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| Product | Description | |
|---|---|---|
| Native Baker's yeast (S. cerevisiae) S-Acetyl-coenzyme A synthetase | Acetyl-coenzyme A synthetase catalyzes the production of acetyl-CoA. It is involved in histone acetylation in the nucleus. It may be involved in the growth of nonfermentable carbon sources such as glycerol. Acetyl-coenzyme A synthetase is induced by acetate, acetaldehyde and ethanol. Applications: S-acetyl-coenzyme a synthetase may be used to study various metabolic pathways, such as glycolysis, gluconeogenesis, pyruvate metabolism and co fixation. it may also be used in gene expression studies. Group: Enzymes. Synonyms: acetyl-CoA synthetase; acetyl activating enzyme; acetate thiokinase; acyl-activating enzyme; acetyl coenzyme A synthetase; acetic thiokinase; acetyl CoA ligase; acetyl C. Enzyme Commission Number: EC 6.2.1.1. CAS No. 9012-31-1. ACS. Activity: > 3 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing stabilizers as potassium phosphate, sucrose, and reduced glutathione. Source: Baker's yeast (S. cerevisiae). acetyl-CoA synthetase; acetyl activating enzyme; acetate thiokinase; acyl-activating enzyme; acetyl coenzyme A synthetase; acetic thiokinase; acetyl CoA ligase; acetyl CoA synthase; acetyl-coenzyme A synthase; short chain fatty acyl-CoA synthetase; short-chain acyl-coenzyme A synthetase; ACS; EC 6.2.1.1; 9012-31-1. Pack: Package size based on protein content. Cat No: NATE-0026. |  |
| Native Yeast Coenzyme A, Trilithium Salt | Coenzyme A (CoA, CoASH, or HSCoA) is a coenzyme, notable for its role in the synthesis and oxidation of fatty acids, and the oxidation of pyruvate in the citric acid cycle. All genomes sequenced to date encode enzymes that use coenzyme A as a substrate, and around 4% of cellular enzymes use it (or a thioester, such as acetyl-CoA) as a substrate. In humans, CoA biosynthesis requires cysteine, pantothenate, and adenosine triphosphate (ATP). Group: Coenzymes. Synonyms: Coenzyme A, Trilithium Salt; CoA-Li; 18439-24-2. CAS No. 18439-24-2. Purity: Determined by enzyme analysis with PTA* (> 75%) *PTA = Phosphotrasacetylase (LM) (EC 2.3.1.8.). CoA. Mole weight: 685.41. Storage: Keep tightly stoppered in the dark below 5°C. For Prolonged storage, keep below-20°C. Source: Yeast. Coenzyme A, Trilithium Salt; CoA-Li; 18439-24-2. Cat No: NATE-0146. | |
| 10-[3-(2,2-Diimethyl-1,3-dioxolan-4-yl)-2,3-dihydroxypropyl]-7,8-dimethyl-isoalloxazine | 10-[3-(2,2-Diimethyl-1,3-dioxolan-4-yl)-2,3-dihydroxypropyl]-7,8-dimethyl-isoalloxazine is an intermediate uin the synthesis of Riboflavin 4',5'-Diphosphate which is a diphosphate derivative of Riboflavin (R414995); a nutritional factor found in milk, eggs, malted barley, liver, kidney, heart, and leafy vegetables. Richest natural source is yeast. Minute amounts present in all plant and animal cells. Vitamin (enzyme cofactor). Group: Biochemicals. Grades: Highly Purified. CAS No. 22854-81-5. Pack Sizes: 2.5mg, 5mg. Molecular Formula: C20H24N4O6. US Biological Life Sciences. |  Worldwide |
| 10- ( ( (4R, 5R, 6S) -6- ( ( (tert-Butyldiphenylsilyl) oxy) methyl) -5-hydroxy-2, 2-dimethyl-1, 3-dioxan-4-yl) methyl) -7, 8-dimethylbenzo [g]pteridine-2, 4 (3H, 10H) -dione | 10- ( ( (4R, 5R, 6S) -6- ( ( (Tert-butyldiphenylsilyl) oxy) methyl) -5-hydroxy-2, 2-dimethyl-1, 3-dioxan-4-yl) methyl) -7, 8-dimethylbenzo [g]pteridine-2, 4 (3H, 10H) -dioneis an intermediate uin the synthesis of Riboflavin 4',5'-Diphosphate which is a diphosphate derivative of Riboflavin (R414995); a nutritional factor found in milk, eggs, malted barley, liver, kidney, heart, and leafy vegetables. Richest natural source is yeast. Minute amounts present in all plant and animal cells. Vitamin (enzyme cofactor). Group: Biochemicals. Grades: Highly Purified. Pack Sizes: 5mg, 10mg. Molecular Formula: C36H42N4O6Si, Molecular Weight: 654.83. US Biological Life Sciences. | Worldwide |
| 1,6-α-D-mannosidase | The enzyme is specific for (1?6)-linked mannobiose and has no activity towards any other linkages, or towards p-nitrophenyl-α-D-mannopyranoside or baker's yeast mannan. It is strongly inhibited by Mn2+ but does not require Ca2+ or any other metal cofactor for activity. Group: Enzymes. Enzyme Commission Number: EC 3.2.1.163. 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-3845; 1,6-α-D-mannosidase; EC 3.2.1.163. Cat No: EXWM-3845. | |
| 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. | |
| 1-Deoxy-1-[ (3-hydroxymethyl-4-methyl-6- (2-phenyldiazenyl) phenyl) amino]-D-ribitol | 1-Deoxy-1-[ (3-hydroxymethyl-4-methyl-6- (2-phenyldiazenyl) phenyl) amino]-D-ribitol is an intermediate in the synthesis of 8-Hydroxymethyl Riboflavin which is an impurity of Riboflavin (R414995), a nutritional factor found in milk, eggs, malted barley, liver, kidney, heart, leafy vegetables. Richest natural source is yeast. Minute amounts present in all plant and animal cells. Vitamin (enzyme cofactor). Group: Biochemicals. Grades: Highly Purified. Pack Sizes: 5mg, 10mg. Molecular Formula: C19H25N3O5. US Biological Life Sciences. | Worldwide |
| 1-Deoxy-1-[(3-hydroxymethyl-4-methylphenyl)amino]-D-ribitol | 1-Deoxy-1-[(3-hydroxymethyl-4-methylphenyl)amino]-D-ribitol is an intermediate in the synthesis of 8-Hydroxymethyl Riboflavin which is an impurity of Riboflavin (R414995), a nutritional factor found in milk, eggs, malted barley, liver, kidney, heart, leafy vegetables. Richest natural source is yeast. Minute amounts present in all plant and animal cells. Vitamin (enzyme cofactor). Group: Biochemicals. Grades: Highly Purified. Pack Sizes: 10mg, 25mg. Molecular Formula: C13H21NO5. US Biological Life Sciences. | Worldwide |
| 2-(3-amino-3-carboxypropyl)histidine synthase | A [4Fe-4S] enzyme that modifies a histidine residue of the translation elongation factor 2 (EF2) via a 3-amino-3-carboxypropyl radical. The enzyme is present in archae and eukaryotes but not in eubacteria. The relevant histidine of EF2 is His715 in mammals, His699 in yeast and His600 in Pyrococcus horikoshii. Part of diphthamide biosynthesis. Group: Enzymes. Synonyms: Dph2. Enzyme Commission Number: EC 2.5.1.108. 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-2724; 2-(3-amino-3-carboxypropyl)histidine synthase; EC 2.5.1.108; Dph2. Cat No: EXWM-2724. | |
| 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. | |
| 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-dehydropantolactone reductase (Re-specific) | The yeast enzyme differs from that from Escherichia coli [EC 1.1.1.214 2-dehydropantolactone reductase (Si-specific)], which is specific for the Si-face of NADP+, and in receptor requirements from EC 1.1.99.26 3-hydroxycyclohexanone dehydrogenase. Group: Enzymes. Synonyms: 2-oxopantoyl lactone reductase; ketopantoyl lactone reductase; 2-ketopantoyl lactone reductase; 2-dehydropantoyl-lactone reductase (A-specific); (R)-pantolactone:NADP+ oxidoreductase (A-specific); 2-dehydropantolactone reductase (A-specific). Enzyme Commission Number: EC 1.1.1.168. CAS No. 37211-75-9. 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-0071; 2-dehydropantolactone reductase (Re-specific); EC 1.1.1.168; 37211-75-9; 2-oxopantoyl lactone reductase; ketopantoyl lactone reductase; 2-ketopantoyl lactone reductase; 2-dehydropantoyl-lactone reductase (A-specific); (R)-pantolactone:NADP+ oxidoreductase (A-specific); 2-dehydropantolactone reductase (A-specific). Cat No: EXWM-0071. | |
| 2-dehydropantolactone reductase (Si-specific) | The Escherichia coli enzyme differs from that from yeast [EC 1.1.1.168 2-dehydropantolactone reductase (Re-specific)], which is specific for the Re-face of NADP+, and in receptor requirements from EC 1.1.99.26 3-hydroxycyclohexanone dehydrogenase. Group: Enzymes. Synonyms: 2-oxopantoyl lactone reductase; 2-ketopantoyl lactone reductase; ketopantoyl lactone reductase; 2-dehydropantoyl-lactone reductase (B-specific); (R)-pantolactone:NADP+ oxidoreductase (B-specific); 2-dehydropantolactone reductase (B-specific). Enzyme Commission Number: EC 1.1.1.214. CAS No. 37211-75-9. 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-0119; 2-dehydropantolactone reductase (Si-specific); EC 1.1.1.214; 37211-75-9; 2-oxopantoyl lactone reductase; 2-ketopantoyl lactone reductase; ketopantoyl lactone reductase; 2-dehydropantoyl-lactone reductase (B-specific); (R)-pantolactone:NADP+ oxidoreductase (B-specific); 2-dehydropantolactone reductase (B-specific). Cat No: EXWM-0119. | |
| 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. | |
| 3-Acetylpyridine-Adenine Dinucleotide, Oxidized (APAD) | 3-Acetylpyridine adenine dinucleotide is an NAD analog with higher oxidation potential than NAD. It can substitute for NAD as a hydrogen-accepting cofactor in many dehydrogenase reactions. For example lactate dehydrogenase from Toxoplasma, Clonorchis, and Plasmodium, bacterial lipoamide dehydrogenase, as well as mammalian dehydrogenases. This compound can also act as a proton acceptor in various transhydrogenation reactions with NADH or NADPH. Group: Coenzymes. Synonyms: aldehyde reductase; ADH; alcohol dehydrogenase (NAD); aliphatic alcohol dehydrogenase; ethanol dehydrogenase; NAD-dependent alcohol dehydrogenase; NA. Enzyme Commission Number: EC 1.1.1.1. CAS No. 1986-8-8. Purity: Determined by increase in absorbance at 363 nm on enzymatic reduction with ADH* at pH 10.0 > 92% *ADH = Alcohol dehydrogenase (Horse liver) (EC 1.1.1.1.). APAD. Mole weight: 662.44. Storage: Keep tightly stoppered in the dark below 5°C. Moisture will reduce the purity. For prolonged storage, keep below-20°C. 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; APAD. Cat No: NATE-0077. | |
| 3-Acetylpyridine-Adenine Dinucleotide, Reduced (APADH) | Molecular Formula: C22H28N6O14P2. Group: Coenzymes. Synonyms: 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; APADH. Enzyme Commission Number: EC 1.1.1.1. CAS No. 102029-93-6. Purity: Determined by decrease in absorbance at 363 nm on enzymatic oxidation with ADH* at pH 7.5 (> 92%) *ADH = Alcohol dehydrogenase (horse liver) (EC 1.1.1.1.). APADH. Mole weight: 708.42. Storage: Keep tightly stoppered in the dark below-20°C. Moisture will reduce the purity. For Prolonged storage, keep below-80°C. 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; APADH. Cat No: NATE-0078. | |
| 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. | |
| 4-α-glucanotransferase | This entry covers the former separate entry for EC 2.4.1.3 (amylomaltase). The plant enzyme has been termed D-enzyme. An enzymic activity of this nature forms part of the mammalian and yeast glycogen debranching system (see EC 3.2.1.33 amylo-α-1,6-glucosidase). Group: Enzymes. Synonyms: disproportionating enzyme; dextrin glycosyltransferase; D-enzyme; debranching enzyme maltodextrin glycosyltransferase; amylomaltase; dextrin transglycosylase; 1,4-α-D-glucan:1,4-α-D-glucan 4-α-D-glycosyltransferase. Enzyme Commission Number: EC 2.4.1.25. CAS No. 9032-9-1. Amylomaltase. 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-2479; 4-α-glucanotransferase; EC 2.4.1.25; 9032-09-1; disproportionating enzyme; dextrin glycosyltransferase; D-enzyme; debranching enzyme maltodextrin glycosyltransferase; amylomaltase; dextrin transglycosylase; 1,4-α-D-glucan:1,4-α-D-glucan 4-α-D-glycosyltransferase. Cat No: EXWM-2479. | |
| 4-hydroxysphinganine ceramide fatty acyl 2-hydroxylase | The enzyme, characterized from yeast and mammals, catalyses the hydroxylation of carbon 2 of long- or very-long-chain fatty acids attached to (4R)-4-hydroxysphinganine during de novo ceramide synthesis. The enzymes from yeast and from mammals contain an N-terminal cytochrome b5 domain that acts as the direct electron donor to the desaturase active site. The newly introduced 2-hydroxyl group has R-configuration. cf. EC 1.14.18.7, dihydroceramide fatty acyl 2-hydroxylase. Group: Enzymes. Synonyms: FA2H (gene name); SCS7 (gene name). Enzyme Commission Number: EC 1.14.18.6. 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-0968; 4-hydroxysphinganine ceramide fatty acyl 2-hydroxylase; EC 1.14.18.6; FA2H (gene name); SCS7 (gene name). Cat No: EXWM-0968. | |
| 5-Bromo-5-nitro-1,3-dioxane | 5-Bromo-5-nitro-1,3-dioxane, an antimicrobial compound, is effective against Gram-positive and Gram-negative bacteria and fungi, including yeast. 5-Bromo-5-nitro-1,3-dioxane inhibits enzyme activity and subsequent inhibition of microbial growth by the oxidation of essential protein thiol [1]. Uses: Scientific research. Group: Signaling pathways. CAS No. 30007-47-7. Pack Sizes: 10 mM * 1 mL; 50 mg; 100 mg. Product ID: HY-W014316. |  |
| 5-Bromo-5-nitro-1,3-dioxane | 5-bromo-5-nitro-1,3-Dioxane is an antimicrobial compound that is effective against Gram-positive and Gram-negative bacteria and fungi, including yeast.1 Its mode of action occurs via the oxidation of essential protein thiols causing inhibition of enzyme activity and subsequent inhibition of microbial growth.1 This compound has been used as a preservative for biological molecules and solutions such as antibodies and antisera. Group: Biochemicals. Grades: Highly Purified. CAS No. 30007-47-7. Pack Sizes: 50g, 100g, 250g, 500g, 1Kg. Molecular Formula: C?H?BrNO?, Molecular Weight: 212. US Biological Life Sciences. | Worldwide |
| 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 |
| 6-Chloro-5-(2,3-dichlorophenoxy)-2-methylthio-benzimidazole (Triclabendazole) | Triclabendazole is a member of the benzimidazole family of anthelmintics. It is effective against F. hepatica helminths that cause fascioliasis, reducing secreted protease enzyme activities that are critical for the invasion, migration, nutrition, and survival of the parasite.1 In yeast and mammalian cells, triclabendazole was shown to inhibit adenylyl cyclase in the Ras-adenylyl cyclase-protein kinase A nutrient-sensing pathway and to prevent apoptosis induced by the Parkinsons disease-related protein α-synuclein, demonstrating a protective role during various cellular stresses.2,3. Group: Biochemicals. Alternative Names: 5-Chloro-6- (2, 3-dichlorophenoxy) -2- methyl thiobenzimidazole; CGA-89317, egaten; Fasinex; Triclabendazole. Grades: Highly Purified. CAS No. 68786-66-3. Pack Sizes: 25g, 50g, 100g. Molecular Formula: C14H9Cl3N2OS, Molecular Weight: 359.66. US Biological Life Sciences. | Worldwide |
| adenylyl-sulfate kinase | The human phosphoadenosine-phosphosulfate synthase (PAPSS) system is a bifunctional enzyme (fusion product of two catalytic activities). In a first step, sulfate adenylyltransferase catalyses the formation of adenosine 5'-phosphosulfate (APS) from ATP and inorganic sulfate. The second step is catalysed by the adenylylsulfate kinase portion of 3'-phosphoadenosine 5'-phosphosulfate (PAPS) synthase, which involves the formation of PAPS from enzyme-bound APS and ATP. In contrast, in bacteria, yeast, fungi and plants, the formation of PAPS is carried out by two individual polypeptides, sulfate adenylyltransferase (EC 2.7.7.4) and adenylyl-sulfate kinase (EC 2.7.1.25). Group: Enzymes. Synonyms: adenylylsulfate kinase (phosphorylating); 5'-phosphoadenosine sulfate kinase; adenosine 5'-phosphosulfate kinase; adenosine phosphosulfate kinase; adenosine phosphosulfokinase; . Enzyme Commission Number: EC 2.7.1.25. CAS No. 9012-38-8. 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-3055; adenylyl-sulfate kinase; EC 2.7.1.25; 9012-38-8; adenylylsulfate kinase (phosphorylating); 5'-phosphoadenosine sulfate kinase; adenosine 5'-phosphosulfate kinase; adenosine phosphosulfate kinase; adenosine phosphosulfokinase; adenosine-5'-phosphosulfate-3'-phosphokinase; APS kinase. Cat No: EXWM-3055. | |
| alcohol dehydrogenase | A zinc protein. Acts on primary or secondary alcohols or hemi-acetals with very broad specificity; however the enzyme oxidizes methanol much more poorly than ethanol. The animal, but not the yeast, enzyme acts also on cyclic secondary alcohols. Group: Enzymes. Synonyms: 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. Enzyme Commission Number: EC 1.1.1.1. CAS No. 9031-72-5. Alcohol 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-0001; alcohol dehydrogenase; EC 1.1.1.1; 9031-72-5; 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. Cat No: EXWM-0001. | |
| Alcohol dehydrogenase from E. coli, Recombinant | 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: High purity recombinant alcohol dehyd...l dehydrogenase; yeast alcohol dehydrogenase; EC 1.1.1.1. Enzyme Commission Number: EC 1.1.1.1. CAS No. 9031-72-5. Alcohol dehydrogenase. Mole weight: ~ 38,642 Da. Activity: 6.7 U/mg protein at pH 8.5 and 25°C. Storage: Store at 4°C. Do not store the enzyme in presence of sodium azide. Form: In 3.2 M ammonium sulphate. Source: E. coli. 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-0803. | |
| Alcohol dehydrogenase from Equine, Recombinant | 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+. Group: Enzymes. Synonyms: aldehyde reductase; ADH; alcohol dehydrogenase (NAD); aliphatic alcohol dehydrogenase; ethanol dehydrogenase; NAD-dependent alcohol dehydrogenase; NAD-specific aromatic alcohol dehydrogenase; NADH-alcoh. Enzyme Commission Number: EC 1.1.1.1. CAS No. 9031-72-5. Alcohol dehydrogenase. Activity: >0.5 U/mg. Storage: Store at -20°C. Source: E. coli. Species: Equine. 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-1584. | |
| Alcohol dehydrogenase from Human, Recombinant | 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+. Group: Enzymes. Synonyms: 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 alcoh. Enzyme Commission Number: EC 1.1.1.2. Alcohol dehydrogenase. Mole weight: 36573.0 Da. Source: Human. 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 1.1.1.2. Cat No: NATE-1197. | |
| Alcohol oxidase | Alcohol oxidase is a functional enzyme of methanol utilization pathway and can be isolated from yeast peroxisome [1]. Uses: Scientific research. Group: Signaling pathways. Alternative Names: AO; AOX. CAS No. 9073-63-6. Pack Sizes: 50 U; 250 U. Product ID: HY-P2756. | |
| allophanate hydrolase | Along with EC 3.5.2.15 (cyanuric acid amidohydrolase) and EC 3.5.1.84 (biuret amidohydrolase), this enzyme forms part of thecyanuric-acid metabolism pathway, which degrades s-triazide herbicides, such as atrazine [2-chloro-4-(ethylamino)-6-(isopropylamino)-1,3,5-triazine], in bacteria. The yeast enzyme (but not that from green algae) also catalyses the reaction of EC 6.3.4.6, urea carboxylase, thus bringing about the hydrolysis of urea to CO2 and NH3 in the presence of ATP and bicarbonate. The enzyme from Pseudomonas sp. strain ADP has a narrow substrate specificity, being unable to use the structurally analogous compounds urea, hydroxyurea or methylcarbamate as substrate. Group: Enzymes. Synonyms: allophanate lyase; AtzF; TrzF. Enzyme Commission Number: EC 3.5.1.54. CAS No. 9076-72-6. 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-4443; allophanate hydrolase; EC 3.5.1.54; 9076-72-6; allophanate lyase; AtzF; TrzF. Cat No: EXWM-4443. | |
| α-factor-transporting ATPase | ABC-type (ATP-binding cassette-type) ATPase, characterized by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. A yeast enzyme that exports the α-factor sex pheromone. Group: Enzymes. Enzyme Commission Number: EC 7.4.2.7 (Formerly EC 3.6.3.48). 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-4686; α-factor-transporting ATPase; EC 3.6.3.48. Cat No: EXWM-4686. | |
| α-Glucosidase | α-Glucosidase. Synonyms: alpha-Glucosidase (from Yeast) 100kU pack;a-Glucosidase (EC 3.2.1.20);β-D-Glucoside glycohydrolase (EC 3.2.1.21);MALTASE;MALTASE TYPE I;MALTASE TYPE V;A-glucosidase from bacillus*stearothermophilus ly;A-glucosidase type I from bakers yeast. CAS No. 9001-42-7. Pack Sizes: 1 kg. Product ID: CDF4-0060. Molecular formula: NULL. Category: Enzyme Preparations. Product Keywords: Food Ingredients; Enzyme Preparations; α-Glucosidase; CDF4-0060; 9001-42-7; NULL; 232-604-7; 9001-42-7. Purity: 0.99. Color: off-White. EC Number: 232-604-7. Physical State: Powder. Storage: 2-8°C. Application: For the determination of α-amylase and the synthesis of various 1'-O-sucrose and 1-O-fructose esters. Melting Point: 154.3-155.3 °C. Product Description: This product has been enhanced for energy efficiency and waste prevention when used in starch hydrolysis research. |  |
| α-Glucosidase, Yeast | α-Glucosidase, Yeast (α-D-Glucosidase, Yeast), a carbohydrate hydrolyzing enzyme, catalyzes the liberation of α-glucose from the non-reducing end of the substrate. α-Glucosidase can facilitate the absorption of glucose by the small intestine. Inhibition of α-Glucosidase is an effective management of non-insulin-dependent diabetes mellitus (NIDDM) [1] [2]. Uses: Scientific research. Group: Signaling pathways. Alternative Names: α-D-Glucosidase, Yeast. CAS No. 9001-42-7. Pack Sizes: 100 U; 500 U. Product ID: HY-P2802. | |
| α-L-rhamnosidase | The enzyme, found in animal tissues, plants, yeasts, fungi and bacteria, utilizes an inverting mechanism of hydrolysis, releasing β-L-rhamnose. Substrates include naringin, rutin, quercitrin, hesperidin, dioscin, terpenyl glycosides and many other natural glycosides containing terminal α-L-rhamnose. Group: Enzymes. Synonyms: α-L-rhamnosidase T; α-L-rhamnosidase N. Enzyme Commission Number: EC 3.2.1.40. CAS No. 37288-35-0. RhamA. 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-3903; α-L-rhamnosidase; EC 3.2.1.40; 37288-35-0; α-L-rhamnosidase T; α-L-rhamnosidase N. Cat No: EXWM-3903. | |
| 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. | |
| amylo-α-1,6-glucosidase | This enzyme hydrolyses an unsubstituted glucose unit linked by an α(1?6) bond to an α(1?4) glucose chain. The enzyme activity found in mammals and yeast is in a polypeptide chain containing two active centres. The other activity is similar to that of EC 2.4.1.25 (4-α-glucanotransferase), which acts on the glycogen phosphorylase limit dextrin chains to expose the single glucose residues, which the 6-α-glucosidase activity can then hydrolyse. Together, these two activities constitute the glycogen debranching system. Group: Enzymes. Synonyms: amylo-1,6-glucosidase; dextrin 6-α-D-glucosidase; amylopectin 1,6-glucosidase; dextrin-1,6-glucosidase; glycogen phosphorylase-limit dextrin α-1,6-glucohydrolase. Enzyme Commission Number: EC 3.2.1.33. CAS No. 9012-47-9. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-3896; amylo-α-1,6-glucosidase; EC 3.2.1.33; 9012-47-9; amylo-1,6-glucosidase; dextrin 6-α-D-glucosidase; amylopectin 1,6-glucosidase; dextrin-1,6-glucosidase; glycogen phosphorylase-limit dextrin α-1,6-glucohydrolase. Cat No: EXWM-3896. | |
| anthranilate 3-monooxygenase (deaminating) | The enzyme from Aspergillus niger is an iron protein; that from the yeast Trichosporon cutaneum is a flavoprotein (FAD). Group: Enzymes. Synonyms: anthranilate hydroxylase; anthranilate 2,3-dioxygenase (deaminating); anthranilate hydroxylase (deaminating); anthranilic hydroxylase; anthranilate 2,3-hydroxylase (deaminating). Enzyme Commission Number: EC 1.14.13.35. CAS No. 37256-68-1. 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-0842; anthranilate 3-monooxygenase (deaminating); EC 1.14.13.35; 37256-68-1; anthranilate hydroxylase; anthranilate 2,3-dioxygenase (deaminating); anthranilate hydroxylase (deaminating); anthranilic hydroxylase; anthranilate 2,3-hydroxylase (deaminating). Cat No: EXWM-0842. | |
| assimilatory sulfite reductase (NADPH) | Contains siroheme, [4Fe-4S] cluster, FAD and FMN. The enzyme, which catalyses the six-electron reduction of sulfite to sulfide, is involved in sulfate assimilation in bacteria and yeast. Different from EC 1.8.99.5, dissimilatory sulfite reductase, which is involved in prokaryotic sulfur-based energy metabolism. cf. EC 1.8.7.1, assimilatory sulfite reductase (ferredoxin). Group: Enzymes. Synonyms: sulfite reductase (NADPH); sulfite (reduced nicotinamide adenine dinucleotide phosphate) reductase; NADPH-sulfite reductase; NADPH-dependent sulfite reductase; H2S-NADP oxidoreductase; sulfite reductase (NADPH2); MET5 (gene name); MET10 (gene name); cysI (gene name); cysJ (gene name). Enzyme Commission Number: EC 1.8.1.2. CAS No. 9029-35-0. 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-1646; assimilatory sulfite reductase (NADPH); EC 1.8.1.2; 9029-35-0; sulfite reductase (NADPH); sulfite (reduced nicotinamide adenine dinucleotide phosphate) reductase; NADPH-sulfite reductase; NADPH-dependent sulfite reductase; H2S-NADP oxidoreductase; sulfite reductase (NADPH2); MET5 (gene name); MET10 (gene name); cysI (gene name); cysJ (gene name). Cat No: EXWM-1646. | |
| ATP Sulfurylase from S. cerevisiae, Recombinant | In enzymology, a sulfate adenylyltransferase (EC 2.7.7.4) is an enzyme that catalyzes the chemical reaction:ATP + sulfate<-> diphosphate + adenylyl sulfate. Thus, the two substRates of this enzyme are ATP and sulfate, whereas its two products are diphosphate and adenylyl sulfate. This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). This enzyme participates in 3 metabolic pathways:purine metabolism, selenoamino acid metabolism, and sulfur metabolism. Adenosine 5-triphosphate sulfurylase yeast recombinant produced in e. coli is a non-glycosylated, polypeptide chain containin...formed from aps and ppi. adenosine 5-triphosphate sulfurylase is purified by proprietary chromatographic techniques. Group: Enzymes. Synonyms: ATP-sulfurylase; adenosine-5'-triphosphate sulfurylase; adenosinetriphosphate sulfurylase; adenylylsulfate pyrophosphorylase; ATP sulfurylase; sulfurylase; EC 2.7.7.4; 9012-39-9; Sulfate adenylate transferase. CAS No. 9012-39-9. ATP-sulfurylase. Storage: at -20°C. Source: E. coli. Species: S. cerevisiae. ATP-sulfurylase; adenosine-5'-triphosphate sulfurylase; adenosinetriphosphate sulfurylase; adenylylsulfate pyrophosphorylase; ATP sulfurylase; sulfurylase; EC 2.7.7.4; 9012-39-9; Sulfate adenylate transferase. Cat No: NATE-1280. | |
| 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. | |
| β-Nicotinamide-Adenine Dinucleotide Phosphate, Oxidized Form (β-NADP-K) | β-Nicotinamide adenine dinucleotide 2?-phosphate (NADP+) and β-Nicotinamide adenine dinucleotide 2?-phosphate, reduced (NADPH) comprise a coenzyme redox pair (NADP+:NADPH) involved in a wide range of enzyme catalyzed oxidation reduction reactions. The NADP+/NADPH redox pair facilitates electron transfer in anabolic reactions such as lipid and cholesterol biosynthesis and fatty acyl chain elongation. The NADP+/NADPH redox pair is used in a variety of antioxidation mechanism where it protects agains reactive oxidation species accumulation. NADPH is generated in vivio by the pentose phosphate pathway (PPP). Group: Coenzymes. Synonyms: β-Nicotinamide-Adenine Dinucleotide Phosphate, Oxidized Form (β-NADP-K); β-Nicotinamide-Adenine Dinucleotide Phosphate;. CAS No. 698999-85-8. Purity: Determined by increase in absorbance at 340nm on enzymatic reduction with G6PDH* at pH 10 (More than 95%) *G6PDH = Glucose-6-phosphate dehydrogenase (yeast) (EC 1.1.1.49.). β-NADP-K. Mole weight: 781.5. Storage: Keep tightly stoppered in the dark below 5°C. Moisture will reduce the purity. For prolonged storage, keep below-20°C. β-Nicotinamide-Adenine Dinucleotide Phosphate, Oxidized Form (β-NADP-K); β-Nicotinamide-Adenine Dinucleotide Phosphate; β-NADP-K. Cat No: NATE-0788. | |
| β-Nicotinamide-Adenine Dinucleotide Phosphate, Reduced | β-Nicotinamide adenine dinucleotide 2?-phosphate (NADP+) and β-Nicotinamide adenine dinucleotide 2?-phosphate, reduced (NADPH) comprise a coenzyme redox pair (NADP+:NADPH) involved in a wide range of enzyme catalyzed oxidation reduction reactions. The NADP+/NADPH redox pair facilitates electron transfer in anabolic reactions such as lipid and cholesterol biosynthesis and fatty acyl chain elongation. Group: Coenzymes. Synonyms: β-Nicotinamide-Adenine Dinucleotide Phosphate, Reduced; 2646-71-16; β-NADPH. CAS No. 2646-71-16. Purity: Determined by decrease in absorbance at 340 nm on enzymatic reduction with GR*at pH 10.0 (> 95%) *GR = Glutathion reductase (yeast) (EC 1.6.4.2.). β-NADPH. Mole weight: 833.35. Storage: Keep tightly stoppered in the dark below 5°C. Moisture will reduce the purity. For prolonged storage, keep below-20°C. Unstable in acids, but relatively stable at pH 10-11. β-Nicotinamide-Adenine Dinucleotide Phosphate, Reduced; 2646-71-16; β-NADPH. Cat No: NATE-0787. | |
| β-Nicotinamide-Adenine Dinucleotide, Reduced Form (β-NADH) | NADH is a coenzyme that functions as a regenerating electron donor in catabolic processes including glycolysis, beta-oxidation and the citric acid cycle (Krebs cycle, TCA cycle). It participates in cell signaling events as well, for example as a substrate for the poly (ADP-ribose) polymerases (PARPs) during the DNA damage response. The NAD+/NADH dependent sirtuins play key roles in stress responses during events involving energy metabolism, with implications in cancer biology, diabetes and neurodegenerative disease. Group: Coenzymes. Synonyms. Enzyme Commission Number: EC 1.1.1.1. CAS No. 606-68-8. Purity: Dertermined by decrease in absorbance at 340 nm on enzymatic oxidation with ADH* at pH 10.0 > 95% *ADH = Alcohol dehydrogenase (yeast) (EC 1.1.1.1.). β-NADH. Mole weight: 709.41. Storage: Keep tightly stoppered in the dark below 5°C. Moisture will reduce the purity. For prolonged storage, keep below-20°C. Unstable in acids, but relatively stable at pH 10-11. 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; β-NADH. Cat No: NATE-0786. | |
| Bifunctional Chimeras of Glutamylcysteine Synthetase and Glutathione Synthetase (Crude Enzyme) | GSH, and by extension GCL, is critical to cell survival. Nearly every eukaryotic cell, from plants to yeast to humans, expresses a form of the GCL protein for the purpose of synthesizing GSH. To further highlight the critical nature of this enzyme, genetic knockdown of GCL results in embryonic lethality. Furthermore, dysregulation of GCL enzymatic function and activity is known to be involved in the vast majority of human diseases, such as diabetes, Parkinson's disease, Alzheimers disease, COPD, HIV/AIDS, and cancer. This typically involves impaired function leading to decreased GSH biosynthesis, reduced cellular antioxidant capacity, and the in...se 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: Agriculture; medicine; synthesis; biotechnology; pharmacology. Group: Enzymes. Enzyme Commission Number: EC 6.3.2.2/ 6.3.2.3. CAS No. 9023-64-7/9023-62-5. Activity: Undetermined. Appearance: Clear to translucent yellow solution. Storage: at -20 °C or lower, for at least 1 month. Source: E. coli. Bifunctional Chimeras of Glutamylcysteine Synthetase and Glutathione Synthetase; Glutamylcysteine Synthetase; Glutathione Synthetase. Pack: 100ml. Cat No: NATE-1859. | |
| Ca2+-transporting ATPase | A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. This enzyme family comprises three types of Ca2+-transporting enzymes that are found in the plasma membrane, the sarcoplasmic reticulum and in yeast. The first and third transport one ion per ATP hydrolysed, whereas the second transports two ions. Ca2+ is transported from the cytosol [side 1] into the sarcoplasmic reticulum in muscle cells [side 2]. Group: Enzymes. Synonyms: sarcoplasmic reticulum ATPase; sarco(endo)plasmic reticulum Ca2+-ATPase; calcium pump; Ca2+-pumping ATPase; plasma membrane Ca-ATPase. Enzyme Commission Number: EC 3.6.3.8. 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-4697; Ca2+-transporting ATPase; EC 3.6.3.8; sarcoplasmic reticulum ATPase; sarco(endo)plasmic reticulum Ca2+-ATPase; calcium pump; Ca2+-pumping ATPase; plasma membrane Ca-ATPase. Cat No: EXWM-4697. | |
| cadmium-transporting ATPase | ABC-type (ATP-binding cassette-type) ATPase, characterized by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. A yeast enzyme that exports some heavy metals, especially Cd2+, from the cytosol into the vacuole. Group: Enzymes. Enzyme Commission Number: EC 7.2.2.2 (Formerly EC 3.6.3.46). 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-4684; cadmium-transporting ATPase; EC 3.6.3.46. Cat No: EXWM-4684. | |
| candidapepsin | This endopeptidase from the imperfect yeast Candida albicans is inhibited by pepstatin, but not by methyl 2-diazoacetamidohexanoate or 1,2-epoxy-3-(p-nitrophenoxy)propane. In peptidase family A1 (pepsin A family). Formerly included in EC 3.4.23.6. Group: Enzymes. Synonyms: Candida albicans aspartic proteinase; Candida albicans carboxyl proteinase; Candida albicans secretory acid proteinase; Candida olea acid proteinase; Candida aspartic proteinase; Candida olea aspartic proteinase; Candida albicans aspartic proteinase. Enzyme Commission Number: EC 3.4.23.24. CAS No. 69458-91-9. 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-4262; candidapepsin; EC 3.4.23.24; 69458-91-9; Candida albicans aspartic proteinase; Candida albicans carboxyl proteinase; Candida albicans secretory acid proteinase; Candida olea acid proteinase; Candida aspartic proteinase; Candida olea aspartic proteinase; Candida albicans aspartic proteinase. Cat No: EXWM-4262. | |
| 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. | |
| cystathionine β-lyase | A pyridoxal-phosphate protein. The enzyme cleaves a carbon-sulfur bond, releasing L-homocysteine and an unstable enamine product that tautomerizes to an imine form, which undergoes a hydrolytic deamination to form pyruvate and ammonia. The latter reaction, which can occur spontaneously, can also be catalysed by EC 3.5.99.10, 2-iminobutanoate/2-iminopropanoate deaminase. The enzyme from some sources also acts on L-cystine, forming pyruvate, ammonia and cysteine persulfide, and a number of related compounds. Possibly identical, in yeast, with EC 4.4.1.6 S-alkylcysteine lyase. Group: Enzymes. Synonyms: β-cystathionase; cystine lyase; cystathionine L-homocysteine-lyase (deaminating); L-cystathionine L-homocysteine-lyase (deaminating); CBL. Enzyme Commission Number: EC 4.4.1.8. CAS No. 9055-5-4. Cystathionine β-lyase. 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-5341; cystathionine β-lyase; EC 4.4.1.8; 9055-05-4; β-cystathionase; cystine lyase; cystathionine L-homocysteine-lyase (deaminating); L-cystathionine L-homocysteine-lyase (deaminating); CBL. Cat No: EXWM-5341. | |
| D-(-)-3-Phosphoglyceric acid disodium | D-(-)-3-Phosphoglyceric acid (3-Phospho-D-glyceric acid) disodium is an important intermediate in the enzyme-catalyzed glycolysis process. D-(-)-3-Phosphoglyceric acid disodium competitively inhibits yeast enolase ( enolase ). D-(-)-3-Phosphoglyceric acid disodium can regulate the activity of phosphoglycerate dehydrogenase ( PHGDH ) to modulate p53 protein and apoptosis [1] [2] [3]. Uses: Scientific research. Group: Signaling pathways. Alternative Names: 3-Phospho-D-glyceric acid disodium. CAS No. 80731-10-8. Pack Sizes: 5 mg; 10 mg; 25 mg; 50 mg; 100 mg. Product ID: HY-141412. | |
| D-Amino Acid Oxidase (Crude Enzyme) | D-Amino Acid Oxidase (DAAO; also DAO, OXDA, DAMOX) is a peroxisomal enzyme containing FAD as cofactor that is expressed in a wide range of species from yeasts to human. It is not present in plants or in bacteria which instead use D-amino acid dehydrogenase. Its function is to oxidize D-amino acids to the corresponding imino acids, producing ammonia and hydrogen peroxide. DAAO is a candidate susceptibility gene and together with G72 may play a role in the glutamatergic mechanisms of schizophrenia. Risperidone andsodium benzoate are inhibitors of DAAO. DAAO is used as a biocatalyst in several biotechnological applications, such as the oxidation of cephalosporin C, the deracem...n may use the morpheein model of allosteric regulation. This product with the indicated enzyme activity was briefly purified from engineered E. coli. Applications: Biotechnology; industry; drug development; medicine; pharmacology; analysis; diagnostics; synthesis. Group: Enzymes. Synonyms: ophio-amino-acid oxidase; L-amino acid:O 2 oxidoreductase; new yellow enzyme. Enzyme Commission Number: EC 1.4.3.3. CAS No. 9000-88-8. DAAO. Activity: Undetermined. Appearance: Clear to translucent yellow solution. Storage: at -20 °C or lower, for at least 1 month. Source: E. coli. ophio-amino-acid oxidase; L-amino acid:O 2 oxidoreductase; new yellow enzyme. Pack: 100ml. Cat No: NATE-1807. | |
| D-Asparagine | D-Asparagine (H-D-Asn-OH) is a competitive inhibitor of L-Asparagine hydrolysis with a K i value of 0.24 mM. D-Asparagine is a source of nitrogen for yeast strains. D-Asparagine is a good substrate for the external yeast asparaginase but is a poor substrate for the internal enzyme [1]. Uses: Scientific research. Group: Natural products. Alternative Names: H-D-Asn-OH. CAS No. 2058-58-4. Pack Sizes: 10 mM * 1 mL; 1 g. Product ID: HY-W010378. | |
| Δ7-sterol 5(6)-desaturase | This enzyme, found in eukaryotic organisms, catalyses the introduction of a double bond between the C5 and C6 carbons of the B ring of Δ7-sterols, to yield the corresponding Δ5,7-sterols. The enzymes from yeast, plants and vertebrates act on avenasterol, episterol, and lathosterol, respectively. The enzyme is located at the endoplasmic reticulum and is membrane bound. Group: Enzymes. Synonyms: lathosterol oxidase; Δ7-sterol Δ5-dehydrogenase; Δ7-sterol 5-desaturase; Δ7-sterol-C5(6)-desaturase; 5-DES; SC5DL (gene name); ERG3 (gene name). Enzyme Commission Number: EC 1.14.19.20. CAS No. 37255-37-1. 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-0983; Δ7-sterol 5(6)-desaturase; EC 1.14.19.20; 37255-37-1; lathosterol oxidase; Δ7-sterol Δ5-dehydrogenase; Δ7-sterol 5-desaturase; Δ7-sterol-C5(6)-desaturase; 5-DES; SC5DL (gene name); ERG3 (gene name). Cat No: EXWM-0983. | |
| 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. | |
| 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. | |
| diphthine methyl ester synthase | This eukaryotic enzyme is part of the biosynthetic pathway of diphthamide. Different from the archaeal enzyme, which performs only 3 methylations, producing diphthine (cf. EC 2.1.1.98). The relevant histidine of elongation factor 2 is His715 in mammals and His699 in yeast. The order of the 4 methylations is not known. Group: Enzymes. Synonyms: S-adenosyl-L-methionine:elongation factor 2 methyltransferase (ambiguous); diphthine methyltransferase (ambiguous); Dph5 (ambiguous). Enzyme Commission Number: EC 2.1.1.314. 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-1922; diphthine methyl ester synthase; EC 2.1.1.314; S-adenosyl-L-methionine:elongation factor 2 methyltransferase (ambiguous); diphthine methyltransferase (ambiguous); Dph5 (ambiguous). Cat No: EXWM-1922. | |
| 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. | |
| endo-1,4-β-Xylanase from Clostridium thermocellum, Recombinant | Xylanase is the name given to a class of enzymes which degrade the linear polysaccharide beta-1,4-xylan into xylose, thus breaking down hemicellulose, one of the major components of plant cell walls. As such, it plays a major role in micro-organisms thriving on plant sources for the degradation of plant matter into usable nutrients. Xylanases are produced by fungi, bacteria, yeast, marine algae, protozoans, snails, crustaceans, insect, seeds, etc., (mammals do not produce xylanases). Group: Enzymes. Synonyms: EC 3.2.1.8; endo-(1?4)-β-xylan 4-xylanohydrolase; endo-1,4-xylanase; xylanase; β-1,4-xylanase; endo-1,4-xylanase; endo-β-1,4-xylanase; endo-1,4-β-D-xylanase; 1,4-&. Enzyme Commission Number: EC 3.2.1.8. CAS No. 9025-57-4. Purity: > 95 % as judged by SDS-PAGE. Xylanase. Mole weight: 39474.6 Da. Activity: 2500 U/mg. Storage: Store at 4°C (shipped at room temperature). Form: Supplied in 3.2 M ammonium sulphate. Source: Clostridium thermocellum. EC 3.2.1.8; endo-(1?4)-β-xylan 4-xylanohydrolase; endo-1,4-xylanase; xylanase; β-1,4-xylanase; endo-1,4-xylanase; endo-β-1,4-xylanase; endo-1,4-β-D-xylanase; 1,4-β-xylan xylanohydrolase; β-xylanase; β-1,4-xylan xylanohydrolase; endo-1,4-β-xylanase; β-D-xylanase; endo-1,4-β-xylanase. Cat No: NATE-1202. | |
| enoyl-[acyl-carrier-protein] reductase (NADPH, Si-specific) | One of the activities of EC 2.3.1.86, fatty-acyl-CoA synthase, an enzyme found in yeasts (Ascomycota and the Basidiomycota). Catalyses the reduction of enoyl-acyl-[acyl-carrier protein] derivatives of carbon chain length from 4 to 16. The yeast enzyme is Si-specific with respect to NADP+. cf. EC 1.3.1.39, enoyl-[acyl-carrier-protein] reductase (NADPH, Re-specific) and EC 1.3.1.104, enoyl-[acyl-carrier-protein] reductase (NADPH), which describes enzymes whose stereo-specificity towards NADPH is not known. See also EC 1.3.1.9, enoyl-[acyl-carrier-protein] reductase (NADH). Group: Enzymes. Synonyms: acy. Enzyme Commission Number: EC 1.3.1.10. CAS No. 37251-09-5. 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-1271; enoyl-[acyl-carrier-protein] reductase (NADPH, Si-specific); EC 1.3.1.10; 37251-09-5; acyl-ACP dehydrogenase (ambiguous); enoyl-[acyl carrier protein] (reduced nicotinamide adenine dinucleotide phosphate) reductase; NADPH 2-enoyl Co A reductase; enoyl acyl-carrier-protein reductase (ambiguous); enoyl-ACP reductase (ambiguous); acyl-[acyl-carrier-protein]:NADP+ oxidoreductase (B-specific); acyl-[acyl-carrier protein]:NADP+ oxidoreductase (B-specific); enoyl-[acyl-carrier-protein] reductase (NADPH, B-specific). Cat No: EXWM-1271. | |
| Enzyme blend for flour | Hemicellulase and alpha-amylase activity acts on flour pentosans and starch to improve dough elasticity and volume of yeast-raised baked goods. Applications: Extend shelf life. Group: Enzymes. Synonyms: flour; for flour; Enzyme blend for flour; Hemicellulase and alpha-amylase; Extend Shelf Life; improve dough elasticity; dough; dough elasticity; BAK-1716. Enzyme for flour. Appearance: powder or liquid. flour; for flour; Enzyme blend for flour; Hemicellulase and alpha-amylase; Extend Shelf Life; improve dough elasticity; dough; dough elasticity; BAK-1716. Pack: 25kg/paper barrel (powder form), 30kg/polyster barrel (liquid form). Cat No: BAK-1716. | |
| Enzyme blend for flour proteins | This food-grade , non-synthetic, and organic-certifiable enzyme blend is used to hydrolyze soya, pea, yeast, maize and wheat flour proteins, producing high-quality functional protein hydrolysates. Applications: Vegetable proteins. Group: Enzymes. Enzyme for flour proteins. Appearance: powder or liquid. for flour proteins; Vegetable Proteins enzyme; hydrolyze soya enzyme;hydrolyze pea enzyme; hydrolyze yeast enzyme; maize and wheat flour proteins; pea; maize; wheat; hydrolyze soya; hydrolyze; Enzyme blend for flour proteins; PRO-1825. Pack: 25kg/paper barrel (powder form), 30kg/polyster barrel (liquid form). Cat No: PRO-1825. | |
| fatty-acyl-CoA synthase | The enzyme from yeasts (Ascomycota and Basidiomycota) is a multi-functional protein complex composed of two subunits. One subunit catalyses the reactions EC 1.1.1.100, 3-oxoacyl-[acyl-carrier-protein] reductase and EC 2.3.1.41, 3-oxoacyl-[acyl-carrier-protein] synthase, while the other subunit catalyses the reactions of EC 2.3.1.38, [acyl-carrier-protein] S-acetyltransferase, EC 2.3.1.39, [acyl-carrier-protein] S-malonyltransferase, EC 4.2.1.59, 3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase, EC 1.3.1.10, enoyl-[acyl-carrier-protein] reductase (NADPH, Si-specific) and EC 1.1.1.279, (R)-3-hydroxyacid ester dehydrogenase. The enzyme differs from the animal enzyme (EC 2.3.1.85) in that the enoyl reductase domain requires FMN as a cofactor, and the ultimate product is an acyl-CoA (usually palmitoyl-CoA) instead of a free fatty acid. Group: Enzymes. Synonyms: yeast fatty acid synthase; FAS1 (gene name); FAS2 (gene name). Enzyme Commission Number: EC 2.3.1.86. CAS No. 94219-29-1. 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-2267; fatty-acyl-CoA synthase; EC 2.3.1.86; 94219-29-1; yeast fatty acid synthase; FAS1 (gene name); FAS2 (gene name). Cat No: EXWM-2267. | |
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