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| Product | Description | |
|---|---|---|
| 18S rRNA (guanine1575-N7)-methyltransferase | The enzyme, found in eukaryotes, is involved in pre-rRNA processing. The numbering corresponds to the enzyme from the yeast Saccharomyces cerevisiae. Group: Enzymes. Synonyms: 18S rRNA methylase Bud23; BUD23 (gene name). Enzyme Commission Number: EC 2.1.1.309. 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-1917; 18S rRNA (guanine1575-N7)-methyltransferase; EC 2.1.1.309; 18S rRNA methylase Bud23; BUD23 (gene name). Cat No: EXWM-1917. |  |
| 25S rRNA (cytosine2278-C5)-methyltransferase | The enzyme, found in eukaryotes, is specific for 25S cytosine2278. The numbering corresponds to the enzyme from the yeast Saccharomyces cerevisiae. Group: Enzymes. Synonyms: RCM1 (gene name). Enzyme Commission Number: EC 2.1.1.311. 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-1919; 25S rRNA (cytosine2278-C5)-methyltransferase; EC 2.1.1.311; RCM1 (gene name). Cat No: EXWM-1919. | |
| 25S rRNA (cytosine2870-C5)-methyltransferase | The enzyme, found in eukaryotes, is specific for cytosine2870 of the 25S ribosomal RNA. The numbering corresponds to the enzyme from the yeast Saccharomyces cerevisiae. Group: Enzymes. Synonyms: NOP2 (gene name). Enzyme Commission Number: EC 2.1.1.310. 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-1918; 25S rRNA (cytosine2870-C5)-methyltransferase; EC 2.1.1.310; NOP2 (gene name). Cat No: EXWM-1918. | |
| 25S rRNA (uracil2634-N3)-methyltransferase | The enzyme, described from the yeast Saccharomyces cerevisiae, is involved in ribosome biogenesis. Group: Enzymes. Synonyms: BMT5. Enzyme Commission Number: EC 2.1.1.313. 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-1921; 25S rRNA (uracil2634-N3)-methyltransferase; EC 2.1.1.313; BMT5. Cat No: EXWM-1921. | |
| 25S rRNA (uracil2843-N3)-methyltransferase | The enzyme, described from the yeast Saccharomyces cerevisiae, is involved in ribosome biogenesis. Group: Enzymes. Synonyms: BMT6. Enzyme Commission Number: EC 2.1.1.312. 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-1920; 25S rRNA (uracil2843-N3)-methyltransferase; EC 2.1.1.312; BMT6. Cat No: EXWM-1920. | |
| 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase | Binds 2 Mg2+ ions that are essential for activity. The enzyme participates in the biosynthetic pathways for folate (in bacteria, plants and fungi) and methanopterin (in archaea). The enzyme exists in varying types of multifunctional proteins in different organisms. The enzyme from the bacterium Streptococcus pneumoniae also harbours the activity of EC 4.1.2.25, dihydroneopterin aldolase, the enzyme from the plant Arabidopsis thaliana harbours the activity of EC 2.5.1.15, dihydropteroate synthase, while the enzyme from yeast Saccharomyces cerevisiae is trifunctional with both of the two above mentioned activities. Group: Enzymes. Synonyms: 2-amino-4-hydroxy-6-hydroxymethyldi. Enzyme Commission Number: EC 2.7.6.3. CAS No. 37278-23-2. 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-3222; 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase; EC 2.7.6.3; 37278-23-2; 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase; H2-pteridine-CH2OH pyrophosphokinase; 7,8-dihydroxymethylpterin-pyrophosphokinase; HPPK; 7,8-dihydro-6-hydroxymethylpterin pyrophosphokinase; hydroxymethyldihydropteridine pyrophosphokinase; ATP:2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine 6'-diphosphotransferase. Cat No: EXWM-3222. | |
| 2-methoxy-6-polyprenyl-1,4-benzoquinol methylase | This enzyme is involved in ubiquinone biosynthesis. Ubiquinones from different organisms have a different number of prenyl units (for example, ubiquinone-6 in Saccharomyces, ubiquinone-9 in rat and ubiquinone-10 in human), and thus the natural substrate for the enzymes from different organisms has a different number of prenyl units. However, the enzyme usually shows a low degree of specificity regarding the number of prenyl units. For example, when the COQ5 gene from Saccharomyces cerevisiae is introduced into Escherichia coli, it complements the respiratory deficiency of an ubiE mutant. The bifunctional enzyme from Escherichia coli also catalyses the methylation of demethylmenaquinol-8 (this activity is classified as EC 2.1.1.163). Group: Enzymes. Synonyms: ubiE (gene name, ambiguous). Enzyme Commission Number: EC 2.1.1.201. 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-1802; 2-methoxy-6-polyprenyl-1,4-benzoquinol methylase; EC 2.1.1.201; ubiE (gene name, ambiguous). Cat No: EXWM-1802. | |
| 3-demethylubiquinol 3-O-methyltransferase | This enzyme is involved in ubiquinone biosynthesis. Ubiquinones from different organisms have a different number of prenyl units (for example, ubiquinone-6 in Saccharomyces, ubiquinone-9 in rat and ubiquinone-10 in human), and thus the natural substrate for the enzymes from different organisms has a different number of prenyl units. However, the enzyme usually shows a low degree of specificity regarding the number of prenyl units. For example, the human COQ3 enzyme can restore biosynthesis of ubiquinone-6 in coq3 deletion mutants of yeast.The enzymes from yeast, Escherichia coli and rat also catalyse the methylation of 3,4-dihydroxy-5-all-trans-polyprenylbenzoate (a reac...COQ3 (gene name); Coq3 O-methyltransferase; ubiG (gene name, ambiguous). Enzyme Commission Number: EC 2.1.1.64. CAS No. 63774-48-1. 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-1966; 3-demethylubiquinol 3-O-methyltransferase; EC 2.1.1.64; 63774-48-1; 5-demethylubiquinone-9 methyltransferase; OMHMB-methyltransferase; 2-octaprenyl-3-methyl-5-hydroxy-6-methoxy-1,4-benzoquinone methyltransferase; S-adenosyl-L-methionine:2-octaprenyl-3-methyl-5-hydroxy-6-methoxy-1,4-benzoquinone-O-methyltransferase; COQ3 (gene name); Coq3 O-methyltransferase; ubiG (gene name, ambiguous). Cat No: EXWM-1966. | |
| 3-hydroxy acid dehydrogenase | The enzyme, purified from the bacterium Escherichia coli and the yeast Saccharomyces cerevisiae, shows activity with a range of 3- and 4-carbon 3-hydroxy acids. The highest activity is seen with L-allo-threonine and D-threonine. The enzyme from Escherichia coli also shows high activity with L-serine, D-serine, (S)-3-hydroxy-2-methylpropanoate and (R)-3-hydroxy-2-methylpropanoate. The enzyme has no activity with NAD+ or L-threonine (cf. EC 1.1.1.103, L-threonine 3-dehydrogenase). Group: Enzymes. Synonyms: ydfG (gene name); YMR226c (gene name). Enzyme Commission Number: EC 1.1.1.381. 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-0300; 3-hydroxy acid dehydrogenase; EC 1.1.1.381; ydfG (gene name); YMR226c (gene name). Cat No: EXWM-0300. | |
| 3-methylbutanal reductase | The enzyme purified from Saccharomyces cerevisiae catalyses the reduction of a number of straight-chain and branched aldehydes, as well as some aromatic aldehydes. Group: Enzymes. Enzyme Commission Number: EC 1.1.1.265. CAS No. 214265-44-8. 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-0171; 3-methylbutanal reductase; EC 1.1.1.265; 214265-44-8. Cat No: EXWM-0171. | |
| aminopeptidase Y | Requires Co2+; inhibited by Zn2+ and Mn2+. An enzyme best known from Saccharomyces cerevisiae that hydrolyses Lys-NHPhNO2 and, more slowly, Arg-NHPhNO2. Type example of peptidase family M28. Group: Enzymes. Synonyms: aminopeptidase Co; aminopeptidase (cobalt-activated); lysyl aminopeptidase. Enzyme Commission Number: EC 3.4.11.15. CAS No. 114796-97-3. 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-4011; aminopeptidase Y; EC 3.4.11.15; 114796-97-3; aminopeptidase Co; aminopeptidase (cobalt-activated); lysyl aminopeptidase. Cat No: EXWM-4011. | |
| barrierpepsin | A secreted endopeptidase known from bakers yeast (Saccharomyces cerevisiae). In peptidase family A1 (pepsin A family). Group: Enzymes. Synonyms: barrier proteinase; Bar proteinase. Enzyme Commission Number: EC 3.4.23.35. CAS No. 152060-38-3. 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-4272; barrierpepsin; EC 3.4.23.35; 152060-38-3; barrier proteinase; Bar proteinase. Cat No: EXWM-4272. | |
| cerevisin | From Saccharomyces cerevisiae (baker's yeast, brewer's yeast). In peptidase family S8 (subtilisin family), but contains a Cys residue near the active site His, and is inhibited by mercurials. Proteinase ycaB is a similar enzyme from the yeast Candida albicans. Group: Enzymes. Synonyms: yeast proteinase B; proteinase yscB; baker's yeast proteinase B; brewer's yeast proteinase; peptidase &beta. Enzyme Commission Number: EC 3.4.21.48. CAS No. 37288-81-6. 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-4141; cerevisin; EC 3.4.21.48; 37288-81-6; yeast proteinase B; proteinase yscB; baker's yeast proteinase B; brewer's yeast proteinase; peptidase &beta. Cat No: EXWM-4141. | |
| chorismate lyase | This enzyme catalyses the first step in the biosynthesis of ubiquinone in Escherichia coli and other Gram-negative bacteria. The yeast Saccharomyces cerevisiae can synthesize ubiquinone from either chorismate or tyrosine. Group: Enzymes. Synonyms: CL; CPL; UbiC. Enzyme Commission Number: EC 4.1.3.40. CAS No. 157482-18-3. 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-4917; chorismate lyase; EC 4.1.3.40; 157482-18-3; CL; CPL; UbiC. Cat No: EXWM-4917. | |
| crossover junction endodeoxyribonuclease | The enzyme from Saccharomyces cerevisiae has no endonuclease or exonuclease activity on single-stranded or double-stranded DNA molecules that do not contain Holliday junctions. Group: Enzymes. Synonyms: Hje endonuclease; Holliday junction endonuclease CCE1; Holliday junction resolvase; Holliday junction-cleaving endonuclease; Holliday junction-resolving endoribonuclease; RusA Holliday junction resolvase; RusA endonuclease; RuvC endonuclease; SpCCe1 Holliday junction resolvase; crossover junction endoribonuclease; cruciform-cutting endonuclease; endo X3; endonuclease RuvC; endonuclease VII; endonuclease X3; resolving enzyme CCE1. Enzyme Commission Number: EC 3.1.22.4. CAS No. 99676-43-4. 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-3582; crossover junction endodeoxyribonuclease; EC 3.1.22.4; 99676-43-4; Hje endonuclease; Holliday junction endonuclease CCE1; Holliday junction resolvase; Holliday junction-cleaving endonuclease; Holliday junction-resolving endoribonuclease; RusA Holliday junction resolvase; RusA endonuclease; RuvC endonuclease; SpCCe1 Holliday junction resolvase; crossover junction endoribonuclease; cruciform-cutting endonuclease; endo X3; endonuclease RuvC; endonuclease VII; endonuclease X3; resolving enzyme CCE1. Cat No: EXWM-3582. | |
| diacetyl reductase [(R)-acetoin forming] | The reaction is catalysed in the reverse direction. This activity is usually associated with butanediol dehydrogenase activity (EC 1.1.1.4 or EC 1.1.1.76). While the butanediol dehydrogenase activity is reversible, diacetyl reductase activity is irreversible. This enzyme has been reported in the yeast Saccharomyces cerevisiae. Different from EC 1.1.1.304, diacetyl reductase [(S)-acetoin forming]. Group: Enzymes. Synonyms: (R)-acetoin dehydrogenase. Enzyme Commission Number: EC 1.1.1.303. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-0214; diacetyl reductase [(R)-acetoin forming]; EC 1.1.1.303; (R)-acetoin dehydrogenase. Cat No: EXWM-0214. | |
| diacylglycerol diphosphate phosphatase | The bifunctional enzyme catalyses the dephosphorylation of diacylglycerol diphosphate to phosphatidate and the subsequent dephosphorylation of phosphatidate to diacylglycerol (cf. phosphatidate phosphatase (EC 3.1.3.4)). It regulates intracellular levels of diacylglycerol diphosphate and phosphatidate, phospholipid molecules believed to play a signalling role in stress response. The phosphatase activity of the bifunctional enzyme is Mg2+-independent and N-ethylmaleimide-insensitive and is distinct from the Mg2+-dependent and N-ethylmaleimide-sensitive enzyme EC 3.1.3.4 (phosphatidate phosphatase).The diacylglycerol pyrophosphate phosphatase activity in Saccharomyces cerevisiae is induced by zinc depletion, by inositol supplementation, and when cells enter the stationary phase. Group: Enzymes. Synonyms: DGPP phosphatase; DGPP phosphohydrolase; DPP1; DPPL1; DPPL2; PAP2; pyrophosphate phosphatase. Enzyme Commission Number: EC 3.1.3.81. 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-3687; diacylglycerol diphosphate phosphatase; EC 3.1.3.81; DGPP phosphatase; DGPP phosphohydrolase; DPP1; DPPL1; DPPL2; PAP2; pyrophosphate phosphatase. Cat No: EXWM-3687. | |
| diacylglycerol kinase (CTP) | Requires Ca2+ or Mg2+ for activity. Involved in synthesis of membrane phospholipids and the neutral lipid triacylglycerol. Unlike the diacylglycerol kinases from bacteria, plants, and animals [cf. EC 2.7.1.107, diacylglycerol kinase (ATP)], the enzyme from Saccharomyces cerevisiae utilizes CTP. The enzyme can also use dCTP, but not ATP, GTP or UTP. Group: Enzymes. Synonyms: DAG kinase; CTP-dependent diacylglycerol kinase; diglyceride kinase (ambiguous); DGK1 (gene name); diacylglycerol kinase (CTP dependent). Enzyme Commission Number: EC 2.7.1.174. 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-3005; diacylglycerol kinase (CTP); EC 2.7.1.174; DAG kinase; CTP-dependent diacylglycerol kinase; diglyceride kinase (ambiguous); DGK1 (gene name); diacylglycerol kinase (CTP dependent). Cat No: EXWM-3005. | |
| dihydroneopterin aldolase | The enzyme participates in folate (in bacteria, plants and fungi) and methanopterin (in archaea) biosynthesis. The enzymes from the bacterium Escherichia coli and the plant Arabidopsis thaliana also catalyse the epimerisation of the 2' hydroxy-group (EC 5.1.99.8, 7,8-dihydroneopterin epimerase). The enzyme from the bacterium Mycobacterium tuberculosis is trifunctional and also catalyses EC 5.1.99.8 and EC 1.13.11.81, 7,8-dihydroneopterin oxygenase. The enzyme from the yeast Saccharomyces cerevisiae also catalyses the two subsequent steps in the folate biosynthesis pathway - EC 2.7.6.3, 2-amino-4-hydroxy-6-(hydroxymethyl)dihydropteridine diphosphokinase, and EC 2.5.1.15, dihydropteroate synthase. Group: Enzymes. Synonyms: 7,8-dihydroneopterin aldolase; 2-amino-. Enzyme Commission Number: EC 4.1.2.25. CAS No. 37290-59-8. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4864; dihydroneopterin aldolase; EC 4.1.2.25; 37290-59-8; 7,8-dihydroneopterin aldolase; 2-amino-4-hydroxy-6-(D-erythro-1,2,3-trihydroxypropyl)-7,8-dihydropteridine glycolaldehyde-lyase; 2-amino-4-hydroxy-6-(D-erythro-1,2,3-trihydroxypropyl)-7,8-dihydropteridine glycolaldehyde-lyase (2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine-forming); DHNA; mptD (gene name); folB (gene name). Cat No: EXWM-4864. | |
| dihydropteroate synthase | The enzyme participates in the biosynthetic pathways for folate (in bacteria, plants and fungi) and methanopterin (in archaea). The enzyme exists in varying types of multifunctional proteins in different organisms. The enzyme from the plant Arabidopsis thaliana also harbors the activity of EC 2.7.6.3, 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase, while the enzyme from yeast Saccharomyces cerevisiae is trifunctional with the two above mentioned activities as well as EC 4.1.2.25, dihydroneopterin aldolase. Group: Enzymes. Synonyms: dihydropteroate pyrophosphorylase; DHPS; 7,8-dihydropteroate synthase; 7,8-dihydr. Enzyme Commission Number: EC 2.5.1.15. CAS No. 9055-61-2. 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-2751; dihydropteroate synthase; EC 2.5.1.15; 9055-61-2; dihydropteroate pyrophosphorylase; DHPS; 7,8-dihydropteroate synthase; 7,8-dihydropteroate synthetase; 7,8-dihydropteroic acid synthetase; dihydropteroate synthetase; dihydropteroic synthetase; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine-diphosphate:4-aminobenzoate 2-amino-4-hydroxydihydropteridine-6-methenyltransferase; (2-amino-4-hydroxy-7,8-dihydropteridin-6-yl)methyl-diphosphate:4-aminobenzoate 2-amino-4-hydroxydihydropteridine-6-methenyltransferase. Cat No: EXWM-2751. | |
| 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. | |
| GDP-Man:Man1GlcNAc2-PP-dolichol α-1,3-mannosyltransferase | The biosynthesis of asparagine-linked glycoproteins utilizes a dolichyl diphosphate-linked glycosyl donor, which is assembled by the series of membrane-bound glycosyltransferases that comprise the dolichol pathway. Alg2 mannosyltransferase from Saccharomyces cerevisiae carries out an α1,3-mannosylation of D-Man-β-(1?4)-D-GlcNAc-β-(1?4)-D-GlcNAc-diphosphodolichol, followed by an α1,6-mannosylation (cf. EC 2.4.1.257), to form the first branched pentasaccharide intermediate of the dolichol pathway. Group: Enzymes. Synonyms: Alg2 mannosyltransferase (ambiguous); ALG2 (gene name, ambiguous); glycolipid 3-α-mannosyltransferase; GDP-mannose:glycolipid 3-&alph. Enzyme Commission Number: EC 2.4.1.132. CAS No. 81181-76-2. 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-2357; GDP-Man:Man1GlcNAc2-PP-dolichol α-1,3-mannosyltransferase; EC 2.4.1.132; 81181-76-2; Alg2 mannosyltransferase (ambiguous); ALG2 (gene name, ambiguous); glycolipid 3-α-mannosyltransferase; GDP-mannose:glycolipid 3-α-D-mannosyltransferase; GDP-Man:Man1GlcNAc2-PP-Dol α-1,3-mannosyltransferase; GDP-D-mannose:D-Man-β-(1?4)-D-GlcNAc-β-(1?4)-D-GlcNAc-diphosphodolichol 3-α-mannosyltransferase. Cat No: EXWM-2357. | |
| GDP-Man:Man2GlcNAc2-PP-dolichol α-1,6-mannosyltransferase | The biosynthesis of asparagine-linked glycoproteins utilizes a dolichyl diphosphate-linked glycosyl donor, which is assembled by the series of membrane-bound glycosyltransferases that comprise the dolichol pathway. Alg2 mannosyltransferase from Saccharomyces cerevisiae carries out an α1,3-mannosylation (cf. EC 2.4.1.132) of β-D-Man-(1?4)-β-D-GlcNAc-(1?4)-α-D-GlcNAc-diphosphodolichol, followed by an α1,6-mannosylation, to form the first branched pentasaccharide intermediate of the dolichol pathway. Group: Enzymes. Synonyms: GDP-Man:Man2GlcNAc2-PP-Dol α-1,6-mannosyltransferase; Alg2 mannosyltransferase (ambiguous); ALG2 (gene name, ambiguous); GDP-Man:Man1GlcNAc2-PP-dolichol mannosyltransfera. Enzyme Commission Number: EC 2.4.1.257. 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-2487; GDP-Man:Man2GlcNAc2-PP-dolichol α-1,6-mannosyltransferase; EC 2.4.1.257; GDP-Man:Man2GlcNAc2-PP-Dol α-1,6-mannosyltransferase; Alg2 mannosyltransferase (ambiguous); ALG2 (gene name, ambiguous); GDP-Man:Man1GlcNAc2-PP-dolichol mannosyltransferase (ambiguous); GDP-D-mannose:D-Man-α-(1?3)-D-Man-β-(1?4)-D-GlcNAc-β-(1?4)-D-GlcNAc-diphosphodolichol α-6-mannosyltransferase. Cat No: EXWM-2487. | |
| GDP-Man:Man3GlcNAc2-PP-dolichol α-1,2-mannosyltransferase | The biosynthesis of asparagine-linked glycoproteins (N-linked protein glycosylation) utilizes a dolichyl diphosphate-linked glycosyl donor, which is assembled by the series of membrane-bound glycosyltransferases that comprise the dolichol pathway. ALG11 mannosyltransferase from Saccharomyces cerevisiae carries out two sequential steps in the formation of the lipid-linked core oligosaccharide, adding two mannose residues in α(1?2) linkages to the nascent oligosaccharide. Group: Enzymes. Synonyms: ALG11; AL. Enzyme Commission Number: EC 2.4.1.131. CAS No. 74506-43-7. 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-2356; GDP-Man:Man3GlcNAc2-PP-dolichol α-1,2-mannosyltransferase; EC 2.4.1.131; 74506-43-7; ALG11; ALG11 mannosyltransferase; LEW3 (gene name); At2G40190 (gene name); gmd3 (gene name); galactomannan deficiency protein 3; GDP-mannose:glycolipid 1,2-α-D-mannosyltransferase; glycolipid 2-α-mannosyltransferase; GDP-mannose:glycolipid 2-α-D-mannosyltransferase; GDP-Man:Man3GlcNAc2-PP-Dol α-1,2-mannosyltransferase; GDP-α-D-mannose:D-Man-α-(1?3)-[D-Man-α-(1?6)]-D-Man-β-(1?4)-D-GlcNAc-β-(1?4)-D-GlcNAc-diphosphodolichol 2-α-D-mannosyltransferase. Cat No: EXWM-2356. | |
| IMP-specific 5'-nucleotidase | The enzyme, isolated from the yeast Saccharomyces cerevisiae, is highly specific for inosine 5'-phosphate, and has no detectable activity with other purine and pyrimidine nucleotides. Requires divalent metals, such as Mg2+, Co2+ or Mn2+. Group: Enzymes. Synonyms: ISN1 (gene name). Enzyme Commission Number: EC 3.1.3.99. CAS No. 9027-73-0. 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-3706; IMP-specific 5'-nucleotidase; EC 3.1.3.99; 9027-73-0; ISN1 (gene name). Cat No: EXWM-3706. | |
| L-2-aminoadipate reductase | This enzyme, characterized from the yeast Saccharomyces cerevisiae, catalyses the reduction of L-2-aminoadipate to (S)-2-amino-6-oxohexanoate during L-lysine biosynthesis. An adenylation domain activates the substrate at the expense of ATP hydrolysis, and forms L-2-aminoadipate adenylate, which is attached to a peptidyl-carrier protein (PCP) domain. Binding of NADPH results in reductive cleavage of the acyl-S-enzyme intermediate, releasing (S)-2-amino-6-oxohexanoate. Different from EC 1.2.1.31, L-aminoadipate-semialdehyde dehydrogenase, which catalyses a similar transformation in the opposite direction without ATP hydrolysis. Group: Enzymes. Synonyms: LYS2; α-aminoadipate reductase. Enzyme Commission Number: EC 1.2.1.95. 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-1199; L-2-aminoadipate reductase; EC 1.2.1.95; LYS2; α-aminoadipate reductase. Cat No: EXWM-1199. | |
| methylglyoxal reductase (NADPH) | The enzyme from the yeast Saccharomyces cerevisiae catalyses the reduction of a keto group in a number of compounds, forming enantiopure products. Among the substrates are methylglyoxal (which is reduced to (S)-lactaldehyde), 3-methylbutanal, hexane-2,5-dione and 3-chloro-1-phenylpropan-1-one. The enzyme differs from EC 1.1.1.78, methylglyoxal reductase (NADH), which is found in mammals, by its coenzyme requirement, reaction direction, and enantiomeric preference. Group: Enzymes. Synonyms: lactaldehyde dehydrogenase (NADP+); GRE2 (gene name); methylglyoxal reductase (NADPH-dependent); lactaldehyde:NADP+ oxidoreductase. Enzyme Commission Number: EC 1.1.1.283. CAS No. 78310-66-4. 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-0191; methylglyoxal reductase (NADPH); EC 1.1.1.283; 78310-66-4; lactaldehyde dehydrogenase (NADP+); GRE2 (gene name); methylglyoxal reductase (NADPH-dependent); lactaldehyde:NADP+ oxidoreductase. Cat No: EXWM-0191. | |
| multisite-specific tRNA:(cytosine-C5)-methyltransferase | The enzyme from Saccharomyces cerevisiae is responsible for complete 5-methylcytosine methylations of yeast tRNA. The incidence of modification depends on the cytosine position in tRNA. At positions 34 and 40, 5-methylcytosine is found only in two yeast tRNAs (tRNALeu(CUA) and tRNAPhe(GAA), respectively), whereas most other elongator yeast tRNAs bear either 5-methylcytosine48 or 5-methylcytosine49, but never both in the same tRNA molecule. The formation of 5-methylcytosine34 and 5-methylcytosine40 is a strictly intron-dependent process, whereas the formation of 5-methylcytosine48 and 5-methylcytosine49 is an intron-independent process. Group: Enzymes. Synonyms: multisite-specific tRNA:m5C-methyltransferase; TRM4 (gene name, gene corresponding to ORF YBL024w). Enzyme Commission Number: EC 2.1.1.202. 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-1803; multisite-specific tRNA:(cytosine-C5)-methyltransferase; EC 2.1.1.202; multisite-specific tRNA:m5C-methyltransferase; TRM4 (gene name, gene corresponding to ORF YBL024w). Cat No: EXWM-1803. | |
| Native Arthrobacter luteus Lyticase | Lyticase hydrolyzes poly-β (1?3)-glucose such as yeast cell wall glucan. Applications: Yeast cells are difficult to disrupt because the cell walls may form capsules or resistant spores. dna can be extracted from yeast by using lysing enzymes such as lyticase, chitinase, zymolase, and gluculase to induce partial spheroplast formation; spheroplasts are subsequently lysed to release dna. lyticase is preferred to digest cell walls of yeast and generate spheroplasts from fungi for transformation. reported to be useful for lysis of ashbya, candida, debaryomyces, eremothecium, endomyces, hansenula, hanseniaspora, kloeckera, kluyveromyces, lipomyces, metschikowia, pichia, pullularia, torulopsis, saccharomyces, saccharomycopsis, saccharomycodes, and schwanniomyces species. Group: Enzymes. Synonyms: Lyticase; 37340-57-1. CAS No. 37340-57-1. Lyticase. Activity: > 200 units/mg solid; > 1,500 units/mg protein; > 2,000 units/mg protein, Protein > 20 % by biuret. Storage: 2-8°C. Form: lyophilized powder. Source: Arthrobacter luteus. Lyticase; 37340-57-1. Cat No: NATE-0431. | |
| Native Bacillus amyloliquefaciens α-Amylase | α-Amylase is a protein enzyme EC 3.2.1.1 that hydrolyses alpha bonds of large, alpha-linked polysaccharides, such as starch and glycogen, yielding glucose and maltose. It is the major form of amylase found in Humans and other mammals. It is also present in seeds containing starch as a food reserve, and is secreted by many fungi. Applications: Α-amylase is used to hydrolyze α bonds of α-linked polysaccharides, such as starch and glycogen. this product is from bacillus amyloliquefaciens and is supplied as a liquid. α-amylase has been used in various plant studies, such as metabolism studies in arabidopsis. α-amylase from bacillus amy...ng sugars, which are then used for ethanol fermentation by saccharomyces cerevisiae fncc 3012. the enzyme catalyzes amylolysis of gelatinised waxy maize starch to produce reducing sugars. Group: Enzymes. Synonyms: glycogenase; αamylase, α-amylase; 1,4-α-D-glucan glucanohydrolase; EC 3.2.1.1; 9001-19-8; endoamylase; Taka-amylase A. Enzyme Commission Number: EC 3.2.1.1. CAS No. 9001-19-8. α-Amylase. Mole weight: 55 kDa. Activity: > 250 units/g. Form: liquid. Source: Bacillus amyloliquefaciens. glycogenase; αamylase, α-amylase; 1,4-α-D-glucan glucanohydrolase; EC 3.2.1.1; 9001-19-8; endoamylase; Taka-amylase A. Cat No: NATE-0741. | |
| Native Baker's yeast (S. cerevisiae) Nucleoside 5'-Diphosphate Kinase | Nucleoside 5'-diphosphate kinase is a cytosolic enzyme. Nucleoside 5'-diphosphate kinase from Saccharomyces cerevisiae is found highly expressed in the cytoplasm. It affects DNA synthesis, in part, by binding to Cdc8p. Nucleoside 5?-diphosphate kinase is a cytosolic enzyme. Applications: Nucleoside 5?-diphosphate kinase has been used in a study to examine a possible intracellular activity of the drug disodium cromoglycate in mast cells. it has also been used in a study to investigate protein synthesis in rabbit reticul ocytes. Group: Enzymes. Synonyms: nucleoside 5'-diphosphate kinase; nucleoside diphosphate (UDP) kinase; nucleoside diphosphokinase; nucleotide phosphate kinase; UDP kinase; uridine diphosphate kinase; nucleoside-diphosphate kinase; EC 2.7.4.6; 9026-51-1; NDPK. Enzyme Commission Number: EC 2.7.4.6. CAS No. 9026-51-1. NDPK. Storage: -20°C. Form: lyophilized powder; essentially sulfate-free powder. Contains sodium Citrate with a trace of magnesium and EDTA salts. Source: Baker's yeast (S. cerevisiae). nucleoside 5'-diphosphate kinase; nucleoside diphosphate (UDP) kinase; nucleoside diphosphokinase; nucleotide phosphate kinase; UDP kinase; uridine diphosphate kinase; nucleoside-diphosphate kinase; EC 2.7.4.6; 9026-51-1; NDPK. Cat No: NATE-0476. | |
| Native Saccharomyces cerevisiae Alcohol Dehydrogenase | Alcohol dehydrogenases (ADH) are a group of dehydrogenase enzymes that occur in many organisms and facilitate the interconversion between alcohols and aldehydes or ketones with the reduction of nicotinamide adenine dinucleotide (NAD+ to NADH). In Humans and many other animals, they serve to break down alcohols that otherwise are toxic, and they also participate in geneRation of useful aldehyde, ketone, or alcohol groups during biosynthesis of various metabolites. In yeast, plants, and many bacteria, some alcohol dehydrogenases catalyze the opposite reaction as part of fermentation to ensure a constant supply of NAD+. Applications: Alcohol dehydrogenase from sacchar...dehydrogenase; NADH-alcohol dehydrogenase; NADH-aldehyde dehydrogenase; primary alcohol dehydrogenase; yeast alcohol dehydrogenase; EC 1.1.1.1. Enzyme Commission Number: EC 1.1.1.1. CAS No. 9031-72-5. Activity: > 300 units/mg protein. Storage: -20°C. Form: Solids containing <2% Citrate buffer salts. Source: Saccharomyces cerevisiae. aldehyde reductase; ADH; alcohol dehydrogenase (NAD); aliphatic alcohol dehydrogenase; ethanol dehydrogenase; NAD-dependent alcohol dehydrogenase; NAD-specific aromatic alcohol dehydrogenase; NADH-alcohol dehydrogenase; NADH-aldehyde dehydrogenase; primary alcohol dehydrogenase; yeast alcohol dehydrogenase; EC 1.1.1.1. Cat No: NATE-0035. | |
| Native Saccharomyces cerevisiae Hexokinase | A hexokinase is an enzyme that phosphorylates hexoses (six-carbon sugars), forming hexose phosphate. In most organisms, glucose is the most important substrate of hexokinases, and glucose-6-phosphate the most important product. Hexokinase can transfer an inorganic phosphate group from ATP to a substrate. Hexokinases should not be confused with glucokinase, which is a specific isoform of hexokinase. While other hexokinases are capable of phosphorylating several hexoses, glucokinase acts with a 50-fold lower substrate affinity and its only hexose substrate is glucose. Group: Enzymes. Synonyms: hexokinase type IV glucokinase; hexokinase D; hexokinase type IV. Enzyme Commission Number: EC 2.7.1.1. CAS No. 9001-51-8. Hexokinase. Mole weight: ~ 54 kDa (monomer); ~110 kDa (dimer). Activity: Type I, > 350 units/mg protein; Type II, > 25 units/mg protein (biuret); Type III, > 130 units/mg protein (biuret). Storage: -20°C. Form: Type I, Lyophilized powder containing phosphate/Citrate pH approx. 7.0; Type II, Type III, Lyophilized powder containing approx. 15% sodium Citrate. Source: Saccharomyces cerevisiae. hexokinase type IV glucokinase; hexokinase D; hexokinase type IV; hexokinase (phosphorylating); ATP-dependent hexokinase; glucose ATP phosphotransferase; hexokinase; ATP:D-hexose 6-phosphotransferase; EC 2.7.1.1; 9001-51-8. Cat No: NATE-0342. | |
| Native Wheat Carboxypeptidase W | Carboxypeptidase D can refer to one of several enzymes. A family of serine carboxypeptidases (i.e. enzymes that use an active site serine residue) includes (EC 3.4.16.6, cereal serine carboxypeptidase II, Saccharomyces cerevisiae KEX1 gene product, carboxypeptidase Kex1, gene KEX1 serine carboxypeptidase, KEX1 carboxypeptidase, KEX1 proteinase, KEX1DELTAp, CPDW-II, serine carboxypeptidase, Phaseolus proteinase) is an enzyme. This enzyme has an optimal pH of 4.5-6.0, is inhibited by diisopropyl fluorophosphate. Applications: Carboxypeptidase w from wheat has been used in a study to assess the proteolytic activities in dormant rye (secale cereale l.) grain. carboxypeptidase w from wheat has also been used in a study to investigate the structure determination of the human protective protein. Group: Enzymes. Synonyms: Carboxypeptidase W; 9046-67-7; EC 3.4.16.6; carboxypeptidase D; cereal. Enzyme Commission Number: EC 3.4.16.6. CAS No. 9046-67-7. CPDW-II. Activity: > 50 units/mg protein. Storage: -20°C. Source: Wheat. Carboxypeptidase W; 9046-67-7; EC 3.4.16.6; carboxypeptidase D; cereal serine carboxypeptidase II; Saccharomyces cerevisiae KEX1 gene product; carboxypeptidase Kex1; gene KEX1 serine carboxypeptidase; KEX1 carboxypeptidase; KEX1 proteinase; KEX1DELTAp; CPDW-II; serine carboxypeptidase (misleading); Phaseolus proteinase. Cat No: NATE-0154. | |
| non-specific polyamine oxidase | A flavoprotein (FAD). The non-specific polyamine oxidases may differ from each other considerably. The enzyme from Saccharomyces cerevisiae shows a rather broad specificity and also oxidizes N8-acetylspermidine. The enzyme from Ascaris suum shows high activity with spermine and spermidine, but also oxidizes norspermine. The enzyme from Arabidopsis thaliana shows high activity with spermidine, but also oxidizes other polyamines.The specific polyamine oxidases are classified as EC 1.5.3.13 (N1-acetylpolyamine oxidase), EC 1.5.3.14 (polyamine oxidase (propane-1,3-diamine-forming)), EC 1.5.3.15 (N8-acetylspermidine oxidase (propane-1,3-diamine-forming)) and EC 1.5.3.16 (spermine oxidase). Group: Enzymes. Synonyms: polyamine oxidase (ambiguous); Fms1; AtPAO3. Enzyme Commission Number: EC 1.5.3.17. 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-1544; non-specific polyamine oxidase; EC 1.5.3.17; polyamine oxidase (ambiguous); Fms1; AtPAO3. Cat No: EXWM-1544. | |
| phosphoglycerate mutase (2,3-diphosphoglycerate-dependent) | The enzymes from vertebrates, platyhelminths, mollusks, annelids, crustaceans, insects, algae, fungi, yeast and some bacteria (particularly Gram-negative) require 2,3-bisphospho-D-glycerate as a cofactor. The enzyme is activated by 2,3-bisphospho-D-glycerate by transferring a phosphate to histidine (His10 in man and Escherichia coli, His8 in Saccharomyces cerevisiae). This phosphate can be transferred to the free OH of 2-phospho-D-glycerate, followed by transfer of the phosphate already on the phosphoglycerate back to the histidine. cf. EC 5.4.2.12 phosphoglycerate mutase. The enzyme has no requirement for metal ions. This enzyme also catalyse, slowly, the reacti... dPGM. Enzyme Commission Number: EC 5.4.2.11. 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-5522; phosphoglycerate mutase (2,3-diphosphoglycerate-dependent); EC 5.4.2.11; glycerate phosphomutase (diphosphoglycerate cofactor); 2,3-diphosphoglycerate dependent phosphoglycerate mutase; cofactor dependent phosphoglycerate mutase; phosphoglycerate phosphomutase (ambiguous); phosphoglyceromutase (ambiguous); monophosphoglycerate mutase (ambiguous); monophosphoglyceromutase (ambiguous); GriP mutase (ambiguous); PGA mutase (ambiguous); MPGM; PGAM; PGAM-d; PGM; dPGM. Cat No: EXWM-5522. | |
| phospholipid:diacylglycerol acyltransferase | This enzyme differs from EC 2.3.1.20, diacylglycerol O-acyltransferase, by synthesising triacylglycerol using an acyl-CoA-independent mechanism. The specificity of the enzyme for the acyl group in the phospholipid varies with species, e.g., the enzyme from castor bean (Ricinus communis) preferentially incorporates vernoloyl (12,13-epoxyoctadec-9-enoyl) groups into triacylglycerol, whereas that from the hawk's beard (Crepis palaestina) incorporates both ricinoleoyl (12-hydroxyoctadec-9-enoyl) and vernoloyl groups. The enzyme from the yeast Saccharomyces cerevisiae specifically transfers acyl groups from the sn-2 position of the phospholipid to diacylglycerol, thus forming an sn-1-lysophospholipid. Group: Enzymes. Synonyms: PDAT. Enzyme Commission Number: EC 2.3.1.158. CAS No. 288587-47-3. 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-2097; phospholipid:diacylglycerol acyltransferase; EC 2.3.1.158; 288587-47-3; PDAT. Cat No: EXWM-2097. | |
| polyprenyldihydroxybenzoate methyltransferase | This enzyme is involved in ubiquinone biosynthesis. Ubiquinones from different organisms have a different number of prenyl units (for example, ubiquinone-6 in Saccharomyces, ubiquinone-9 in rat and ubiquinone-10 in human), and thus the natural substrate for the enzymes from different organisms has a different number of prenyl units. However, the enzyme usually shows a low degree of specificity regarding the number of prenyl units. For example, the human COQ3 enzyme can restore biosynthesis of ubiquinone-6 in coq3 deletion mutants of yeast. The enzymes from yeast and rat also catalyse the methylation of 3-demethylubiquinol-6 and 3-demethylubiquinol-9, respectively (this activity is classified as EC 2.1.1.64, 3-demethylubiquinol 3-O-methyltransferase). Group: Enzymes. Synonyms: 3,4-dihydroxy-5-hexaprenylbenzoate methyltransferase; dihydroxyhexaprenylbenzoate methyltransferase; C. Enzyme Commission Number: EC 2.1.1.114. CAS No. 139569-31-6. 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-1713; polyprenyldihydroxybenzoate methyltransferase; EC 2.1.1.114; 139569-31-6; 3,4-dihydroxy-5-hexaprenylbenzoate methyltransferase; dihydroxyhexaprenylbenzoate methyltransferase; COQ3 (gene name); Coq3 O-methyltransferase; DHHB O-methyltransferase. Cat No: EXWM-1713. | |
| precorrin-2 dehydrogenase | This enzyme catalyses the second of three steps leading to the formation of siroheme from uroporphyrinogen III. The first step involves the donation of two S-adenosyl-L-methionine-derived methyl groups to carbons 2 and 7 of uroporphyrinogen III to form precorrin-2 (EC 2.1.1.107, uroporphyrin-III C-methyltransferase) and the third step involves the chelation of ferrous iron to sirohydrochlorin to form siroheme (EC 4.99.1.4, sirohydrochlorin ferrochelatase). In Saccharomyces cerevisiae, the last two steps are carried out by a single bifunctional enzyme, Met8p. In some bacteria, steps 1-3 are catalysed by a single multifunctional protein called CysG, whereas in Bacillus megaterium, three separate enzymes carry out each of the steps, with SirC being responsible for the above reaction. Group: Enzymes. Synonyms: Met8p; SirC; CysG. Enzyme Commission Number: EC 1.3.1.76. CAS No. 227184-47-6. 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-1345; precorrin-2 dehydrogenase; EC 1.3.1.76; 227184-47-6; Met8p; SirC; CysG. Cat No: EXWM-1345. | |
| saccharolysin | An 83 kDa cytoplasmic thiol-dependent metalloendopeptidase from Saccharomyces cerevisiae. In peptidase family M3 (thimet oligopeptidase family). Group: Enzymes. Synonyms: proteinase yscD; yeast cysteine proteinase D (Misleading); Saccharomyces cerevisiae proteinase yscD. Enzyme Commission Number: EC 3.4.24.37. CAS No. 96779-48-5. 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-4319; saccharolysin; EC 3.4.24.37; 96779-48-5; proteinase yscD; yeast cysteine proteinase D (Misleading); Saccharomyces cerevisiae proteinase yscD. Cat No: EXWM-4319. | |
| sirohydrochlorin ferrochelatase | This enzyme catalyses the third of three steps leading to the formation of siroheme from uroporphyrinogen III. The first step involves the donation of two S-adenosyl-L-methionine-derived methyl groups to carbons 2 and 7 of uroporphyrinogen III to form precorrin-2 (EC 2.1.1.107, uroporphyrin-III C-methyltransferase) and the second step involves an NAD+-dependent dehydrogenation to form sirohydrochlorin from precorrin-2 (EC 1.3.1.76, precorrin-2 dehydrogenase). In Saccharomyces cerevisiae, the last two steps are carried out by a single bifunctional enzyme, Met8p. In some bacteria, steps 1-3 are catalysed by a single multifunctional protein called CysG, whereas in Bacillus megaterium, three separate enzymes carry out each of the steps, with SirB being responsible for the above reaction. Group: Enzymes. Synonyms: CysG; Met8P; SirB; sirohydrochlorin ferro-lyase (incorrect). Enzyme Commission Number: EC 4.99.1.4. 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-5361; sirohydrochlorin ferrochelatase; EC 4.99.1.4; CysG; Met8P; SirB; sirohydrochlorin ferro-lyase (incorrect). Cat No: EXWM-5361. | |
| SUMO Protease 1 (GST-tagged) from Yeast, Recombinant | SUMO (Small Ubiquitin-like MOdifiers) Protease 1 (Ulp1, Ubl-specific protease 1 from Saccharomyces cerevisiae) is a highly active cysteine protease. It is highly specific as it recognizes the tertiary structure of the ubiquitin-like (UBL) protein, SUMO (Smt3), rather than its amino acid sequence. SUMO fusion tag, as an N-terminal fusion partner, has been shown to enhance functional protein production in prokaryotic and eukaryotic expression systems with significantly improved protein stability and solubility. The SUMO protease 1 can be used to cleave SUMO protein tag from recombinant SUMO-fusion proteins. The optimal temperature for cleavage is 30°C; however, the en...eaction by affinity chromatography using the Glutathione resin. Group: Enzymes. Synonyms: Ulp1 peptidase; SUMO Protease; SUMO Protease. Enzyme Commission Number: EC 3.4.22.68. Purity: > 90% by SDS-PAGE. Mole weight: 52.6 kDa (403-621 aa + N-terminal GST). Activity: >10,000 units/mg. Storage: Store at -80°C. Stable for at least 1 year as supplied. It may be further diluted to 0.1-0.5 mg/ml with 50 mM Tris-HCl, 100 mM NaCl, 5 mM DTT and 20% glycerol pH 8.0 and stored at -20°C in aliquots. Avoid repeated freezing and thawing cycles. Form: Liquid. Source: E. coli. Species: Yeast. Ulp1 peptidase; SUMO Protease; SUMO Protease; SUMO Protease 1; Protease. Cat No: NATE-1708. | |
| SUMO Protease 1 (His-tagged) from Yeast, Recombinant | SUMO (Small Ubiquitin-like MOdifiers) Protease 1 (Ulp1, Ubl-specific protease 1 from Saccharomyces cerevisiae) is a highly active cysteine protease. It is highly specific as it recognizes the tertiary structure of the ubiquitin-like (UBL) protein, SUMO (Smt3), rather than its amino acid sequence. SUMO fusion tag, as an N-terminal fusion partner, has been shown to enhance functional protein production in prokaryotic and eukaryotic expression systems with significantly improved protein stability and solubility. The SUMO Protease 1 can be used to cleave SUMO protein tag from recombinant SUMO-fusion proteins. The optimal temperature for cleavage is 30°C; however, the en...finity chromatography using the Ni chelating resin. Group: Enzymes. Synonyms: Ulp1 peptidase; SUMO Protease; SUMO Protease. Enzyme Commission Number: EC 3.4.22.68. Purity: > 90% by SDS-PAGE. Mole weight: 28.7 kDa (403-621 aa + N-terminal Poly-His tag). Activity: 1 X 10^6 units/mg. Storage: Store at -80°C. Stable for at least 1 year as supplied. It may be further diluted to 0.01-0.05 mg/ml with 50 mM Tris-HCl, 100 mM NaCl, 5 mM DTT and 20% glycerol pH 8.0 and stored at -20°C in aliquots. Avoid repeated freezing and thawing cycles. Form: Liquid. Source: E. coli. Species: Yeast. Ulp1 peptidase; SUMO Protease; SUMO Protease; SUMO Protease 1; Protease. Cat No: NATE-1709. | |
| trans-aconitate 2-methyltransferase | Also catalyses the formation of the methyl monoester of cis-aconitate, isocitrate and citrate, but more slowly. While the enzyme from Escherichia coli forms (E)-3-(methoxycarbonyl)-pent-2-enedioate as the product, that from Saccharomyces cerevisiae forms (E)-2-(methoxycarbonylmethyl)butenedioate and is therefore classified as a separate enzyme (cf. EC 2.1.1.145, trans-aconitate 3-methyltransferase). Group: Enzymes. Enzyme Commission Number: EC 2.1.1.144. CAS No. 235107-12-7. 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-1740; trans-aconitate 2-methyltransferase; EC 2.1.1.144; 235107-12-7. Cat No: EXWM-1740. | |
| trans-aconitate 3-methyltransferase | Also catalyses the formation of the methyl monoester of cis-aconitate, isocitrate and citrate, but more slowly. While the enzyme from Saccharomyces cerevisiae forms (E)-2-(methoxycarbonylmethyl)butenedioate as the product, that from Escherichia coli forms (E)-3-(methoxycarbonyl)-pent-2-enedioate and is therefore classified as a separate enzyme (cf. EC 2.1.1.144, trans-aconitate 2-methyltransferase). Group: Enzymes. Enzyme Commission Number: EC 2.1.1.145. CAS No. 235107-12-7. 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-1741; trans-aconitate 3-methyltransferase; EC 2.1.1.145; 235107-12-7. Cat No: EXWM-1741. | |
| [trehalose-6-phosphate synthase]-L-cysteine S-methyltransferase | The enzyme, characterized from the yeast Saccharomyces cerevisiae, enhances the activity of EC 2.4.1.15, trehalose-6-phosphate synthase, resulting in elevating the levels of trehalose in the cell and contributing to stationary phase survival. In vitro the enzyme performs S-methylation of L-cysteine residues of various protein substrates. Group: Enzymes. Enzyme Commission Number: EC 2.1.1.318. 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-1926; [trehalose-6-phosphate synthase]-L-cysteine S-methyltransferase; EC 2.1.1.318. Cat No: EXWM-1926. | |
| tRNA (cytidine32/guanosine34-2'-O)-methyltransferase | The enzyme from Saccharomyces cerevisiae catalyses the formation of 2'-O-methylnucleotides at positions 32 and 34 of the yeast tRNAPhe, tRNATrp and, possibly, tRNALeu. Group: Enzymes. Synonyms: Trm7p. Enzyme Commission Number: EC 2.1.1.205. 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-1806; tRNA (cytidine32/guanosine34-2'-O)-methyltransferase; EC 2.1.1.205; Trm7p. Cat No: EXWM-1806. | |
| tRNA (guanine9-N1)-methyltransferase | The enzyme from Saccharomyces cerevisiae specifically methylates guanine9. The bifunctional enzyme from Thermococcus kodakaraensis also catalyses the methylation of adenine9 in tRNA (cf. EC 2.1.1.218, tRNA (adenine9-N1)-methyltransferase). Group: Enzymes. Synonyms: Trm10p (ambiguous); tRNA(m1G9/m1A9)-methyltransferase; tRNA(m1G9/m1A9)MTase; tRNA (guanine-N(1)-)-methyltransferase; tRNA m1G9-methyltransferase; tRNA m1G9 MTase. Enzyme Commission Number: EC 2.1.1.221. 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-1824; tRNA (guanine9-N1)-methyltransferase; EC 2.1.1.221; Trm10p (ambiguous); tRNA(m1G9/m1A9)-methyltransferase; tRNA(m1G9/m1A9)MTase; tRNA (guanine-N(1)-)-methyltransferase; tRNA m1G9-methyltransferase; tRNA m1G9 MTase. Cat No: EXWM-1824. | |
| tRNA:m4X modification enzyme | The enzyme from Saccharomyces cerevisiae 2'-O-methylates cytidine4 in tRNAPro and tRNAGly(GCC), and adenosine4 in tRNAHis. Group: Enzymes. Synonyms: TRM13; Trm13p; tRNA:Xm4 modification enzyme. Enzyme Commission Number: EC 2.1.1.225. 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-1828; tRNA:m4X modification enzyme; EC 2.1.1.225; TRM13; Trm13p; tRNA:Xm4 modification enzyme. Cat No: EXWM-1828. | |
| tRNA pseudouridine13 synthase | Pseudouridine synthase TruD from Escherichia coli specifically acts on uridine13 in tRNA. The Pus7 protein from Saccharomyces cerevisiae is a multisite-multisubstrate pseudouridine synthase that is able to modify uridine13 in several yeast tRNAs, uridine35 in the pre-tRNATyr, uridine35 in U2 small nuclear RNA, and uridine50 in 5S rRNA. Group: Enzymes. Synonyms: TruD; YgbO; tRNA PSI13 synthase; RNA:PSI-synthase Pus7p; Pus7p; RNA:pseudouridine-synthase Pus7p; Pus7 protein. Enzyme Commission Number: EC 5.4.99.27. CAS No. 430429-15-5. 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-5567; tRNA pseudouridine13 synthase; EC 5.4.99.27; 430429-15-5; TruD; YgbO; tRNA PSI13 synthase; RNA:PSI-synthase Pus7p; Pus7p; RNA:pseudouridine-synthase Pus7p; Pus7 protein. Cat No: EXWM-5567. | |
| tRNA pseudouridine38/39 synthase | The enzyme from Saccharomyces cerevisiae is active only towards uridine38 and uridine39, and shows no activity with uridine40 (cf. EC 5.4.99.12, tRNA pseudouridine38-40 synthase). In vitro the enzyme from mouse is active on uridine39 and very slightly on uridine38 (human tRNALeu). Group: Enzymes. Synonyms: Deg1; Pus3p; pseudouridine synthase 3. Enzyme Commission Number: EC 5.4.99.45. 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-5587; tRNA pseudouridine38/39 synthase; EC 5.4.99.45; Deg1; Pus3p; pseudouridine synthase 3. Cat No: EXWM-5587. | |
| tRNAThr (cytosine32-N3)-methyltransferase | The enzyme from Saccharomyces cerevisiae specifically methylates cytosine32 in tRNAThr and in tRNASer. Group: Enzymes. Synonyms: ABP140; Trm140p. Enzyme Commission Number: EC 2.1.1.268. 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-1873; tRNAThr (cytosine32-N3)-methyltransferase; EC 2.1.1.268; ABP140; Trm140p. Cat No: EXWM-1873. | |
| type IV protein arginine methyltransferase | This enzyme, characterized from the yeast Saccharomyces cerevisiae, methylates the the Δ-nitrogen atom of arginine residues within proteins. Among its substrates are Arg67 of the ribosomal protein L12. cf. EC 2.1.1.319, type I protein arginine methyltransferase, EC 2.1.1.320, type II protein arginine methyltransferase, and EC 2.1.1.321, type III protein arginine methyltransferase. Group: Enzymes. Synonyms: RMT2 (gene name). Enzyme Commission Number: EC 2.1.1.322. 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-1930; type IV protein arginine methyltransferase; EC 2.1.1.322; RMT2 (gene name). Cat No: EXWM-1930. | |
| Ulp1 peptidase | The enzyme from Saccharomyces cerevisiae can also recognize small ubiquitin-like modifier 1 (SUMO-1) from human as a substrate in both SUMO-processing (α-linked peptide bonds) and SUMO-deconjugation (ε-linked peptide bonds) reactions. Ulp1 has several functions, including an essential role in chromosomal segregation and progression of the cell cycle through the G2/M phase of the cell cycle. Belongs in peptidase family C48. Group: Enzymes. Synonyms: Smt3-protein conjugate proteinase; Ubl-specific protease 1; Ulp1; Ulp1 endopeptidase; Ulp1 protease. Enzyme Commission Number: EC 3.4.22.68. 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-4244; Ulp1 peptidase; EC 3.4.22.68; Smt3-protein conjugate proteinase; Ubl-specific protease 1; Ulp1; Ulp1 endopeptidase; Ulp1 protease. Cat No: EXWM-4244. | |
| uroporphyrinogen-III C-methyltransferase | This enzyme catalyses two sequential methylation reactions, the first forming precorrin-1 and the second leading to the formation of precorrin-2. It is the first of three steps leading to the formation of siroheme from uroporphyrinogen III. The second step involves an NAD+-dependent dehydrogenation to form sirohydrochlorin from precorrin-2 (EC 1.3.1.76, precorrin-2 dehydrogenase) and the third step involves the chelation of Fe2+ to sirohydrochlorin to form siroheme (EC 4.99.1.4, sirohydrochlorin ferrochelatase). In Saccharomyces cerevisiae, the last two steps are carried out by a single bifunctional enzyme, Met8p. In some bacteria, steps 1-3 are catalysed by a single mult...(incorrect). Enzyme Commission Number: EC 2.1.1.107. CAS No. 125752-76-3. 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-1705; uroporphyrinogen-III C-methyltransferase; EC 2.1.1.107; 125752-76-3; uroporphyrinogen methyltransferase; uroporphyrinogen-III methyltransferase; adenosylmethionine-uroporphyrinogen III methyltransferase; S-adenosyl-L-methionine-dependent uroporphyrinogen III methylase; uroporphyrinogen-III methylase; SirA; CysG; CobA [ambiguous - see EC 2.5.1.17] SUMT; uroporphyrin-III C-methyltransferase (incorrect); S-adenosyl-L-methionine:uroporphyrin-III C-methyltransferase | |
| 25S rRNA (adenine2142-N1)-methyltransferase | In the yeast Saccharomyces cerevisiae this methylation is important for resistance towards hydrogen peroxide and the antibiotic anisomycin. Group: Enzymes. Synonyms: BMT2 (gene name); 25S rRNA m1A2142 methyltransferase. Enzyme Commission Number: EC 2.1.1.286. 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-1893; 25S rRNA (adenine2142-N1)-methyltransferase; EC 2.1.1.286; BMT2 (gene name); 25S rRNA m1A2142 methyltransferase. Cat No: EXWM-1893. | |
| 25S rRNA (adenine645-N1)-methyltransferase | The enzyme is found in eukaryotes. The adenine position refers to rRNA in the yeast Saccharomyces cerevisiae, in which the enzyme is important for ribosome biogenesis. Group: Enzymes. Synonyms: 25S rRNA m1A645 methyltransferase; Rrp8. Enzyme Commission Number: EC 2.1.1.287. 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-1894; 25S rRNA (adenine645-N1)-methyltransferase; EC 2.1.1.287; 25S rRNA m1A645 methyltransferase; Rrp8. Cat No: EXWM-1894. | |
| 2-methylisocitrate dehydratase | The enzyme from the fungus Yarrowia lipolytica (Saccharomycopsis) does not act on isocitrate. Group: Enzymes. Synonyms: (2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate hydro-lyase. Enzyme Commission Number: EC 4.2.1.99. CAS No. 170780-51-5. 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-5083; 2-methylisocitrate dehydratase; EC 4.2.1.99; 170780-51-5; (2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate hydro-lyase. Cat No: EXWM-5083. | |
| 2'-phosphotransferase | Catalyses the final step of tRNA splicing in the yeast Saccharomyces cerevisiae. The reaction takes place in two steps: in the first step, the 2'-phosphate on the RNA substrate is ADP-ribosylated, causing the relase of nicotinamide and the formation of the reaction intermediate, ADP-ribosylated tRNA. In the second step, dephosphorylated (mature) tRNA is formed along with ADP ribose 1''-2''-cyclic phosphate. Highly specific for oligonucleotide substrates bearing an internal 2'-phosphate. Oligonucleotides with only a terminal 5'- or 3'-phosphate are not substrates. Group: Enzymes. Synonyms: yeast 2'-phosphotransferase; Tpt1; Tpt1p; 2'-phospho-tRNA:NAD+ phosphotransferase. Enzyme Commission Number: EC 2.7.1.160. CAS No. 126905-00-8. 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-2990; 2'-phosphotransferase; EC 2.7.1.160; 126905-00-8; yeast 2'-phosphotransferase; Tpt1; Tpt1p; 2'-phospho-tRNA:NAD+ phosphotransferase. Cat No: EXWM-2990. | |
| 5-Fluoroorotic Acid Monohydrate (FOA, 5-FOA) | Useful in the identification and selection of the strains of Saccharomyces cerevisiae that contain the mutant ura3- gene. 5-FOA is toxic to yeast cells that can synthesize the enzyme orotidine-5-phosphate decarboxylase and are therefore unable to grow on 5-FOA-containing media. Group: Biochemicals. Alternative Names: FOA; 5-FOA; 5-Fluoroorotate; 5-FLUORO-4-PYRIMIDINECARBOXYLIC ACID; 5-FLUORO-1,2,3,6-TETRAHYDRO-2,6-DIOXO-(9CI); 1,2,3,6-TETRAHYDRO-2,6-DIOXO-5-FLUORO-4- PYRIMIDINECARBOXYLIC ACID; 2,6-Dihydroxy-5-fluoropyrimidine-4-carboxylic acid; 5-Fluorouracil-4-carboxylic acid. Grades: Molecular Biology Grade. CAS No. 207291-81-4,220141-70-8,703-95-7. Pack Sizes: 500mg, 1g, 10g, 25g, 50g, 100g. US Biological Life Sciences. |  Worldwide |
| Alcohol dehydrogenase, Saccharomyces cerevisiae | Alcohol dehydrogenase, Saccharomyces cerevisiae is a dimeric protein in the cytosol of cells. Alcohol dehydrogenase, the key enzyme for alcohol consumption in the body, is the highest expressed in the liver and participates in the detoxification mechanism of environmental alcohol [1]. Uses: Scientific research. Group: Signaling pathways. Alternative Names: EC 1.1.1.1. CAS No. 9031-72-5. Pack Sizes: 25 KU. Product ID: HY-P2740. |  |
| aminopeptidase I | A 640-kDa, dodecameric enzyme best known as the major vacuolar aminopeptidase of yeast, Saccharomyces cervisiae, in which species it was first given the name aminopeptidase I (one), amongst others. Activity is stimulated by both Zn2+ and Cl- ions. Type example of peptidase family M18. Group: Enzymes. Synonyms: aminopeptidase III; aminopeptidase yscI; leucine aminopeptidase IV; yeast aminopeptidase I. Enzyme Commission Number: EC 3.4.11.22. CAS No. 9031-94-1. Aminopeptidase I. 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-4019; aminopeptidase I; EC 3.4.11.22; 9031-94-1; aminopeptidase III; aminopeptidase yscI; leucine aminopeptidase IV; yeast aminopeptidase I. Cat No: EXWM-4019. | |
| carboxypeptidase D | A carboxypeptidase with optimum pH 4.5-6.0, inhibited by diisopropyl fluorophosphate, and sensitive to thiol-blocking reagents (reviewed in). In peptidase family S10 (carboxypeptidase C family). Group: Enzymes. Synonyms: cereal serine carboxypeptidase II; Saccharomyces cerevisiae KEX1 gene product; carboxypeptidase Kex1; gene KEX1 serine carboxypeptidase; KEX1 carboxypeptidase; KEX1 proteinase; KEX1DELTAp; CPDW-II; serine carboxypeptidase (misleading); Phaseolus proteinase. Enzyme Commission Number: EC 3.4.16.6. CAS No. 153967-26-1. CPDW-II. 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-4060; carboxypeptidase D; EC 3.4.16.6; 153967-26-1; cereal serine carboxypeptidase II; Saccharomyces cerevisiae KEX1 gene product; carboxypeptidase Kex1; gene KEX1 serine carboxypeptidase; KEX1 carboxypeptidase; KEX1 proteinase; KEX1DELTAp; CPDW-II; serine carboxypeptidase (misleading); Phaseolus proteinase. Cat No: EXWM-4060. | |
| initiation-specific α-1,6-mannosyltransferase | Requires Mn2+. In Saccharomyces cerevisiae, this enzyme catalyses an essential step in the outer chain elongation of N-linked oligosaccharides. Man8GlcNAc and Man9GlcNAc are equally good substrates. Group: Enzymes. Synonyms: α-1,6-mannosyltransferase; GDP-mannose:oligosaccharide 1,6-α-D-mannosyltransferase; GDP-mannose:glycolipid 1,6-α-D-mannosyltransferase; glycolipid 6-α-mannosyltransferase; GDP-mannose:oligosaccharide 1,6-α-D-mannosyltransferase. Enzyme Commission Number: EC 2.4.1.232. CAS No. 346003-17-6. 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-2462; initiation-specific α-1,6-mannosyltransferase; EC 2.4.1.232; 346003-17-6; α-1,6-mannosyltransferase; GDP-mannose:oligosaccharide 1,6-α-D-mannosyltransferase; GDP-mannose:glycolipid 1,6-α-D-mannosyltransferase; glycolipid 6-α-mannosyltransferase; GDP-mannose:oligosaccharide 1,6-α-D-mannosyltransferase. Cat No: EXWM-2462. | |
| Inorganic Pyrophosphatase from Saccharomyces cerevisiae, Recombinant | Pyrophosphatase (or inorganic pyrophosphatase) is an enzyme (EC 3.6.1.1) that catalyzes the conversion of one molecule of pyrophosphate to two phosphate ions. This is a highly exergonic reaction, and therefore can be coupled to unfavorable biochemical transformations in order to drive these transformations to completion. The functionality of this enzyme plays a critical role in lipid metabolism (including lipid synthesis and degradation), calcium absorption and bone formation, and DNA synthesis,as well as other biochemical transformations. Inorganic pyrophosphatase (ppase) catalyzes the hydrolysis of inorganic pyrophosphate to form orthophosphate. a variety ...actions that can be pulled far in the synthesis direction by the action of inorganic pyrophosphatase. Applications: Enhancing yields of rna in transcription reactions. Group: Enzymes. Synonyms: Pyrophosphate phosphohydrolase; inorganic pyrophosphatase; EC 3.6.1.1; 9024-82-2; iphosphate phosphohydrolase. CAS No. 9024-82-2. Inorganic pyrophosphatase. Mole weight: 71 kDa. Storage: at -20°C. Form: 20 mM Tris-HCl (pH 8.0), 100 mM KCl, 0.1 mM EDTA, 1 mM dithiothreitol and 50% glycerol. Source: E. coli. Species: Saccharomyces cerevisiae. Pyrophosphate phosphohydrolase; inorganic pyrophosphatase; EC 3.6.1.1; 9024-82-2; iphosphate phosphohydrolase. Cat No: NATE-1281. | |
| Invertase | An enzyme capable of hydrolyzing sucrose into glucose and fructose. Typically used in manufacturing confectionaries, dietary supplements, and other food grade applications. Applications: Dietary supplements. Group: Enzymes. Synonyms: Invertase. CAS No. 9001-57-4. Invertase. Appearance: powder or liquid. Source: Saccharomyces cerevisiae. Invertase; Invertase for confectionaries; Baking Enzymes; BAK-1729. Pack: 25kg/paper barrel (powder form), 30kg/polyster barrel (liquid form). Cat No: DIS-1024. | |
| Kex2 Protease from Saccharomyces cerevisiae, Recombinant | Kex2 is a Ca2+-dependent serine protease and cleaves at C-terminal site of Lys-Arg, Arg-Arg, Pro-Arg in pro-α-factor and killer-toxin precursors maturing, it was discovered in Saccharomyces cerevisiae. But Kex2 cant recognize and cut a single basic amino acid,such as carboxyl end peptide bond of arginine and lysine. Recombinant Kex2 is a genetically engineered protein expressed in Pichia pastoris and purified by high pressure liquid chromatography. The activity of Kex2 is not affected by the conventional serine protease inhibitors such as PMSF, TPCK, TLCK inhibition. Group: Enzymes. Synonyms: KEX2 protease; KEX2; protease; kexin; EC 3.4.21.61. Enzyme Commission Number: EC 3.4.21.61. Mole weight: 67±6.7 kD. Activity: >10 unit/mg protein. Storage: Recommended storage temperature: 2°C-8°C.Transport condition: blue ice to keep the environment cool.It should be stored in 20mM NaAc-HAc (pH 5.0-5.5) and 2mM Ca2+. It is stable after 5 cycles freezing and thawing. Form: White lyophilized. Source: Pichia pastoris. Species: Saccharomyces cerevisiae. KEX2 protease; KEX2; protease; kexin; EC 3.4.21.61. Cat No: NATE-1891. | |
| Native baker's yeast (S. cerevisiae) Proteinase A | Saccharopepsin is an enzyme. This enzyme catalyses the following chemical reaction:Hydrolysis of proteins with broad specificity for peptide bonds. Cleaves-Leu-Leu-Val-Tyr bond in a synthetic substrate. This enzyme is present in baker's yeast (Saccharomyces cerevisiae). Applications: Possibly useful for producing overlap peptides in sequence studies. Group: Enzymes. Synonyms: Endopeptidase; Proteinase A; EC 3.4.23.25; yeast endopeptidase A; Saccharomyces aspartic proteinase; aspartic proteinase yscA; proteinase yscA; yeast proteinase A; Saccharomyces cerevisiae aspartic proteinase A. Enzyme Commission Number: EC 3.4.23.25. Proteinase A. Activity: 15-50 units/mg protein. Storage: -20°C. Form: Lyophilized solids containing sodium Citrate, pH 5.0. Source: S. cerevisiae. Species: baker's yeast. Endopeptidase; Proteinase A; EC 3.4.23.25; yeast endopeptidase A; Saccharomyces aspartic proteinase; aspartic proteinase yscA; proteinase yscA; yeast proteinase A; Saccharomyces cerevisiae aspartic proteinase A. Pack: Package size based on protein content. Cat No: NATE-0636. | |
| Native Porcine Trehalase | Trehalase is a glycoside hydrolase enzyme located in on the brush border of the small intestine that catalyzes the conversion of trehalose to glucose. It is found in most animals. The non-reducing disaccharide trehalose (α-D-glucopyranosyl-1,1-α-D-glucopyranoside) is one of the most important storage carbohydRates, which is present in almost all forms of life except mammals. The disaccharide is hydrolyzed into two molecules of glucose by the enzyme trehalase. There are two types of trehalases found in Saccharomyces cerevisiae, viz. neutral trehalase (NT) and acid trehalase (AT) classified according to their pH optima. NT has an optimum pH of 7.0, while that of AT is 4...mopara viticola-infected grapevine leaves. trehalase has also been used in a study to investigate growth arrest by trehalose-6-phosphate. Group: Enzymes. Synonyms: α,α-Trehalose glucohydrolase; Trehalase; EC 3.2.1.28; 9025-52-9; α,α-trehalase. Enzyme Commission Number: EC 3.2.1.28. CAS No. 9025-52-9. Trehalase. Activity: > 1.0 units/mg protein. Storage: -20°C. Form: buffered aqueous glycerol solution; Solution in 50% glycerol containing 1% Triton(TM) X-100 and 25 mM potassium phosphate, pH 6.5. Source: Porcine kidney. Species: Porcine. α,α-Trehalose glucohydrolase; Trehalase; EC 3.2.1.28; 9025-52-9; α,α-trehalase. Cat No: NATE-0717. | |
| Native Saccharomyces cerevisiae Adenosine-5'-triphosphate Sulfurylase | In enzymology, a sulfate adenylyltransferase (EC 2.7.7.4) is an enzyme that catalyzes the chemical reaction:ATP + sulfate<-> diphosphate + adenylyl sulfate. Thus, the two substRates of this enzyme are ATP and sulfate, whereas its two products are diphosphate and adenylyl sulfate. This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). This enzyme participates in 3 metabolic pathways:purine metabolism, selenoamino acid metabolism, and sulfur metabolism. Applications: Adenosine-5?-triphosphate sulfurylase (atp sulfurylase) may be used to study sulfur metabolism and h...s. Synonyms: ATP-sulfurylase; adenosine-5'-triphosphate sulfurylase; adenosinetriphosphate sulfurylase; adenylylsulfate pyrophosphorylase; ATP sulfurylase; sulfurylase; EC 2.7.7.4; 9012-39-9; Sulfate adenylate transferase. Enzyme Commission Number: EC 2.7.7.4. CAS No. 9012-39-9. ATP-sulfurylase. Activity: > 1.0 units/mg protein. Storage: -20°C. Form: lyophilized powder. Contains Citrate buffer salts. Source: Saccharomyces cerevisiae. ATP-sulfurylase; adenosine-5'-triphosphate sulfurylase; adenosinetriphosphate sulfurylase; adenylylsulfate pyrophosphorylase; ATP sulfurylase; sulfurylase; EC 2.7.7.4; 9012-39-9; Sulfate adenylate transferase. Cat No: NATE-0090. | |
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