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| Product | Description | |
|---|---|---|
| Yeast Beta Glucan (1,3/1,6) 70% & 85% | Yeast Beta Glucan (1,3/1,6) 70% & 85%. |  CA, FL & NJ |
| Yeast, Brewer's, Powder, Laboratory Grade, 500 g | Brewer's Yeast, Powder, Laboratory Grade, 500 g. Grades: chem-grade laboratory. Product ID: 898900. -- SOLD FOR EDUCATIONAL USE ONLY -- |  |
| Yeast extract | 100g Pack Size. Group: Analytical Reagents, Biochemicals, Diagnostic Raw Materials. Formula: N/A. CAS No. 8013-1-2. Prepack ID 35752308-100g. See USA prepack pricing. |  |
| Yeast extract | 1kg Pack Size. Group: Analytical Reagents, Biochemicals, Diagnostic Raw Materials. Formula: N/A. CAS No. 8013-1-2. Prepack ID 35752308-1kg. See USA prepack pricing. | |
| Yeast extract | Yeast extract is a concentrate of the soluble part of yeast, especially Saccharomyces cerevisiae. The main nutritional components of yeast extract include partly hydrolyzed protein with 35-40% of free amino acid, and it also contain B vitamins and some trace elements. Yeast extract can be used as nutrients for bacterial culture media [1]. Uses: Scientific research. Group: Biochemical assay reagents. CAS No. 8013-1-2. Pack Sizes: 50 g; 100 g. Product ID: HY-153126. |  |
| Yeast Extract | Yeast Extract is a food flavoring. It can be used in culture medium. Synonyms: Yeast, ext.; Yeast powder; Extract of Yeast; Yeast Extract Powder. CAS No. 8013-1-2. |  |
| Yeast Extract Polar | Yeast Extract Polar. Group: Others. Stability: 3 Months. Storage: -20°C. Avanti Polar Lipids; lipid products; natural lipids; natural; synthetic lipid; synthetic; modified lipids; headgroup modified lipids; fatty acid modified lipids; singnal transduction; cell pathways; Yeast Extract Polar; Yeast Polar Lipid Extract (S. cerevisiae). Cat No: NSMZ-048. |  |
| Yeast Extract Total | Yeast Extract Total. Group: Others. Stability: 3 Months. Storage: -20°C. Avanti Polar Lipids; lipid products; natural lipids; natural; synthetic lipid; synthetic; modified lipids; headgroup modified lipids; fatty acid modified lipids; singnal transduction; cell pathways; Yeast Extract Total; Yeast Total Lipid Extract (S. cerevisiae). Cat No: NSMZ-047. | |
| Yeast, Powder, Activated, Laboratory Grade, 100 g | Storage Code: Green; general chemical storage. Grades: chem-grade laboratory. Product ID: 898890. -- SOLD FOR EDUCATIONAL USE ONLY -- | |
| Yeast Protein Extract | Yeast Protein Extract. Uses: For analytical and research use. Group: Building blocks. Alternative Names: TP. Catalog: APS013955. Shipping: Room Temperature. |  |
| yeast ribonuclease | Similar enzyme: RNase U4. Group: Enzymes. Enzyme Commission Number: EC 3.1.14.1. 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-3541; yeast ribonuclease; EC 3.1.14.1. Cat No: EXWM-3541. | |
| Yeast S | A dried Aspergillus oryzae fermentation extract that is an ideal nutrient support system for yeast during the fermentation process. It contains protein, free-form amino acids, minerals, enzymes, vitamins, fiber and other nutrients. Group: Enzymes. Synonyms: Yeast S; Yeast; BRE-1622. Yeast S. Appearance: powder or liquid. Yeast S; Yeast; BRE-1622. Pack: 25kg/paper barrel (powder form), 30kg/polyster barrel (liquid form) or subject to client requirement. Cat No: BRE-1622. | |
| Yeasts. Riched selenium | Yeasts. Riched selenium. Product ID: CDF4-0217. Molecular formula: NA. Category: Nutrient supplements. Product Keywords: Food Ingredients; Nutrients; CDF4-0217; Yeasts. Riched selenium; Nutrient supplements. Applications: Used as selenium enhancer in dairy products, rice products, biscuits and beverages. |  |
| α-Factor Mating Pheromone, yeast | Alpha1-Mating Factor a tridecapeptide secreted by S. cerevisiae α cells via Ste2p receptor, facilitates in regulating the mating in yeast. Synonyms: Trp-His-Trp-Leu-Gln-Leu-Lys-Pro-Gly-Gln-Pro-Met-Tyr; Mating Factor α; alphaSC1-Pheromone; L-tryptophyl-L-histidyl-L-tryptophyl-L-leucyl-L-glutaminyl-L-leucyl-L-lysyl-L-prolyl-glycyl-L-glutaminyl-L-prolyl-L-methionyl-L-tyrosine. Grades: 95%. CAS No. 59401-28-4. Molecular formula: C82H114N20O17S. Mole weight: 1683.97. | |
| α-Factor Mating Pheromone, yeast | α-Factor Mating Pheromone, yeast is a tridecapeptide secreted by S. cerevisiae α cells via Ste2p receptor. Uses: Scientific research. Group: Peptides. Alternative Names: Mating Factor α. CAS No. 59401-28-4. Pack Sizes: 1 mg; 5 mg. Product ID: HY-P1482. | |
| α-Factor Mating Pheromone, yeast acetate | α-Factor Mating Pheromone, yeast acetate is a tridecapeptide secreted by Saccharomyces cerevisiae α cells via the Ste2p receptor, which facilitates in regulating the mating in yeast. Synonyms: H-Trp-His-Trp-Leu-Gln-Leu-Lys-Pro-Gly-Gln-Pro-Met-Tyr-OH.CH3CO2H; Mating Factor α acetate; alphaSC1-Pheromone acetate; L-tryptophyl-L-histidyl-L-tryptophyl-L-leucyl-L-glutaminyl-L-leucyl-L-lysyl-L-prolyl-glycyl-L-glutaminyl-L-prolyl-L-methionyl-L-tyrosine acetic acid. Grades: ≥95%. Molecular formula: C84H118N20O19S. Mole weight: 1744.05. | |
| 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. | |
| Amino Acid Complex with Yeast Extract | Amino acid complex combined with yeast extract (Saccharomyces cerevisiae). It enhances oxygen uptake, cell viability and cell turnover for a youthful-looking skin. Uses: Anti-aging creams lotions, and serums. skin-rejuvenating products. Group: Skin actives. CAS No. 84604-16-0 / 72-18-4 / 72-19-5 / 56-86-0 / 56-40-6 / 56-81-5 / 7732-18-5 / 150-90-3 / 122-99-6 / 70445-33-9. Appearance: Clear to a pale yellow liquid. Catalog: CI-SC-0579. |  |
| Baker's yeast (S. cerevisiae) Carboxypeptidase Y, recombinant | Carboxypeptidase Y (CPY) catalyzes the following reaction: Peptidyl-L-amino acid + H2O ------> Peptide + L-amino acid.It is prepared according to the method of Moore & Stein (J. Biol Chem, 211, 907, 1954). It resembles Carboxypeptidase A in its substrate specificity, but it hydrolyzes C-terminal glycine and L-leuicine more rapidly and L-phenylalanine more slowly. Group: Enzymes. Synonyms: carboxypeptidase Y; serine carboxypeptidase I; cathepsin A; lysosomal protective protein; deamidase; lysosomal carboxypeptidase A; phaseolin; EC 3.4.16.5; 9046-67-7; Peptidyl-L-amino acid Hydrolase; Serine Carboxypeptidase; Carboxypeptidase C; Peptidyl-L. Enzyme Commission Number: EC 3.4.16.1. Purity: > 90 %. Carboxypeptidase Y. Activity: > 10u/mg. Appearance: Clear, colorless to lightly colored. Storage: Long term below -20°C, short term 2-8°C. Avoid multiple freeze-thaws. Form: 500 mM sodium chloride, 500 mM imidazole, 20 mM sodium phosphate monobasic, 20 mM sodium phosphate dibasic, pH 7.5. Species: S. cerevisiae. carboxypeptidase Y; serine carboxypeptidase I; cathepsin A; lysosomal protective protein; deamidase; lysosomal carboxypeptidase A; phaseolin; EC 3.4.16.5; 9046-67-7; Peptidyl-L-amino acid Hydrolase; Serine Carboxypeptidase; Carboxypeptidase C; Peptidyl-L-amino-acid (-L-proline ) hydrolase; EC 3.4.12.8. Cat No: NATE-0103. | |
| b-D-Glucan - from Yeast (Saccharomyces Cerevisiae) | b-D-Glucan - from Yeast (Saccharomyces Cerevisiae): b-D-Glucan, derived from Saccharomyces cerevisiae yeast, is a natural compound utilized in the biomedical industry. Widely recognized for its immunomodulatory properties, b-D-Glucan is extensively employed as an adjuvant in vaccines and therapeutics for enhancing immune responses. Uses: Adjuvants, immunologic. Synonyms: 1,3-b-D-Glucan; b-1,3-D-Glucan. CAS No. 9012-72-0. Molecular formula: (C6H10O5)n. Mole weight: 472.4. | |
| Chromium Yeast 0.2% | Chromium Yeast 0.2%. | CA, FL & NJ |
| Glucan from Black Yeast | Glucan from Black Yeast. Group: Polymers. CAS No. 9012-72-0. Product ID: (2S,3R,4S,5S,6R)-2-[(2R,4R,5R,6S)-4,5-dihydroxy-2-(hydroxymethyl)-6-[(2R,4R,5R,6S)-4,5,6-trihydroxy-2-(hydroxymethyl)oxan-3-yl]oxyoxan-3-yl]oxy-6-(hydroxymethyl)oxane-3,4,5-triol. Molecular formula: 504.4g/mol. Mole weight: C18H32O16. C (C1C (C (C (C (O1)OC2C (OC (C (C2O)O)OC3C (OC (C (C3O)O)O)CO)CO)O)O)O)O. InChI=1S/C18H32O16/c19-1-4-7 (22)8 (23)12 (27)17 (31-4)34-15-6 (3-21)32-18 (13 (28)10 (15)25)33-14-5 (2-20)30-16 (29)11 (26)9 (14)24/h4-29H, 1-3H2/t4-, 5-, 6-, 7-, 8+, 9-, 10-, 11-, 12-, 13-, 14?, 15?, 16+, 17+, 18+/m1/s1. FYGDTMLNYKFZSV-URKRLVJHSA-N. |  |
| Glutathione Reductase, baker's yeast | Glutathione reductase (EC 1.6.4.2) (EC 1.6.4.2) is a reductase responsible for maintaining the supply of reduced glutathione [1]. Uses: Scientific research. Group: Signaling pathways. Alternative Names: EC 1.6.4.2; GR. CAS No. 9001-48-3. Pack Sizes: 100 U. Product ID: HY-125862. | |
| 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. | |
| Invertase, baker's yeast (S. cerevisiae) | Invertase, baker's yeast (S. cerevisiae) is a major enzyme present in plants and microorganisms, is often used in biochemical studies. Invertase catalyzes the hydrolysis of the disaccharide sucrose into glucose and fructose [1]. Uses: Scientific research. Group: Signaling pathways. Alternative Names: β-D-Fructofuranosidase. CAS No. 9001-57-4. Pack Sizes: 250 mg; 500 mg; 1 g. Product ID: HY-P2979. | |
| Isocitrate Dehydrogenase (NADP+) from Yeast, Recombinant | Isocitrate dehydrogenase (IDH) (EC 1.1.1.42) is an enzyme that catalyzes the oxidative decarboxylation of Isocitrate, producing alpha-ketoglutarate (α-ketoglutarate) and CO2. This is a two-step process, which involves oxidation of Isocitrate (a secondary alcohol) to oxalosuccinate (a ketone), followed by the decarboxylation of the carboxyl group beta to the ketone, forming alpha-ketoglutarate. In humans, IDH exists in three isoforms:IDH3 catalyzes the third step of the citric acid cycle while converting NAD+ to NADH in the mitochondria. The isoforms IDH1 and IDH2 catalyze the same reaction outside the context of the citric acid cycle and use NADP+ as a cofactor instead of NAD+. They localize to the cytosol as well as the mitochondrion and peroxisome. Group: Enzymes. Synonyms: Isocitrate Dehydrogenase (NADP+); EC 1.1.1.42; IDH; Isocitrate . Enzyme Commission Number: EC 1.1.1.42. CAS No. 9028-48-2. IDH. Activity: r-ICDH activity = 100%. Storage: -20°C. Form: Liquid. Source: Pichia pastoris. Species: Yeast. Isocitrate Dehydrogenase (NADP+); EC 1.1.1.42; IDH; Isocitrate Dehydrogenase; Dual-cofactor-specific Isocitrate dehydrogenase; IDP; Isocitrate (NADP) dehydrogenase; Isocitrate (nicotinamide adenine dinucleotide phosphate) dehydrogenase; Isocitrate dehydrogenase (NADP); Isocitrate dehydrogenase (NADP-dependent); NADP | |
| Lipase (Yeast) | A lipase enzyme that gives non-specific fat and oil hydrolysis over a broad pH range. Applications: Dietary supplements. Group: Enzymes. Synonyms: Lipase; (Yeast). CAS No. 9001-62-1. Lipase. Appearance: powder or liquid. Source: Candida cylindracea (Candida rugosa). Lipase Feed Grade Enzymes; digestion and utilization of fat; for Fish; piglet; fowl; Feed;Lipase; Feed Grade Enzymes; Lipase Feed Grade Enzymes; FEED-2321. Pack: 25kg/paper barrel (powder form), 30kg/polyster barrel (liquid form). Cat No: DIS-1027. | |
| 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) Glucose-6-phosphate Dehydrogenase | Glucose-6-phosphate dehydrogenase (G6PD or G6PDH) (EC 1.1.1.49) is a cytosolic enzyme that catalyzes the chemical reaction:D-glucose 6-phosphate + NADP+ <-> 6-phospho-D-glucono-1,5-lactone + NADPH + H+. This enzyme is in the pentose phosphate pathway, a metabolic pathway that supplies reducing energy to cells (such as erythrocytes) by maintaining the level of the co-enzyme nicotinamide adenine dinucleotide phosphate (NADPH). Applications: Glucose-6-phosphate dehydrogenase is used to test ketose reductase activity in developing maize endosperm. Group: Enzymes. Synonyms: Glucose-6-phosphate dehydrogenase; G6PD; G6PDH; Glucose-6-phosphate dehydrogenase (NADP(+)); EC 1.1.1.49; Glucose-6-phosphate 1-dehydrogenase; Glucose-6-phosphate dehydrogenase; GPD. Enzyme Commission Number: EC 1.1.1.49. CAS No. 9001-40-5. Glucose-6-phosphate dehydrogenase. Storage: -20°C. Form: lyophilized powder. Source: Baker's yeast (S. cerevisiae). Glucose-6-phosphate dehydrogenase; G6PD; G6PDH; Glucose-6-phosphate dehydrogenase (NADP(+)); EC 1.1.1.49; Glucose-6-phosphate 1-dehydrogenase; Glucose-6-phosphate dehydrogenase; GPD. Cat No: DIA-219. | |
| Native Baker's yeast (S. cerevisiae) Glutathione Reductase | Glutathione reductase (GR) is a crucial flavoenzyme in the antioxidant defense system. Reduced glutathione (GSH) is used by glutathione peroxidase to detoxify hydrogen peroxide and in the precess is converted to oxidized glutathione (GSSG). The GSSG is then recycled back to GSH by glutathione reductase (GR) using NADPH that is then converted to NADP+. The regenerated GSH is then available to detoxify more hydrogen peroxide. The enzyme uses FAD as a cofactor. GR and glutathione peroxidase may inhibit lipid peroxidation by functioning as antioxidant enzymes in sperm. Glutathione reductase shares a structural motif with a number of other proteins including aspartyl ...reductase; NADPH-GSSG reductase; glutathione S-reductase; NADPH:oxidized-glutathione oxidoreductase. Enzyme Commission Number: EC 1.6.4.2. CAS No. 9001-48-3. GR. Mole weight: mol wt 118 kDa. Activity: 100-300 units/mg protein (biuret). Storage: 2-8°C. Form: ammonium sulfate suspension; Suspension in 3.6 M (NH4)2SO4, pH 7.0, containing 0.1 mM dithiothreitol. Source: Baker's yeast (S. cerevisiae). EC 1.6.4.2; 9001-48-3; Glutathione Reductase; GR; glutathione reductase; glutathione reductase (NADPH); NADPH-glutathione reductase; GSH reductase; GSSG reductase; NADPH-GSSG reductase; glutathione S-reductase; NADPH:oxidized-glutathione oxidoreductase. Cat No: NATE-0317. | |
| Native Baker's yeast (S. cerevisiae) Glyceraldehyde-3-phosphate Dehydrogenase | Glyceraldehyde-3-phosphate dehydrogenase catalyzes the conversion of glyceraldehyde-3-phosphate to 1,3-bisphosphoglycerate as part of glycolysis. It has also been shown to have roles in initiation of apoptosis, transcription activation and the shuttling of ER to Golgi vesicles. Group: Enzymes. Synonyms: EC 1.2.1.12; GAPDH; glyceraldehyde-3-phosphate dehydrogenase (phosphorylating); triosephosphate dehydrogenase; dehydrogenase, glyceraldehyde phosphate; phosphoglyceraldehyde dehydrogenase; 3-phosphoglyceraldehyde . Enzyme Commission Number: EC 1.2.1.12. CAS No. 9001-50-7. Glyceraldehyde-3-phosphate Dehydrogenase. Activity: 70-140 units/mg protein. Storage: -20°C. Form: Lyophilized, sulfate-free powder stabilized with trehalose, Citrate, and DTT. Useful for systems requiring low sulfate. Source: Baker's yeast (S. cerevisiae). EC 1.2.1.12; GAPDH; glyceraldehyde-3-phosphate dehydrogenase (phosphorylating); triosephosphate dehydrogenase; dehydrogenase, glyceraldehyde phosphate; phosphoglyceraldehyde dehydrogenase; 3-phosphoglyceraldehyde dehydrogenase; NAD+-dependent glyceraldehyde phosphate dehydrogenase; glyceraldehyde phosphate dehydrogenase (NAD+); glyceraldehyde-3-phosphate dehydrogenase (NAD+); NADH-glyceraldehyde phosphate dehydrogenase; glyceraldehyde-3-P-dehydrogenase; 9001-50-7. Cat No: NATE-0278. | |
| Native Baker's yeast (S. cerevisiae) Inorganic Pyrophosphatase | Pyrophosphatase (or inorganic pyrophosphatase) is an enzyme (EC 3.6.1.1) that catalyzes the conversion of one molecule of pyrophosphate to two phosphate ions. This is a highly exergonic reaction, and therefore can be coupled to unfavorable biochemical transformations in order to drive these transformations to completion. The functionality of this enzyme plays a critical role in lipid metabolism (including lipid synthesis and degradation), calcium absorption and bone formation, and DNA synthesis,as well as other biochemical transformations. This ubiquitous enzyme serves to drive metabolic reactions that produce pyrophosphate, since these reactions typically have...phohydrolase; inorganic pyrophosphatase; EC 3.6.1.1; 9024-82-2; iphosphate phosphohydrolase. Enzyme Commission Number: EC 3.6.1.1. CAS No. 9024-82-2. Inorganic pyrophosphatase. Mole weight: 71 kDa (homodimer consisting of two equal subunits of molecular weight 32-35 kDa). Activity: Type I, > 1,000 units/mg protein (BCA); Type II, > 500 units/mg protein (E1%/280). Storage: -20°C. Form: Type I, lyophilized powder containing 90% buffer salts; Type II, Lyophilized powder containing 85% buffer salts. Source: Baker's yeast (S. cerevisiae). Pyrophosphate phosphohydrolase; inorganic pyrophosphatase; EC 3.6.1.1; 9024-82-2; iphosphate phosphohydrolase. Cat No: NATE-0354. | |
| Native Baker's yeast (S. cerevisiae) Invertase | Invertase is an enzyme that catalyzes the hydrolysis (breakdown) of sucrose (table sugar). The resulting mixture of fructose and glucose is called inverted sugar syrup. Related to invertases are sucrases. Invertases and sucrases hydrolyze sucrose to give the same mixture of glucose and fructose. Invertases cleave the O-C (fructose) bond, whereas the sucrases cleave the O-C (glucose) bond. Typically used in manufacturing confectionaries, dietary supplements, and other food grade applications. Applications: Used in the production of confectionary foods and artificial honey. Group: Enzymes. Synonyms: EC 3.2.1.26; invertase; saccharase; glucosucrase; β-h-fructosidase; β-fructosidase; invertin; sucrase; maxinvert L 1000; fructosylinvertase; alkaline invertase; acid invertase; β-fructofuranosidase; β-D-fructofuranoside fructohydrolase; 9001-57. Enzyme Commission Number: EC 3.2.1.26. CAS No. 9001-57-4. Invertase. Activity: Type I, 200-300 units/mg solid; Type II, > 300 units/mg solid. Storage: -20°C. Source: Baker's yeast (S. cerevisiae). EC 3.2.1.26; invertase; saccharase; glucosucrase; β-h-fructosidase; β-fructosidase; invertin; sucrase; maxinvert L 1000; fructosylinvertase; alkaline invertase; acid invertase; β-fructofuranosidase; β-D-fructofuranoside fructohydrolase; 9001-57-4. Cat No: NATE-0357. | |
| 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 (S. cerevisiae) Phosphoglucose Isomerase | Phosphoglucose Isomerase (PGI) is an enzyme crucial for the interconversion of D-glucose 6-phosphate and D-fructose 6-phosphate. PGI is responsible for the second step of glycolysis and is involved in glucogenesis. It is highly conserved in bacteria and eukaryotes. Applications: Isomerization of ketoses to aldoses. Group: Enzymes. Synonyms: Glucose-6-phosphate isomerase; EC 5.3.1.9; phosphohexose isomerase; phosphohexomutase; oxoisomerase; hexosephosphate isomerase; phosphosaccharomutase; phosphoglucoisomerase; phosphohexoisomerase; phosphoglucose isomerase; glucose phosphate isomerase; hexose phosphate isomerase; D-glucose-6-phosphate ketol-isomerase; 9001-41-6; PGI. Enzyme Commission Number: EC 5.3.1.9. CAS No. 9001-41-6. PGI. Mole weight: 145 kDa. Activity: 350 U/mg at +25°C with F6P as substrate. Storage: Stable at +2 to +8°C. Source: Baker's yeast (S. cerevisiae). Glucose-6-phosphate isomerase; EC 5.3.1.9; phosphohexose isomerase; phosphohexomutase; oxoisomerase; hexosephosphate isomerase; phosphosaccharomutase; phosphoglucoisomerase; phosphohexoisomerase; phosphoglucose isomerase; glucose phosphate isomerase; hexose phosphate isomerase; D-glucose-6-phosphate ketol-isomerase; 9001-41-6; PGI. Cat No: NATE-0554. | |
| Native baker's yeast (S. cerevisiae) Proteinase A | Saccharopepsin is an enzyme. This enzyme catalyses the following chemical reaction:Hydrolysis of proteins with broad specificity for peptide bonds. Cleaves-Leu-Leu-Val-Tyr bond in a synthetic substrate. This enzyme is present in baker's yeast (Saccharomyces cerevisiae). Applications: Possibly useful for producing overlap peptides in sequence studies. Group: Enzymes. Synonyms: Endopeptidase; Proteinase A; EC 3.4.23.25; yeast endopeptidase A; Saccharomyces aspartic proteinase; aspartic proteinase yscA; proteinase yscA; yeast proteinase A; Saccharomyces cerevisiae aspartic proteinase A. Enzyme Commission Number: EC 3.4.23.25. Proteinase A. Activity: 15-50 units/mg protein. Storage: -20°C. Form: Lyophilized solids containing sodium Citrate, pH 5.0. Source: S. cerevisiae. Species: baker's yeast. Endopeptidase; Proteinase A; EC 3.4.23.25; yeast endopeptidase A; Saccharomyces aspartic proteinase; aspartic proteinase yscA; proteinase yscA; yeast proteinase A; Saccharomyces cerevisiae aspartic proteinase A. Pack: Package size based on protein content. Cat No: NATE-0636. | |
| Native Baker's yeast (S. cerevisiae) Pyruvate Decarboxylase | Pyruvate decarboxylase (PDC) is a homotetrameric enzyme that catalyses the decarboxylation of pyruvic acid to acetaldehyde and carbon dioxide in the cytoplasm. Pyruvate decarboxylase depends on cofactors thiamine pyrophosphate (TPP) and magnesium. PDC contains a β-α-β structure, yielding parallel β-sheets. Applications: Pyruvate decarboxylase (pdc) is used to study residues involved in thiamine pyrophosphate (tpp) binding. it is used to study the regulation of fermentation pathways in plant species. Group: Enzymes. Synonyms: Pyruvate decarboxylase; EC 4.1.1.1; α-carboxylase (ambiguous); pyruvic decarboxylase; α-ketoacid carboxylase; 2-oxo-acid carboxy-lyase; 9001-04-1; 2-Oxo-acid carboxy-lyase; PDC. Enzyme Commission Number: EC 4.1.1.1. CAS No. 9001-4-1. PDC. Activity: 5.0-20.0 units/mg protein (biuret). Storage: 2-8°C. Form: ammonium sulfate suspension; Suspension in 3.2 M (NH4)2SO4 pH 6.5, stabilized with 5% glycerol, 5 mM potassium phosphate, 1 mM magnesium acetate, 0.5 mM EDTA, and 25 μM c ocarboxylase. Source: Baker's yeast (S. cerevisiae). Pyruvate decarboxylase; EC 4.1.1.1; α-carboxylase (ambiguous); pyruvic decarboxylase; α-ketoacid carboxylase; 2-oxo-acid carboxy-lyase; 9001-04-1; 2-Oxo-acid carboxy-lyase; PDC. Cat No: NATE-0510. | |
| 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 Baker's yeast (S. cerevisiae) Transaldolase | Transaldolase is an enzyme (EC 2.2.1.2) of the non-oxidative phase of the pentose phosphate pathway. In humans, transaldolase is encoded by the TALDO1 gene. The following chemical reaction is catalyzed by transaldolase:sedoheptulose 7-phosphate + glyceraldehyde 3-phosphate<-> erythrose 4-phosphate + fructose 6-phosphate. Applications: Useful in systems requiring low sulfate concentrations. Group: Enzymes. Synonyms: Transaldolase; EC 2.2.1.2; 9014-46-4; dihydroxyacetonetransferase; dihydroxyacetone synthase; formaldehyde transketolase; D-Sedoheptulose-7-phosphate:D-Glyceraldehyde-3-phosphate dihydroxyacetonetransferase. Enzyme Commission Number: EC 2.2.1.2. CAS No. 9014-46-4. Transaldolase. Activity: 10-30 units/mg protein (biuret). Storage: -20°C. Form: Lyophilized, essentially sulfate-free; contains approx. 5% Citrate buffer salts. Source: Baker's yeast (S. cerevisiae). Transaldolase; EC 2.2.1.2; 9014-46-4; dihydroxyacetonetransferase; dihydroxyacetone synthase; formaldehyde transketolase; D-Sedoheptulose-7-phosphate:D-Glyceraldehyde-3-phosphate dihydroxyacetonetransferase. Cat No: NATE-0714. | |
| Native Baker's yeast (S. cerevisiae) Triosephosphate Isomerase | Triose-phosphate isomerase (TPI or TIM) is an enzyme (EC 5.3.1.1) that catalyzes the reversible interconversion of the triose phosphate isomers dihydroxyacetone phosphate and D-glyceraldehyde 3-phosphate. TPI plays an important role in glycolysis and is essential for efficient energy production. TPI has been found in nearly every organism searched for the enzyme, including animals such as mammals and insects as well as in fungi, plants, and bacteria. However, some bacteria that do not perform glycolysis, like ureaplasmas, lack TPI. Applications: Triosephosphate isomerase has been used in a study to assess differential expression of fourteen proteins of uveal melanoma. triosephosphate isomerase has also been used in a study to investigate the use of sigmoid ph gradients in free-flow isoelectric f ocusing of human endothelial cell proteins. Group: Enzymes. Synonyms: Triose-. Enzyme Commission Number: EC 5.3.1.1. CAS No. 9023-78-3. TPI. Activity: ~10,000 units/mg protein. Storage: 2-8°C. Form: ammonium sulfate suspension; Crystalline suspension in 2.7 M (NH4)2SO4, 0.5 mM EDTA, pH 6.5. Source: Baker's yeast (S. cerevisiae). Triose-phosphate isomerase; phosphotriose isomerase; triose phosphoisomerase; triose phosphate mutase; D-glyceraldehyde-3-phosphate ketol-isomerase; TPI; TIM; EC 5.3.1.1; 9023-78-3. Cat No: NATE-0711. | |
| 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 Galactose-adapted yeast Galactose-1-phosphate Uridyltransferase | Galactose-1-phosphate uridyltransferase (GALT) facilitates the simultaneous conversion of uridine diphosphoglucose (UDP-glucose) and galactose-1-phosphate (gal-1P) to uridine diphosphogalactose (UDP-galactose) and glucose-1-phosphate. Classic Galactosemia (CG) is an inherited metabolic condition caused by deficiency of GALT activity. Group: Enzymes. Synonyms: EC 2.7.7.12; UDP-glucose-hexose-1-phosphate uridylyltransferase; uridyl transferase; hexose-1-phosphate uridylyltransferase; uridyltransferase; hexose 1-phosphate uridyltransferase; UDP-glucose:alpha-D-galactose-1-phosphate uridylyltransferase; 9016-11-9. Enzyme Commission Number: EC 2.7.7.12. CAS No. 9026-21-5. GALT. Activity: 20-60 units/mg protein (modified Warburg-Christian). Storage: -20°C. Form: lyophilized powder; Contains buffer salts as Citrate and reduced glutathione. Source: Galactose-adapted yeast. EC 2.7.7.12; UDP-glucose-hexose-1-phosphate uridylyltransferase; uridyl transferase; hexose-1-phosphate uridylyltransferase; uridyltransferase; hexose 1-phosphate uridyltransferase; UDP-glucose:alpha-D-galactose-1-phosphate uridylyltransferase; 9016-11-9. Cat No: NATE-0277. | |
| Native Galactose-adapted yeast Uridine-5'-diphosphogalactose 4-epimerase | The enzyme UDP-glucose 4-epimerase (EC 5.1.3.2), also known as UDP-galactose 4-epimerase or GALE, is a homodimeric epimerase found in bacterial, fungal, plant, and mammalian cells. This enzyme performs the final step in the Leloir pathway of galactose metabolism, catalyzing the reversible conversion of UDP-galactose to UDP-glucose. GALE tightly binds nicotinamide adenine dinucleotide (NAD+), a co-factor required for catalytic activity. Group: Enzymes. Synonyms: UDP-galactose 4-epimerase; uridine diphosphoglucose epimerase; galactowaldenase; UDPG-4-epimerase; uridine diphosphate galactose 4-epimerase; uridine diphospho-gal. Enzyme Commission Number: EC 5.1.3.2. CAS No. 9032-89-7. UDP-Glc 4-epimerase. Activity: 10-20 units/mg protein (modified Warburg-Christian). Storage: -20°C. Form: Lyophilized powder containing approx. 40% buffer salts. Source: Galactose-adapted yeast. UDP-galactose 4-epimerase; uridine diphosphoglucose epimerase; galactowaldenase; UDPG-4-epimerase; uridine diphosphate galactose 4-epimerase; uridine diphospho-galactose-4-epimerase; UDP-glucose epimerase; UDP-galactose 4-epimerase; 4-epimerase; UDPG-4-epimerase; uridine diphosphoglucose 4-epimerase; uridine diphosphate glucose 4-epimerase; UDP-D-galactose 4-epimerase; EC 5.1.3.2; UDP-glucose 4-epimerase; GALE. Pack: vial. Cat No: NATE-0275. | |
| Native Glutamate dehydrogenase (NADP+) from Yeast | Glutamate dehydrogenase (GLDH) is an enzyme, present in most microbes and the mitochondria of eukaryotes, as are some of the other enzymes required for urea synthesis, that converts glutamate to α-ketoglutarate, and vice versa. In animals, the produced ammonia is usually used as a substrate in the urea cycle. Typically, the α-ketoglutarate to glutamate reaction does not occur in mammals, as glutamate dehydrogenase equilibrium favours the production of ammonia and α-ketoglutarate. Group: Enzymes. Synonyms: glutamate dehydrogenase (NADP+); glutamic dehydrogenase; dehydrogenase; glutamate (nicotinamide adenine dinucleotide (phosphate)); glutamic acid dehydrogenase; L-glutamate dehydrogenase; L-glutamic acid dehydrogenase; NAD(P)-glutamate dehydrogenase; NAD(P)H-dependent glutamate dehydrogenase; glutamate d. Enzyme Commission Number: EC 1.4.1.4. CAS No. 9029-11-2. GLDH. Activity: > 10 U/mg protein. Storage: Below -20°C. Form: Lyophilized Powder. Source: Yeast. glutamate dehydrogenase (NADP+); glutamic dehydrogenase; dehydrogenase; glutamate (nicotinamide adenine dinucleotide (phosphate)); glutamic acid dehydrogenase; L-glutamate dehydrogenase; L-glutamic acid dehydrogenase; NAD(P)-glutamate dehydrogenase; NAD(P)H-dependent glutamate dehydrogenase; glutamate dehydrogenase (NADP); EC 1.4.1.4; GLDH. Cat No: NATE-1037. | |
| Native Myokinase from Yeast | Adenylate kinase (EC 2.7.4.3) (also known as ADK or myokinase) is a phosphotransferase enzyme that catalyzes the interconversion of adenine nucleotides, and plays an important role in cellular energy homeostasis. Group: Enzymes. Synonyms: Adenylate kinase; EC 2.7.4.3; ADK; myokinase; 9013-02-9; Adenylic kinase; Adenylokinase. Enzyme Commission Number: EC 2.7.4.3. CAS No. 9013-2-9. Myokinase. Activity: > 200 units/mg protein (at 25°C and pH 7.5). Storage: Below -20°C. Form: 50% Glycerol solution. Source: Yeast. Adenylate kinase; EC 2.7.4.3; ADK; myokinase; 9013-02-9; Adenylic kinase; Adenylokinase. Cat No: NATE-1039. | |
| Native Torula yeast Glucose-6-phosphate dehydrogenase | Glucose-6-phosphate dehydrogenase (G6PD or G6PDH) (EC 1.1.1.49) is a cytosolic enzyme that catalyzes the chemical reaction:D-glucose 6-phosphate + NADP+ <-> 6-phospho-D-glucono-1,5-lactone + NADPH + H+. This enzyme is in the pentose phosphate pathway, a metabolic pathway that supplies reducing energy to cells (such as erythrocytes) by maintaining the level of the co-enzyme nicotinamide adenine dinucleotide phosphate (NADPH). Group: Enzymes. Synonyms: EC 1.1.1.49; NADP-glucose-6-phosphate dehydrogenase; Zwischenferment; D-glucose 6-phosphate dehydrogenase; glucose 6-phosphate dehydrogenase (NADP); NADP-dependent glucose 6-phosphate dehydrogenase; 6-phosphoglucose dehydrogenase; Entner-Doudoroff enzyme; glucose-. Enzyme Commission Number: EC 1.1.1.49. CAS No. 9001-40-5. Glucose-6-phosphate dehydrogenase. Activity: 300-600 units/mg protein (biuret). Storage: 2-8°C. Form: ammonium sulfate suspension; Suspension in 2.6 M (NH4)2SO4 solution, pH 7.5. Source: Torula yeast. EC 1.1.1.49; NADP-glucose-6-phosphate dehydrogenase; Zwischenferment; D-glucose 6-phosphate dehydrogenase; glucose 6-phosphate dehydrogenase (NADP); NADP-dependent glucose 6-phosphate dehydrogenase; 6-phosphoglucose dehydrogenase; Entner-Doudoroff enzyme; glucose-6-phosphate 1-dehydrogenase; G6PDH; GPD; glucose-6-phosphate dehydrogenase; 9001-40-5. Cat No: DIA-322. | |
| Native Yeast 6-Phosphogluconic Dehydrogenase | In enzymology, a phosphogluconate dehydrogenase (decarboxylating) (EC 1.1.1.44) is an enzyme that catalyzes the chemical reaction:6-phospho-D-gluconate + NADP+<-> D-ribulose 5-phosphate + CO2 + NADPH. Thus, the two substRates of this enzyme are 6-phospho-D-gluconate and NADP+, whereas its 3 products are D-ribulose 5-phosphate, CO2, and NADPH. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. Applications: 6-phosphoglyconic dehydrogenase (6pgd) is a key enzyme in the oxidative portion of the hexose monophosphate shunt. it is specific for oxidized nicotinamide adenine dinucleotide ph...luconic carboxylase; 6-phosphogluconate dehydrogenase (decarboxylating); 6-phospho-D-gluconate dehydrogenase; EC 1.1.1.44; phosphogluconate dehydrogenase; decarboxylating; 9073-95-4. Enzyme Commission Number: EC 1.1.1.44. CAS No. 9073-95-4. 6-Phosphogluconic Dehydrogenase. Activity: 3.0-6.0 units/mg solid. Storage: 2-8°C. Form: lyophilized powder. Source: Yeast. 6-Phosphogluconic Dehydrogenase; phosphogluconic acid dehydrogenase; 6-phosphogluconic dehydrogenase; 6-phosphogluconic carboxylase; 6-phosphogluconate dehydrogenase (decarboxylating); 6-phospho-D-gluconate dehydrogenase; EC 1.1.1.44; phosphogluconate dehydrogenase; decarboxylating; 9073-95-4. Cat No: NATE-0009. | |
| Native Yeast Alcohol dehydrogenase | Alcohol dehydrogenases (ADH) are a group of dehydrogenase enzymes that occur in many organisms and facilitate the interconversion between alcohols and aldehydes or ketones with the reduction of nicotinamide adenine dinucleotide (NAD+ to NADH). In Humans and many other animals, they serve to break down alcohols that otherwise are toxic, and they also participate in geneRation of useful aldehyde, ketone, or alcohol groups during biosynthesis of various metabolites. In yeast, plants, and many bacteria, some alcohol dehydrogenases catalyze the opposite reaction as part of fermentation to ensure a constant supply of NAD+. Dehydrogenase that catalyzes the interconversion of alcoho...rimary alcohol dehydrogenase; yeast alcohol dehydrogenase. Enzyme Commission Number: EC 1.1.1.1. CAS No. 9031-72-5. Activity: >300 U/mg. Appearance: White lyophilizate (50 mg lyophilizate contain approximately 30 mg enzyme protein,15 mg sucrose, 5 mg phosphate). Storage: -20°C. Form: Solids containing <2% Citrate buffer salts. Source: Yeast. 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-0975. | |
| Native Yeast Aldehyde Dehydrogenase | In enzymology, an aldehyde dehydrogenase [NAD(P)+] (EC 1.2.1.5) is an enzyme that catalyzes the chemical reaction: an aldehyde + NAD(P)+ + H2O <-> an acid + NAD(P)H + H+. The 4 substrates of this enzyme are aldehyde, NAD+, NADP+, and H2O, whereas its 4 products are acid, NADH, NADPH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with NAD+ or NADP+ as acceptor. This enzyme participates in 5 metabolic pathways: glycolysis / gluconeogenesis, histidine metabolism, tyrosine metabolism, phenylalanine metabolism, and metabolism of xenobiotics by cytochrome p450. Applications: Component of nadh and nadph recycling systems. Group: Enzymes. Synonyms: aldehyde:NAD(P)+ oxidoreductase; aldehyde dehydrogenase [NAD(P)+]; ALDH; Aldehyde Dehydrogenase; EC 1.2.1.5. Enzyme Commission Number: EC 1.2.1.5. CAS No. 9028-88-0. ALDH. Activity: ~20 units/mg protein (At 25 °C with acetaldehyde as the substrate.). Form: Lyophilized. Source: Yeast. aldehyde:NAD(P)+ oxidoreductase; aldehyde dehydrogenase [NAD(P)+]; ALDH; Aldehyde Dehydrogenase; EC 1.2.1.5. Cat No: NATE-0902. | |
| 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. | |
| Native Yeast Formate Dehydrogenase | Formate dehydrogenase is involved in the stress response of plants and catalyzes the reduction of NAD+ to NADH. Dehydrogenase that catalyzes the interconversion of formate to carbon dioxide. rely on the proven diagnostic quality of this product. Applications: Use formate dehydrogenase in diagnostic tests for the determination of oxalate in combination with oxalate decarboxylase or for the determination of formic acid. also used in cofactor recycling systems for nadh. Group: Enzymes. Synonyms: 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. FDH. Activity: >0.4 U/mg. Stability: At +2 to +8°C within specification range for 12 months. Store dry. Appearance: White lyophilizate. Source: Yeast. 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-0978. | |
| Native Yeast Malate Dehydrogenase | Malate dehydrogenase is an enzyme in the citric acid cycle that catalyzes the conversion of malate into oxaloacetate (using NAD+) and vice versa (this is a reversible reaction). Malate dehydrogenase is not to be confused with malic enzyme, which catalyzes the conversion of malate to pyruvate producing NADPH. Malate dehydrogenase is also involved in gluconeogenesis, the synthesis of glucose from smaller molecules. Pyruvate in the mitochondria is acted upon by pyruvate carboxylase to form oxaloacetate, a citric acid cycle intermediate. In order to get the oxaloacetate out of the mitochondria, malate dehydrogenase reduces it to malate, and it then traverses the inner mitochondr...te: NAD+ oxidoreductase; EC 1.1.1.37; Malate Dehydrogenase. Enzyme Commission Number: EC 1.1.1.37. CAS No. 9001-64-3. MDH. Activity: > 1,000 units/mg protein (at 25°C and pH 7.5). Storage: 1 -10°C. Form: Ammonium sulfate suspension. Source: Yeast. malic dehydrogenase; L-malate dehydrogenase; NAD-L-malate dehydrogenase; malic acid dehydrogenase; NAD-dependent malic dehydrogenase; NAD-malate dehydrogenase; NAD-malic dehydrogenase; malate NAD dehydrogenase; NAD-dependent malate dehydrogenase; NAD-sp; ECific malate dehydrogenase; NAD-linked malate dehydrogenase; MDH; L-malate-NAD+ oxidoreductase; S-malate: NAD+ oxidoreductase; EC 1.1.1.37; Malate Dehydrogenase. Cat No: NATE-1030. | |
| Native Yeast Phytase | Phytase catalyzes the hydrolysis of phytic acid to inositol and free orthophosphate. Wheat phytase can degrade inositol phosphate-6 and 5 at a pH of 4 and 5. Group: Enzymes. Synonyms: myo-inositol-hexakisphosphate 4-phosphohydrolase; 9001-89-2; 6-phytase; phytase; phytate 6-phosphatase; myo-inositol-hexakisphosphate 6-phosphohydrolase; 4-phytase; EC 3.1.3.26. Enzyme Commission Number: EC 3.1.3.26. CAS No. 9001-89-2. Phytase. Activity: 5000 u/g. Storage: Store at -20°C. Form: Powder. Source: Yeast. myo-inositol-hexakisphosphate 4-phosphohydrolase; 9001-89-2; 6-phytase; phytase; phytate 6-phosphatase; myo-inositol-hexakisphosphate 6-phosphohydrolase; 4-phytase; EC 3.1.3.26. Cat No: NATE-0565. | |
| Phosphoglycerate kinase, yeast | Phosphoglycerate kinase, yeast (PGK), namely phosphoglycerate kinase, is a glycolytic enzyme commonly used in biochemical research. Phosphoglycerate kinase can catalyze the reversible transfer of phosphate groups from 1,3-bisphosphoglycerate (1,3-BPG) to ADP to generate 3-phosphoglycerate (3-PG) and ATP. At the same time, it can also participate in gluconeogenesis, catalyzing the opposite reaction to produce 1,3BPGA and ADP. Phosphoglycerate kinase is involved in energy metabolism, interaction with nucleic acid, tumor progression, cell death and virus replication and other related processes [1]. Uses: Scientific research. Group: Signaling pathways. Alternative Names: PGK. CAS No. 9001-83-6. Pack Sizes: 500 U; 1 KU. Product ID: HY-P2822. | |
| Protein hydrolyzates, yeast | Heterocyclic Organic Compound. CAS No. 100684-36-4. Catalog: ACM100684364. | |
| Protein hydrolyzates, yeast | Protein hydrolyzates, yeast is a hydrolyzed product of yeast cells, which is obtained by autolysis or hydrolysis with additional enzymes. Hydrolyzed yeast products contain a large number of amino acids, small peptides, rich B vitamins, glutathione and nucleotide substances. It is mainly used as an antioxidant in cosmetics and skin care products, controlling oil and resisting fat overflow. Synonyms: Hydrolyzed yeast protein; Proteins, yeast, hydrolysate; Yeast protein hydrolysate. Grades: 95%. CAS No. 100684-36-4. | |
| Red Rice Yeast Powder | Red Rice Yeast Powder. | CA, FL & NJ |
| Red yeast rice extract (Ratio) | Red yeast rice extract (Ratio). Group: Others. Purity: 4:1~20:1. Red yeast rice extract (Ratio). Cat No: EXTW-047. | |
| Ribonucleic Acid (Torula Yeast) | Ribonucleic acid (RNA) from torula yeast may be used as a substrate for studying ribonuclease activities of enzymes such as ribonuclease-A, ribonuclease T1 (RNAase) and bougainvillea xbuttiana antiviral protein 1 (BBAP1). Group: Biochemicals. Alternative Names: RNA free acid. Grades: Molecular Biology Grade. CAS No. 63231-63-0. Pack Sizes: 25g, 100g, 250g. US Biological Life Sciences. |  Worldwide |
| Ribonucleic acid (yeast) | Ribonucleic acid (yeast) is a biochemical reagent that can be used as a biological material or organic compound for life science related research. Uses: Scientific research. Group: Biochemical assay reagents. Alternative Names: RNA (yeast). CAS No. 63231-63-0. Pack Sizes: 100 mg. Product ID: HY-W250124. | |
| Selenium Yeast 0.2% Powder | Selenium Yeast 0.2% Powder . | CA, FL & NJ |
| SUMO Protease 1 (GST-tagged) from Yeast, Recombinant | SUMO (Small Ubiquitin-like MOdifiers) Protease 1 (Ulp1, Ubl-specific protease 1 from Saccharomyces cerevisiae) is a highly active cysteine protease. It is highly specific as it recognizes the tertiary structure of the ubiquitin-like (UBL) protein, SUMO (Smt3), rather than its amino acid sequence. SUMO fusion tag, as an N-terminal fusion partner, has been shown to enhance functional protein production in prokaryotic and eukaryotic expression systems with significantly improved protein stability and solubility. The SUMO protease 1 can be used to cleave SUMO protein tag from recombinant SUMO-fusion proteins. The optimal temperature for cleavage is 30°C; however, the en...eaction by affinity chromatography using the Glutathione resin. Group: Enzymes. Synonyms: Ulp1 peptidase; SUMO Protease; SUMO Protease. Enzyme Commission Number: EC 3.4.22.68. Purity: > 90% by SDS-PAGE. Mole weight: 52.6 kDa (403-621 aa + N-terminal GST). Activity: >10,000 units/mg. Storage: Store at -80°C. Stable for at least 1 year as supplied. It may be further diluted to 0.1-0.5 mg/ml with 50 mM Tris-HCl, 100 mM NaCl, 5 mM DTT and 20% glycerol pH 8.0 and stored at -20°C in aliquots. Avoid repeated freezing and thawing cycles. Form: Liquid. Source: E. coli. Species: Yeast. Ulp1 peptidase; SUMO Protease; SUMO Protease; SUMO Protease 1; Protease. Cat No: NATE-1708. | |
| SUMO Protease 1 (His-tagged) from Yeast, Recombinant | SUMO (Small Ubiquitin-like MOdifiers) Protease 1 (Ulp1, Ubl-specific protease 1 from Saccharomyces cerevisiae) is a highly active cysteine protease. It is highly specific as it recognizes the tertiary structure of the ubiquitin-like (UBL) protein, SUMO (Smt3), rather than its amino acid sequence. SUMO fusion tag, as an N-terminal fusion partner, has been shown to enhance functional protein production in prokaryotic and eukaryotic expression systems with significantly improved protein stability and solubility. The SUMO Protease 1 can be used to cleave SUMO protein tag from recombinant SUMO-fusion proteins. The optimal temperature for cleavage is 30°C; however, the en...finity chromatography using the Ni chelating resin. Group: Enzymes. Synonyms: Ulp1 peptidase; SUMO Protease; SUMO Protease. Enzyme Commission Number: EC 3.4.22.68. Purity: > 90% by SDS-PAGE. Mole weight: 28.7 kDa (403-621 aa + N-terminal Poly-His tag). Activity: 1 X 10^6 units/mg. Storage: Store at -80°C. Stable for at least 1 year as supplied. It may be further diluted to 0.01-0.05 mg/ml with 50 mM Tris-HCl, 100 mM NaCl, 5 mM DTT and 20% glycerol pH 8.0 and stored at -20°C in aliquots. Avoid repeated freezing and thawing cycles. Form: Liquid. Source: E. coli. Species: Yeast. Ulp1 peptidase; SUMO Protease; SUMO Protease; SUMO Protease 1; Protease. Cat No: NATE-1709. | |
| Thioredoxin Reductase (NADPH) from Yeast, Recombinant | Thioredoxin reductase (TrxR/NTR), an enzyme belonging to the flavoprotein family of pyridine nucleotide-disulfide oxidoreductases. Thioredoxin reductase (TrxR), a component of the thioredoxin system, including thioredoxin (Trx) and NADPH, catalyzes the transfer of electrons from NADPH to Trx, acts as a reductant of disulfide-containing proteins and participates in the defense system against oxidative stresses. Thioredoxin reductase (nadph) yeast recombinant produced in e. coli is a single, nonglycosylated, polypeptide chain having a molecular mass of 36 kda. thioredoxin reductase is purified by proprietary chromatographic techniques. Group: Enzymes. Synonyms: NADP-thioredoxin reductase; NADPH-thioredoxin reductase; thioredoxin reductase (NADPH); NADPH. CAS No. 9074-14-0. Purity: Greater than 98.0% as determined by (a) Analysis by RP-HPLC. (b) Analysis by SDS-PAGE. TrxR. Mole weight: 36 kDa. Activity: 5 IU/mg. Stability: NTR although stable at 4°C for 3 weeks, should be stored desiccated below -18°C. Please prevent freeze thaw cycles. Appearance: Sterile Filtered White lyophilized (freeze-dried) powder. Source: E. coli. Species: Yeast. NADP-thioredoxin reductase; NADPH-thioredoxin reductase; thioredoxin reductase (NADPH); NADPH2:oxidized thioredoxin oxidoreductase; thioredoxin-disulfide reductase; NTR; TrxR. Cat No: NATE-0917. | |
| Uridine-5'-monophosphate disodium (from yeast) 98+% | Uridine-5'-monophosphate disodium (from yeast) 98+%. Group: Biochemicals. Grades: Reagent Grade. Pack Sizes: 5g, 25g, 100g, 250g. US Biological Life Sciences. | Worldwide |
| 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 |
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