.85. Cat No: EXWM-0893. | |
| glyceraldehyde-3-phosphate dehydrogenase (ferredoxin) | Contains tungsten-molybdopterin and iron-sulfur clusters. This enzyme is thought to function in place of glyceralde-3-phosphate dehydrogenase and possibly phosphoglycerate kinase in the novel Embden-Meyerhof-type glycolytic pathway found in Pyrococcus furiosus. It is specific for glyceraldehyde-3-phosphate. Group: Enzymes. Synonyms: GAPOR; glyceraldehyde-3-phosphate Fd oxidoreductase; glyceraldehyde-3-phosphate ferredoxin reductase. Enzyme Commission Number: EC 1.2.7.6. CAS No. 162995-20-2. 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-1229; glyceraldehyde-3-phosphate dehydrogenase (ferredoxin); EC 1.2.7.6; 162995-20-2; GAPOR; glyceraldehyde-3-phosphate Fd oxidoreductase; glyceraldehyde-3-phosphate ferredoxin reductase. Cat No: EXWM-1229. | |
| Glyceraldehyde-3-phosphate dehydrogenase from Human, Recombinant | Glyceraldehyde-3-phosphate dehydrogenase (GAPDH), a tetramer of 36 kDa subunits, is a catalytic enzyme involved in glycolysis. GAPDH catalyzes the reversible reduction of glyceraldehyde-3-phosphate to 3-phosphoglycerol phosphate in the presence of NAD+. Besides functioning as a glycolytic enzyme in the cytoplasm, mammalian GAPDH is also involved in a variety of intracellular processes such as membrane fusion, microtubule bundling, phosphotransferase activity, nuclear RNA export, DNA replication, and DNA repair. Glyceraldehyde-3-phosphate dehydrogenase was also found to bind to mutant polyglutamine proteins formed in neurodegenerative diseases such as Huntingto.horylating); triosephosphate dehydrogenase; dehydrogenase, glyceraldehyde phosphate; phosphoglyceraldehyde dehydrogenase; 3-phosphoglyceraldehyde dehydrogenase; NAD+-dependent glyceraldehyde phosphate dehydrogenase; glyceraldehyde phosphate dehydrogenase (NAD+); glyceraldehyde-3-phosphate dehydrogenase (NAD+); NADH-glyceraldehyde phosphate dehydrogenase; glyceraldehyde-3-P-dehydrogenase; 9001-50-7. Glyceraldehyde-3-phosphate Dehydrogenase. Mole weight: 37,984 Da. Activity: > 80 units/mg protein. Stability: Store at -20°C. Form: Lyophilized from a buffered solution with stabilizers. Source: E. coli. Species: Human. EC 1.2.1.12; GAPDH; glyceraldehyde-3-phosphate. | |
| Glyceraldehyde-3-phosphate Dehydrogenase from Mouse, Recombinant | Glyceraldehyde-3-phosphate dehydrogenase catalyzes the conversion of glyceraldehyde-3-phosphate to 1,3-bisphosphoglycerate as part of glycolysis. It has also been shown to have roles in initiation of apoptosis, transcription activation and the shuttling of ER to Golgi vesicles. Group: Enzymes. Synonyms: G3PD; GAPD; HEL-S-162eP; Glyceraldehyde-3-phosphate dehydrogenase isoform 2. Enzyme Commission Number: EC 1.2.1.12. Purity: > 95% by SDS-PAGE. Glyceraldehyde-3-phosphate Dehydrogenase. Mole weight: 38.2kDa. Activity: > 40 units/mg. Storage: Store at +4°C for short term (1-2 weeks). For long term storage, aliquot and store at -70°C. Avoid repeated freeze/thaw cycles. Form: Liquid. Source: E. coli and fused to His-tag at C-terminus. Species: Mouse. GAPDH; glyceraldehyde-3-phosphate dehydrogenase; G3PD; GAPD; HEL-S-162eP; Glyceraldehyde-3-phosphate dehydrogenase isoform 2; glyceraldehyde-3-P-dehydrogenase. Cat No: NATE-1635. | |
| glyceraldehyde-3-phosphate dehydrogenase (NADP+) | Glyceraldehyde-3-phosphate dehydrogenase (NADP+) (EC 1.2.1.9) (GAPN) is an enzyme that irreversibly catalyzes the oxidation of glyceraldehyde-3-phosphate (GAP) to 3-phosphoglycerate (3-PG or 3-PGA) using the reduction of NADP+ to NADPH. GAPN is used in a variant of glycolysis that conserves energy as NADPH rather than as ATP. The NADPH and 3-PG can then be used for synthesis. The most familiar variant of glycolysis uses glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and phosphoglycerate kinase to produce ATP. GAPDH is phosphorylating. GAPN is non-phosphorylating. GAPN was reported first by Rosenberg and Arnon in 1954. It has been found in plants, algae, and bacteria. it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1193; glyceraldehyde-3-phosphate dehydrogenase (NADP+); EC 1.2.1.9; 9028-92-6; triosephosphate dehydrogenase; dehydrogenase, glyceraldehyde phosphate (nicotinamide adenine dinucleotide phosphate); glyceraldehyde phosphate dehydrogenase (NADP); glyceraldehyde 3-phosphate dehydrogenase (NADP); NADP-glyceraldehyde phosphate dehydrogenase; NADP-glyceraldehyde-3-phosphate dehydrogenase; glyceraldehyde-3-phosphate:NADP reductase; nonphosphorylating glyceraldehyde-3-phosphate dehydrogenase; glyceraldehyde-3-phosphate dehydrogenase (NADP). Cat No: EXWM-1193. | |
| glyceraldehyde-3-phosphate dehydrogenase [NAD(P)+] | The enzyme is part of the modified Embden-Meyerhof-Parnas pathway of the archaeon Thermoproteus tenax. cf. EC 1.2.1.9 [glyceraldehyde-3-phosphate dehydrogenase (NADP+)]. Group: Enzymes. Synonyms: non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase; GAPN. Enzyme Commission Number: EC 1.2.1.90. 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-1194; glyceraldehyde-3-phosphate dehydrogenase [NAD(P)+]; EC 1.2.1.90; non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase; GAPN. Cat No: EXWM-1194. | |
| glyceraldehyde-3-phosphate dehydrogenase (NAD(P)+) (phosphorylating) | NAD+ and NADP+ can be used as cofactors with similar efficiency, unlike EC 1.2.1.12 glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) and EC 1.2.1.13 glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating), which are NAD+- and NADP+-dependent, respectively. Group: Enzymes. Synonyms: triosephosphate dehydrogenase (NAD(P)); glyceraldehyde-3-phosphate dehydrogenase (NAD(P)) (phosphorylating). Enzyme Commission Number: EC 1.2.1.59. CAS No. 39369-25-0. 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-1161; glyceraldehyde-3-phosphate dehydrogenase (NAD(P)+) (phosphorylating); EC 1.2.1.59; 39369-25-0; triosephosphate dehydrogenase (NAD(P)); glyceraldehyde-3-phosphate dehydrogenase (NAD(P)) (phosphorylating). Cat No: EXWM-1161. | |
| glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating) | This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. This enzyme participates in the Calvin cycle which is an autotrophic carbon fixation pathway. Group: Enzymes. Synonyms: triosephosphate dehydrogenase (NADP+); dehydrogenase, glyceraldehyde phosphate (nicotinamide adenine dinucleotide phosphate) (phosphorylating); glyceraldehyde phosphate dehydrogenase (nicotinamide adenine dinucleotide phosphate) (phosphoryla. Enzyme Commission Number: EC 1.2.1.13. CAS No. 37250-87-6. 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-1119; glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating); EC 1.2.1.13; 37250-87-6; triosephosphate dehydrogenase (NADP+); dehydrogenase, glyceraldehyde phosphate (nicotinamide adenine dinucleotide phosphate) (phosphorylating); glyceraldehyde phosphate dehydrogenase (nicotinamide adenine dinucleotide phosphate) (phosphorylating); NADP+-glyceraldehyde-3-phosphate dehydrogenase; NADP+-glyceraldehyde phosphate dehydrogenase; NADP+-dependent glyceraldehyde phosphate dehydrogenase; NADP+-triose phosphate dehydrogenase; glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating); GAPDH. Cat No: EXWM-1119. | |
| glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) | Also acts very slowly on D-glyceraldehyde and some other aldehydes; thiols can replace phosphate. Group: Enzymes. Synonyms: triosephosphate dehydrogenase; dehydrogenase, glyceraldehyde phosphate; phosphoglyceraldehyde dehydrogenase; 3-phosphoglyceraldehyde dehydrogenase; NAD+-dependent glyceraldehyde phosphate dehydrogenase; glyceraldehyde phosphate dehydrogenase (NAD+); glyceraldehyde-3-phosphate dehydrogenase (NAD+); NADH-glyceraldehyde phosphate dehydrogenase; glyceraldehyde-3-P-dehydrogenase. Enzyme Commission Number: EC 1.2.1.12. CAS No. 9001-50-7. Glyceraldehyde-3-phosphate Dehydrogenase. 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-1118; glyceraldehyde-3-phosphate dehydrogenase (phosphorylating); EC 1.2.1.12; 9001-50-7; triosephosphate dehydrogenase; dehydrogenase, glyceraldehyde phosphate; phosphoglyceraldehyde dehydrogenase; 3-phosphoglyceraldehyde dehydrogenase; NAD+-dependent glyceraldehyde phosphate dehydrogenase; glyceraldehyde phosphate dehydrogenase (NAD+); glyceraldehyde-3-phosphate dehydrogenase (NAD+); NADH-glyceraldehyde phosphate dehydrogenase; glyceraldehyde-3-P-dehydrogenase. Cat No: EXWM-1118. | |
| glyceraldehyde dehydrogenase (FAD-containing) | The enzyme from the archaeon Sulfolobus acidocaldarius catalyses the oxidation of D-glyceraldehyde in the nonphosphorylative Entner-Doudoroff pathway. With 2,6-dichlorophenolindophenol as artificial electron acceptor, the enzyme shows a broad substrate range, but is most active with D-glyceraldehyde. It is not known which acceptor is utilized in vivo. The iron-sulfur protein contains FAD and molybdopterin guanine dinucleotide. Group: Enzymes. Synonyms: glyceraldehyde oxidoreductase. Enzyme Commission Number: EC 1.2.99.8. 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-1236; glyceraldehyde dehydrogenase (FAD-containing); EC 1.2.99.8; glyceraldehyde oxidoreductase. Cat No: EXWM-1236. | |
| glycerate 2-kinase | A key enzyme in the nonphosphorylative Entner-Doudoroff pathway in archaea. In the bacterium Hyphomicrobium methylovorum GM2 the enzyme is involved in formaldehyde assimilation I (serine pathway). In Escherichia coli the enzyme is involved in D-glucarate/D-galactarate degradation. The enzyme requires a divalent metal ion. Group: Enzymes. Synonyms: D-glycerate-2-kinase; glycerate kinase (2-phosphoglycerate forming); ATP:(R)-glycerate 2-phosphotransferase. Enzyme Commission Number: EC 2.7.1.165. 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-2995; glycerate 2-kinase; EC 2.7.1.165; D-glycerate-2-kinase; glycerate kinase (2-phosphoglycerate forming); ATP:(R)-glycerate 2-phosphotransferase. Cat No: EXWM-2995. | |
| glycerate 3-kinase | This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. This enzyme participates in 3 metabolic pathways: serine/glycine/threonine metabolism, glycerolipid metabolism, and glyoxylate-dicarboxylate metabolism. Group: Enzymes. Synonyms: glycerate kinase (phosphorylating) (ambiguous); D-glycerate 3-kinase; D-glycerate kinase (ambiguous); glycerate-kinase (ambiguous); GK (ambiguous); D-glyceric acid kinase (ambiguous); ATP:(R)-glycerate 3-phosphotransferase. Enzyme Commission Number: EC 2.7.1.31. CAS No. 9026-61-3. 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-3062; glycerate 3-kinase; EC 2.7.1.31; 9026-61-3; glycerate kinase (phosphorylating) (ambiguous); D-glycerate 3-kinase; D-glycerate kinase (ambiguous); glycerate-kinase (ambiguous); GK (ambiguous); D-glyceric acid kinase (ambiguous); ATP:(R)-glycerate 3-phosphotransferase. Cat No: EXWM-3062. | |
| glycerate dehydrogenase | This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (R)-glycerate:NAD+ oxidoreductase. Other names in common use include D-glycerate dehydrogenase, and hydroxypyruvate reductase (due to the reversibility of the reaction). This enzyme participates in glycine, serine and threonine metabolism and glyoxylate and dicarboxylate metabolism. Group: Enzymes. Synonyms: D-glycerate dehydrogenase; hydroxypyruvate reductase; (R)-glycerate:NAD+ oxidoreductase. Enzyme Commission Number: EC 1.1.1.29. CAS No. 9028-37-9. 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-0198; glycerate dehydrogenase; EC 1.1.1.29; 9028-37-9; D-glycerate dehydrogenase; hydroxypyruvate reductase; (R)-glycerate:NAD+ oxidoreductase. Cat No: EXWM-0198. | |
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