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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-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. | |
| 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-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-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. | |
| 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 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-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. | |
| 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. | |
| 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-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. | |
| 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. | |
| 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. | |
| 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. | |
| Galactose, Low Endotoxin, Low Glucose (D-Galactose) | D-Galactose is a C-4 epimer of Glucose found in milk and sugar beets as well as being synthesized by the body. Galactose is made from lactose through hydrolysis reaction under acidic conditions. Galactose is a simple monosaccharide that serves as an energy source and as an essential component of glycolipids and glycoproteins. Galactose contributes to energy metabolism via its conversion to glucose by the enzymes that constitute the Leloir pathway. Defects in the genes encoding these proteins lead to the metabolic disorder galactosemia. Applications:Used as an alternate carbon source for wild-type yeastInduces transcription of sequences fused to the GAL10 promoterSuitable for use in two-hybrid protocols. Component of galactosyltransferase labeling bufferSupplement in MRS broth for the growth of thermophilic lactobacilliInduces the expression of uncoupling protein (UCP) in yeast transformantsOral therapy for nephrotic syndrome in focal and segmental glomerulosclerosis. Group: Biochemicals. Alternative Names: D-(+)-Galactose; Dextrogalactose; Lactoglucose; alpha-Galactose(D). Grades: Molecular Biology Grade. CAS No. 59-23-4. Pack Sizes: 100g, 500g, 1Kg, 5Kg, 10Kg. Molecular Formula: C6H12O6, Molecular Weight: 180.16. US Biological Life Sciences. |  Worldwide |
| glycerol-1-phosphatase | The Dunaliella enzyme acts more rapidly on sn-glycerol 1-phosphate than on the 3-phosphate. The enzyme from yeast also acts on propane-1,2-diol 1-phosphate, but not on a variety of other phosphate esters. Group: Enzymes. Synonyms: α-glycerophosphatase; α-glycerol phosphatase; glycerol 3-phosphatase; glycerol-3-phosphate phosphatase; glycerol 3-phosphate phosphohydrolase. Enzyme Commission Number: EC 3.1.3.21. CAS No. 37228-75-4. 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-3624; glycerol-1-phosphatase; EC 3.1.3.21; 37228-75-4; α-glycerophosphatase; α-glycerol phosphatase; glycerol 3-phosphatase; glycerol-3-phosphate phosphatase; glycerol 3-phosphate phosphohydrolase. Cat No: EXWM-3624. | |
| glycylpeptide N-tetradecanoyltransferase | The enzyme from yeast is highly specific for tetradecanoyl-CoA, and highly specific for N-terminal glycine in oligopeptides containing serine in the 5-position. The enzyme from mammalian heart transfers acyl groups to a specific 51 kDa acceptor protein. Group: Enzymes. Synonyms: peptide N-myristoyltransferase; myristoyl-CoA-protein N-myristoyltransferase; myristoyl-coenzyme A:protein N-myristoyl transferase; myristoylating enzymes; protein N-myristoyltransferase. Enzyme Commission Number: EC 2.3.1.97. CAS No. 110071-61-9. 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-2279; glycylpeptide N-tetradecanoyltransferase; EC 2.3.1.97; 110071-61-9; peptide N-myristoyltransferase; myristoyl-CoA-protein N-myristoyltransferase; myristoyl-coenzyme A:protein N-myristoyl transferase; myristoylating enzymes; protein N-myristoyltransferase. Cat No: EXWM-2279. | |
| Gly-Xaa carboxypeptidase | From yeast. In peptidase family M20 (glutamate carboxypeptidase family). Group: Enzymes. Synonyms: glycine carboxypeptidase; carboxypeptidase a; carboxypeptidase S; peptidase α; yeast carboxypeptidase; Gly-X carboxypeptidase. Enzyme Commission Number: EC 3.4.17.4. CAS No. 9025-25-6. 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-4078; Gly-Xaa carboxypeptidase; EC 3.4.17.4; 9025-25-6; glycine carboxypeptidase; carboxypeptidase a; carboxypeptidase S; peptidase α; yeast carboxypeptidase; Gly-X carboxypeptidase. Cat No: EXWM-4078. | |
| Hexokinase from Yeast, chemically modified | 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. Recombinant enzyme that converts hexose to hexose-6-phosphate. take advantage of the improved stability in liquid reagents. rely on the proven diagnostic quality of this product. Applications: Use hexokinase in diagnostic tests for blood glucose using the hexokinase method and for the determination of creatine kinase. Group: Enzymes. Synonyms: hexokinase type . Hexokinase. Mole weight: 57 kD (SDS-PAGE). Activity: > 40 U/mg lyophilizate. Stability: At +2 to +8°C within specification range for 18 months. Store dry. Appearance: White lyophilizate. Source: Yeast. hexokinase type IV glucokinase; hexokinase D; hexokinase type IV; hexokinase (phosphorylating); ATP-dependent hexokinase; glucose ATP phosphotransferase; hexokinase; ATP:D-hexose 6-phosphotransferase. Cat No: NATE-0989. | |
| homoserine dehydrogenase | The yeast enzyme acts most rapidly with NAD+; the Neurospora enzyme with NADP+. The enzyme from Escherichia coli is a multi-functional protein, which also catalyses the reaction of EC 2.7.2.4 (aspartate kinase). Group: Enzymes. Synonyms: HSDH; HSD. Enzyme Commission Number: EC 1.1.1.3. CAS No. 9028-13-1. 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-0209; homoserine dehydrogenase; EC 1.1.1.3; 9028-13-1; HSDH; HSD. Cat No: EXWM-0209. | |
| 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. | |
| inositol-1,3,4-trisphosphate 5/6-kinase | In humans, this enzyme, along with EC 2.7.1.127 (inositol-trisphosphate 3-kinase), EC 2.7.1.140 (inositol-tetrakisphosphate 5-kinase) and EC 2.7.1.158 (inositol pentakisphosphate 2-kinase) is involved in the production of inositol hexakisphosphate (InsP6). InsP6 is involved in many cellular processes, including mRNA export from the nucleus. Yeasts do not have this enzyme, so produce InsP6 from Ins(1,4,5)P3 by the actions of EC 2.7.1.151 (inositol-polyphosphate multikinase) and EC 2.7.1.158 (inositol-pentakisphosphate 2-kinase). Group: Enzymes. Synonyms: Ins(1,3,4)P3 5/6-kinase; inositol trisphosphate 5/6-kinase. Enzyme Commission Number: EC 2.7.1.159. CAS No. 288307-53-9. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-2988; inositol-1,3,4-trisphosphate 5/6-kinase; EC 2.7.1.159; 288307-53-9; Ins(1,3,4)P3 5/6-kinase; inositol trisphosphate 5/6-kinase. Cat No: EXWM-2988. | |
| inositol-polyphosphate multikinase | This enzyme also phosphorylates Ins(1,4,5)P3 to Ins(1,3,4,5)P4, Ins(1,3,4,5)P4 to Ins(1,3,4,5,6)P5, and Ins(1,3,4,5,6)P4 to Ins(PP)P4, isomer unknown. The enzyme from the plant Arabidopsis thaliana can also phosphorylate Ins(1,3,4,6)P4 and Ins(1,2,3,4,6)P5 at the D-5-position to produce 1,3,4,5,6-pentakisphosphate and inositol hexakisphosphate (InsP6), respectively. Yeast produce InsP6 from Ins(1,4,5)P3 by the actions of this enzyme and EC 2.7.1.158, inositol-pentakisphosphate 2-kinase. Group: Enzymes. Synonyms: IpK2; IP3/IP4 6-/3-kinase; IP3/IP4 dual-specificity 6-/3-kinase; IpmK; ArgRIII; AtIpk2α; AtIpk2β; inositol polyphosphate 6-/3-/5-kinase. Enzyme Commission Number: EC 2.7.1.151. CAS No. 9077-69-4. 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-2982; inositol-polyphosphate multikinase; EC 2.7.1.151; 9077-69-4; IpK2; IP3/IP4 6-/3-kinase; IP3/IP4 dual-specificity 6-/3-kinase; IpmK; ArgRIII; AtIpk2α; AtIpk2β; inositol polyphosphate 6-/3-/5-kinase. Cat No: EXWM-2982. | |
| inositol-tetrakisphosphate 5-kinase | The enzyme from plants and yeast can also use Ins(1,2,3,4,6)P5 as a substrate. Group: Enzymes. Synonyms: 1D-myo-inositol-tetrakisphosphate 5-kinase. Enzyme Commission Number: EC 2.7.1.140. CAS No. 123940-40-9. 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-2971; inositol-tetrakisphosphate 5-kinase; EC 2.7.1.140; 123940-40-9; 1D-myo-inositol-tetrakisphosphate 5-kinase. Cat No: EXWM-2971. | |
| Invertase, Powder, Reagent Grade, 100 g | Notes: Enzyme from yeast; contains 10, 000 units per gram; keep refrigerated. Health Risk: 1. Flammability: 1. Reactivity: 0. Uses: breaks down sucrose into fructose and glucose. Grades: chem-grade reagent. CAS No. 9001-57-4. Product ID: 868900. -- SOLD FOR EDUCATIONAL USE ONLY -- |  |
| Kresoxim-methyl | Kresoxim-methyl (BAS 490 F), a Strobilurin-based fungicide, inhibits the respiration at the complex III (cytochrome bc1 complex). Kresoxim-methyl binds to complex III from yeast with an apparent K d of 0.07 μM proving a high affinity for this enzyme [1] [2]. Uses: Scientific research. Group: Signaling pathways. Alternative Names: BAS 490 F. CAS No. 143390-89-0. Pack Sizes: 5 mg; 10 mg; 25 mg. Product ID: HY-125776. | |
| 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. | |
| L-iditol 2-dehydrogenase | This enzyme is widely distributed and has been described in archaea, bacteria, yeast, plants and animals. It acts on a number of sugar alcohols, including (but not limited to) L-iditol, D-glucitol, D-xylitol, and D-galactitol. Enzymes from different organisms or tissues display different substrate specificity. The enzyme is specific to NAD+ and can not use NADP+. Group: Enzymes. Synonyms: polyol dehydrogenase; sorbitol dehydrogenase; L-iditol:NAD+ 5-oxidoreductase; L-iditol (sorbitol) dehydrogenase; glucitol dehydrogenase; L-iditol:NAD+ oxidoreductase; NAD+-dependent sorbitol dehydrogenase; NAD+-sorbitol dehydrogenase. Enzyme Commission Number: EC 1.1.1.14. CAS No. 9028-21-1. SDH. 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-0043; L-iditol 2-dehydrogenase; EC 1.1.1.14; 9028-21-1; polyol dehydrogenase; sorbitol dehydrogenase; L-iditol:NAD+ 5-oxidoreductase; L-iditol (sorbitol) dehydrogenase; glucitol dehydrogenase; L-iditol:NAD+ oxidoreductase; NAD+-dependent sorbitol dehydrogenase; NAD+-sorbitol dehydrogenase. Cat No: EXWM-0043. | |
| long-chain fatty acid ω-monooxygenase | The plant enzyme CYP704B1, which is involved in the synthesis of sporopollenin, a complex polymer found at the outer layer of spores and pollen, acts on palmitate (18:0), stearate (18:0) and oleate (18:1). The plant enzyme CYP86A1 also acts on laurate (12:0). The enzyme from the yeast Starmerella bombicola (CYP52M1) acts on C16 to C20 saturated and unsaturated fatty acids and can also hydroxylate the (ω-1) position. The mammalian enzyme CYP4A acts on laurate (12:0), myristate (14:0), palmitate (16:0), oleate (18:1), and arachidonate (20:4). Group: Enzymes. Synonyms: CYP704B1 (gene name); CYP52M1 (gene name); CYP4A (gene name); CYP86A (gene name). Enzyme Commission Number: EC 1.14.13.205. 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-0807; long-chain fatty acid ω-monooxygenase; EC 1.14.13.205; CYP704B1 (gene name); CYP52M1 (gene name); CYP4A (gene name); CYP86A (gene name). Cat No: EXWM-0807. | |
| methylglyoxal reductase (NADH) | This mammalian enzyme differs from the yeast enzyme, EC 1.1.1.283, methylglyoxal reductase (NADPH-dependent), by its coenzyme requirement, reaction direction, and enantiomeric preference. Group: Enzymes. Synonyms: methylglyoxal reductase; D-lactaldehyde dehydrogenase; methylglyoxal reductase (NADH-dependent). Enzyme Commission Number: EC 1.1.1.78. CAS No. 37250-16-1. 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-0361; methylglyoxal reductase (NADH); EC 1.1.1.78; 37250-16-1; methylglyoxal reductase; D-lactaldehyde dehydrogenase; methylglyoxal reductase (NADH-dependent). Cat No: EXWM-0361. | |
| 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. | |
| mitochondrial processing peptidase | Known from the mitochondrial matrix of fungi and mammals. Formed from two subunits, both homologous with pitrilysin, and the products of the MAS1 and MAS2 genes in yeast. In peptidase family M16 (pitrilysin family). Group: Enzymes. Synonyms: processing enhancing peptidase (for one of two subunits); mitochondrial protein precursor-processing proteinase; matrix peptidase; matrix processing peptidase; matrix processing proteinase; mitochondrial protein precursor-processing proteinase; MPP. Enzyme Commission Number: EC 3.4.24.64. CAS No. 86280-61-7. 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-4347; mitochondrial processing peptidase; EC 3.4.24.64; 86280-61-7; processing enhancing peptidase (for one of two subunits); mitochondrial protein precursor-processing proteinase; matrix peptidase; matrix processing peptidase; matrix processing proteinase; mitochondrial protein precursor-processing proteinase; MPP. Cat No: EXWM-4347. | |
| 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. | |
| NAD Kinase (Crude Enzyme) | NAD + kinase (EC 2. 7. 1. 23, NADK) is an enzyme that converts nicotinamide adenine dinucleotide (NAD + ) into NADP + through phosphorylating the NAD + coenzyme. NADP + is an essential coenzyme that is reduced to NADPH primarily by the pentose phosphate pathway to provide reducing power in biosynthetic processes such as fatty acid biosynthesis and nucleotide synthesis. The structure of the NADK from the archaean Archaeoglobus fulgidus has been determined. In humans, the genes NADK and MNADK encode NAD + kinases localized in cytosol and mitochondria,respectively. Similarly, yeast have both cytosolic and mitochondrial isoforms, and the yeast mitochondrial isoform accepts both NAD + and NADH as substrates for phosphorylation. This product with the indicated enzyme activity was briefly purified from engineered E. coli. Applications: Synthesis; agriculture; analysis. Group: Enzymes. Synonyms: DPN kinase; nicotinamide adenine dinucleotide kinase (phosphorylating); nicotinamide adenine dinucleotide kin. Enzyme Commission Number: EC 2.7.1.23. CAS No. 9032-66-0. Activity: Undetermined. Appearance: Clear to translucent yellow solution. Storage: at -20 °C or lower, for at least 1 month. Source: E. coli. DPN kinase; nicotinamide adenine dinucleotide kinase (phosphorylating); nicotinamide adenine dinucleotide kinase; NAD kinase; NADK. Pack: 100ml. Cat No: NATE-1824. | |
| Na+-exporting ATPase | A P-type ATPase that undergoes covalent phosphorylation during the transport cycle. This enzyme from yeast is involved in the efflux of Na+, with one ion being exported per ATP hydrolysed. Group: Enzymes. Enzyme Commission Number: EC 7.2.2.3 (Formerly EC 3.6.3.7). 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-4696; Na+-exporting ATPase; EC 3.6.3.7. Cat No: EXWM-4696. | |
| 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 stearothermophilus Phosphofructokinase | Phosphofructokinase is a kinase enzyme that phosphorylates fructose 6-phosphate in glycolysis. The enzyme-catalysed transfer of a phosphoryl group from ATP is an important reaction in a wide variety of biological processes. One enzyme that utilizes this reaction is phosphofructokinase (PFK), which catalyses the phosphorylation of fructose-6-phosphate to fructose-1,6-bisphosphate, a key regulatory step in the glycolytic pathway. PFK exists as a homotetramer in bacteria and mammals (where each monomer possesses 2 similar domains) and as an octomer in yeast (where there are 4 alpha-(PFK1) and 4 beta-chains (PFK2), the latter, like the mammalian monomers, possessing 2 ...cs reagent. Applications: Useful for enzymatic determiantion of fructose-6-phosphate. Group: Enzymes. Synonyms: PFKWII; EC 2.7.1.11; PFK; phosphofructokinase; 6-phosphofructokinase; Phosphofructokinase I; Phosphohexokinase. Enzyme Commission Number: EC 2.7.1.11. CAS No. 9001-80-3. PFK. Mole weight: 72 kDa (gel filtration); 35 kDa (SDS-PAGE). Activity: > 250 U/mg. Appearance: White to pale yellow powder. Storage: Storage at-20°C in the presence of a desiccant is recommended. Form: Freeze dried powder. Source: Bacillus stearothermophilus. PFKWII; EC 2.7.1.11; PFK; phosphofructokinase; 6-phosphofructokinase; Phosphofructokinase I; Phosphohexokinase. Cat No: NATE-0551. | |
| Native Bacillus subtilis Xylanase Enzyme (Food Grade) | 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). Xylanase which made from the best strain of bacillus subtilis. it is a kind of purified endo-bacteria-xylanase. it can be applied in the flour treatment for bread powder and steam brea...and chewy. 2) in the storage of bread, the appropriate xylanase can retrad bread staling, improve the water holding capacity of the bread and optimize the gluten network, thereby, preventing water loss and re-allocate, stabilize the organizational structure of the bread. 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-β-xylan xylanohydrolase; β-xylanase; β-1,4-xylan xylanohydrolase; endo-1,4-β-xylanase; β-D-xylanase; endo-1,4-β-xylanase. Enzyme Commission Number: EC 3.2.1.8. CAS | |
| Native Baker's yeast (S. cerevisiae) 3-Phosphoglyceric Phosphokinase | PhosphoglyceRate kinase (EC 2.7.2.3) (PGK) is an enzyme that catalyzes the reversible transfer of a phosphate group from 1,3-bisphosphoglyceRate (1,3-BPG) to ADP producing 3-phosphoglyceRate (3-PG) and ATP. Like all kinases it is a transferase. PGK is a major enzyme used in glycolysis, in the first ATP-geneRating step of the glycolytic pathway. In gluconeogenesis, the reaction catalyzed by PGK proceeds in the opposite direction, geneRating ADP and 1,3-BPG. Applications: 3-phosphoglyceric phosphokinase generates atp by catalyzing the transfer of a phosphate group from 1,3-diphosphoglycerate to adp. 3-phosphoglycerate phosphokinase is used to study glycolysis ...phoglyceric kinase; phosphoglycerokinase; EC 2.7.2.3. Enzyme Commission Number: EC 2.7.2.3. CAS No. 9001-83-6. 3-PGK. Activity: > 1000 units/mg protein. Storage: 2-8°C. Form: ammonium sulfate suspension. Source: Baker's yeast (S. cerevisiae). PGK; 3-PGK; ATP-3-phospho-D-glyceRate-1-phosphotransferase; ATP:D-3-phosphoglyceRate 1-phosphotransferase; 3-phosphoglyceRate kinase; 3-phosphoglyceRate phosphokinase; 3-phosphoglyceric acid kinase; 3-phosphoglyceric acid phosphokinase; 3-phosphoglyceric kinase; glyceRate 3-phosphate kinase; glycerophosphate kinase; phosphoglyceric acid kinase; phosphoglyceric kinase; phosphoglycerokinase; EC 2.7.2.3. Cat No: NATE-0006. | |
| Native Baker's yeast (S. cerevisiae) D-Ribulose-5-phosphate 3-Epimerase | RPE is a metalloenzyme and has been shown to use the divalent Zn2+ ion predominantly for catalysis. Human D-ribulose-5-phosphate 3-epimerase (hRPE) has been shown to use Fe2+ for catalysis. Applications: D-ribulose-5-phosphate 3-epimerase is an enzyme that converts the reversible conversion of d-ribulose 5-phosphate into d-xylulose 5-phosphate, which is important for the cellular response against oxidative stress. d-ribulose-5-phosphate 3-epimerase is involved in the pentose phosphate pathway, pentose and glucuronate interconversions and carbon fixation. this product is from bakers yeast and is provided as a lyophilized powder. it is useful in enzyme syste...EC 5.1.3.1. CAS No. 9024-20-8. RPE. Activity: 50-100 units/mg protein (modified Warburg-Christian). Storage: -20°C. Form: lyophilized powder. Lyophilized and essentially sulfate-free; contains approx. 35% Citrate buffer salts. Source: Baker's yeast (S. cerevisiae). EC 5.1.3.1; RPE; phosphoribulose epimerase; erythrose-4-phosphate isomerase; phosphoketopentose 3-epimerase; xylulose phosphate 3-epimerase; phosphoketopentose epimerase; ribulose 5-phosphate 3-epimerase; D-ribulose phosphate-3-epimerase; D-ribulose 5-phosphate epimerase; D-ribulose-5-P 3-epimerase; D-xylulose-5-phosphate 3-epimerase; pentose-5-phosphate 3-epimerase; 9024-20-8. Cat No: NATE-0659. | |
| Native Baker's yeast (S. cerevisiae) Enolase | Enolase is a metalloenzyme that catalyzes the interconversion of 2-phosphoglycerate to phosphoenolpyruvate. Enolase is essential for both glycolysis and gluconeogenesis. Enolase from bakers yeast is a homodimer containing two bound Mg2+ ions. The molecular weight is 93.069 kDa.The peptide consists of 436 amino acids and contains a single cysteine residue. Two of the active site components include His191 and Arg414. The phosphorylated tyrosine residue present in yeast enolase forms a substrate for phosphorylation by tyrosine protein kinase. Apart from Mg2+, the enzyme can be activated by Zn2+, Mn2+, and Cd2+. Applications: Enolase from baker?s yeast has been used in a st...d spectroscopy. it has also been used along with other proteins to study gradient chromatof ocusing-mass spectrometry; a new technique for protein analysis. Group: Enzymes. Synonyms: EC 4.2.1.11; enolase; 2-phosphoglyceRate dehydRatase; 14-3-2-protein; nervous-system specific enolase; phosphoenolpyruvate hydRatase; 2-phosphoglyceRate dehydRatase; 2-phosphoglyceric dehydRatase; 2-phosphoglyceRate enolase; γ-enolase; 2-phospho-D-glyceRate hydro-lyase; 9014-08-8. Enzyme Commission Number: EC 4.2.1.11. CAS No. 9014-8-8. Enolase. Activity: > 50 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing Tris buffer salts. Source: Baker's yeast (S. cerevisiae) | |
| 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 Baker's yeast Uridine-5'-diphosphoglucose pyrophosphorylase | UTP-glucose-1-phosphate uridylyltransferase is an enzyme associated with glycogenesis. It synthesizes UDP-glucose from glucose-1-phosphate and UTP; i.e., glucose-1-phosphate + UTP<-> UDP-glucose + pyrophosphate. Applications: Uridine-5?-diphosphoglucose pyrophosphorylase has been used in assays to determine the concentration of pyrophosphate in human urine samples. Group: Enzymes. Synonyms: UDP glucose pyrophosphorylase; glucose-1-phosphate uridylyltransferase; UDPG phosphorylase; UDPG pyrophosphorylase; uridine 5'-diphosphoglucose pyrophosphorylase; uridine diphosphoglucose pyrophosphorylase; uridine diphosphate-D-glucose pyrophosphorylase; uridine-diphosphate glucose pyrophosphorylase; EC 2.7.7.9; 9026-22-6. Enzyme Commission Number: EC 2.7.7.9. CAS No. 9026-22-6. UDPG pyrophosphorylase. Activity: > 50 units/mg protein. Storage: -20°C. Form: Lyophilized, sulfate-free powder containing Citrate buffer salt. Source: Baker's yeast. UDP glucose pyrophosphorylase; glucose-1-phosphate uridylyltransferase; UDPG phosphorylase; UDPG pyrophosphorylase; uridine 5'-diphosphoglucose pyrophosphorylase; uridine diphosphoglucose pyrophosphorylase; uridine diphosphate-D-glucose pyrophosphorylase; uridine-diphosphate glucose pyrophosphorylase; EC 2.7.7.9; 9026-22-6. Cat No: NATE-0728. | |
| Native Brewer's bottom yeast Orotidine-5'-monophosphate pyrophosphorylase | Orotate phosphoribosyltransferase (OPRTase) or Orotic acid phosphoribosyltransferase is an enzyme involved in pyrimidine biosynthesis. It catalyzes the formation of orotidine 5'-monophosphate (OMP) from orotate and phosphoribosyl pyrophosphate. In yeast and bacteria, orotate phosphoribosyltransferase is an independent enzyme with a unique gene coding for the protein, whereas in mammals and other multicellular organisms, the catalytic function is carried out by a domain of the bifunctional enzyme UMP synthase. Applications: This is the preferred enzyme for assaying orotidine 5?-monophosphate and for the production of omp analogs from the corresponding orot...ty: ~25 units/mg protein (modified Warburg-Christian). Storage: -20°C. Form: Lyophilized powder containing approx. 50% buffer salts. Source: Brewer's bottom yeast. orotidylic acid phosphorylase; orotidine-5'-phosphate pyrophosphorylase; OPRTase; orotate phosphoribosyl pyrophosphate transferase; orotic acid phosphoribosyltransferase; orotidine 5'-monophosphate pyrophosphorylase; orotidine monophosphate pyrophosphorylase; orotidine phosphoribosyltransferase; orotidylate phosphoribosyltransferase; orotidylate pyrophosphorylase; orotidylic acid pyrophosphorylase; orotidylic phosphorylase; orotidylic pyrophosphorylase; EC 2.4.2.10; 9030-25-5. Cat No: NATE-0498. | |
| Native Candida boidinii Formate Dehydrogenase | Formate dehydrogenase is involved in the stress response of plants and catalyzes the reduction of NAD+ to NADH. Fdh is an abundant enzyme from yeast candida boidinii (cbfdh) that plays an important role in the energy supply of methylotrophic microorganisms and in the stress response of plants. Applications: Formate dehydrogenase (fdh) is used for diagnostics in large scale industrial pr ocesses. its used in the production of an unnatural amino acid, tert-l-leucine, a component of some hiv protease and matrix metalloprotease inhibitors. Group: Enzymes. Synonyms: EC 1.2.1.2; 9028-85-7; formate-NAD oxidoreductase; FDH; FDH I; FDH II; N-FDH; formic hydrogen-lyase; formate hydrogenlyase; hydrogenlyase; NAD-linked formate. Enzyme Commission Number: EC 1.2.1.2. CAS No. 9028-85-7. FDH. Activity: Type I, 5.0-15.0 units/mg protein; Type II, 0.3-0.6 units/mg; Type III, ~50 U/mL. Storage: -20°C. Form: Type I, lyophilized powder; Type II, powder; Type III, clear brown liquid. Source: Candida boidinii. EC 1.2.1.2; 9028-85-7; formate-NAD oxidoreductase; FDH; FDH I; FDH II; N-FDH; formic hydrogen-lyase; formate hydrogenlyase; hydrogenlyase; NAD-linked formate dehydrogenase; NAD-dependent formate dehydrogenase; formate dehydrogenase (NAD); NAD-formate dehydrogenase; formate benzyl-viologen oxidoreductase; formic acid dehydrogenase. Cat No: NATE-0254. | |
| Native Environmental DNA Pustulanase (β-glucanase) | A thermostable β-1,6-endoglucanase or pustulanase (E.C. 3.2.1.75) which catalyses the cleavage of β-1,6 bonds in pustulan and other beta-glucans containing 1,6 linked glucose units. The enzyme is now a component in a standard assay for beta-glucan from Bakers yeast as documented in US Pharmacopeia Food and Chemicals Index. Group: Enzymes. Synonyms: EC 3.2.1.75; glycoside hydrolase; pustulanase; glucan endo-1,6-β-glucosidase; 6-β-D-glucan glucanohydrolase; endo-1,6-β-glucanase; β-1?6)-β-D-glucanase; β-1,6-glucanase-pustulanase; β-1,6-glucan hydrolase; β-1,6-glucan 6-glucanohydrolase; 1,6-β-D-glucan glucanohydrolase. Enzyme Commission Number: EC 3.2.1.75. CAS No. 37278-39-0. Pustulanase. Source: Proprietary metagenome environmental DNA. Species: Environmental DNA. EC 3.2.1.75; glycoside hydrolase; pustulanase; glucan endo-1,6-β-glucosidase; 6-β-D-glucan glucanohydrolase; endo-1,6-β-glucanase; β-1?6)-β-D-glucanase; β-1,6-glucanase-pustulanase; β-1,6-glucan hydrolase; β-1,6-glucan 6-glucanohydrolase; 1,6-β-D-glucan glucanohydrolase. Cat No: NATE-0645. | |
| Native Escherichia coli Thioredoxin Reductase | Thioredoxin reductase (TrxR) is an NADPH-dependent oxidoreductase containing one FAD per subunit that reduces the active site disulfide in oxidised thioredoxin (Trx). The molecular weight of the isozymes from mammalian sources vary between 55-67 kDa as compared with 35 kDa in prokaryotes, plants or yeast. The substrate specificity of the mammalian enzyme is much broader than the prokaryotic enzyme reducing both mammalian and E. coli thioredoxins as well as well as non-disulfide substrates such selenite, lipoic acids, lipid hydroperoxides and hydrogen peroxide. Applications: Thioredoxin reductase from escherichia coli can be used in peroxidase-coupled thioredoxin system assay for assessing the peroxidase activitiy of cys-based thiol peroxidases. the product was used for determining the enzymatic activity of his6-ahp1p. Group: Enzymes. Synonyms: NADP-thioredoxi. Enzyme Commission Number: EC 1.8.1.9. CAS No. 9074-14-0. TrxR. Activity: >25 units/mg protein (Bradford). Storage: 2-8°C. Form: ammonium sulfate suspension; Suspension in 3.6 M (NH4)2SO4 containing 30 mM potassium phosphate buffer, pH 7.5, and 2 mM EDTA. Source: Escherichia coli. NADP-thioredoxin reductase; NADPH-thioredoxin reductase; thioredoxin reductase (NADPH); NADPH2:oxidized thioredoxin oxidoreductase; thioredoxin-disulfide reductase; EC 1.8.1.9; TrxR. Cat No: NATE-0718. | |
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