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| Product | Description | |
|---|---|---|
| 2-iminobutanoate/2-iminopropanoate deaminase | This enzyme, which has been found in all species and tissues examined, catalyses the hydrolytic deamination of imine intermediates formed by several types of pyridoxal-5'-phosphate-dependent dehydratases, such as EC 4.3.1.19, threonine ammonia-lyase and EC 4.3.1.17, L-serine ammonia-lyase. The reactions, which can occur spontaneously, are accelerated to minimize the cellular damage that could be caused by these reactive intermediates. Group: Enzymes. Synonyms: yjgF (gene name); ridA (gene name); enamine/imine deaminase (ambiguous). Enzyme Commission Number: EC 3.5.99.10. 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-4586; 2-iminobutanoate/2-iminopropanoate deaminase; EC 3.5.99.10; yjgF (gene name); ridA (gene name); enamine/imine deaminase (ambiguous). Cat No: EXWM-4586. |  |
| Aspartate Aminotransferase from Human, Recombinant | GOT1 is a pyridoxal phosphate-dependent enzyme which exists in cytoplasmic and mitochondrial forms, GOT1 and GOT2, which participate in amino acid metabolism and the urea and tricarboxylic acid cycles. Both enzymes are homodimeric and show close homology.GOT1 Human Recombinant E.coli produced in E.Coli is a single, non-glycosylated polypeptide chain containing 433 amino acids (1-413 a.a.) and having a molecular mass of 48.4 kDa. The GOT1 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques. Group: Enzymes. Synonyms: Aspartate transaminase; AST; aspartate aminotransferase; sgot AspAT; ASAT; AAT; serum glutamic oxaloac. Purity: Greater than 95.0% as determined by SDS-PAGE. AST. Activity: > 50 units/mg. Stability: Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles. Form: Sterile filtered colorless solution. Source: E.coli. Species: Human. Aspartate transaminase; AST; aspartate aminotransferase; sgot AspAT; ASAT; AAT; serum glutamic oxaloacetic transaminase; SGOT; pyridoxal phosphate PLP-dependent transaminase enzyme; EC 2.6.1.1; 9000-97-9; Aspartate aminotransferase 1; Transaminase A; GIG18. Cat No: DIA-128. | |
| L-Cycloserine | L-Cycloserine ((S)-4-Amino-3-isoxazolidone) irreversibly inhibits GABA pyridoxal 5'-phosphate-dependent aminitransferase in E. coli, as well in the brains of various animals in a time-dependent manner, results in increased levels of gamma-aminobutyric acid (GABA), which is an inhibitory neurotransmitter in vivo. Group: Inhibitors. Alternative Names: (l)-3-isoxazolidinon;(s)-3-isoxazolidinon;H-CYCLOSERINE;L-CYCLOSERINE;L-4-AMINO-3-ISOOXAZOLIDINONE;L-4-AMINO-3-ISOXALOLIDINONE;L-4-AMINO-3-ISOXAZOLIDINONE;S(-)-4-AMINO-3-ISOXAZOLIDINONE. CAS No. 339-72-0. Molecular formula: C3H6N2O2. Mole weight: 102.09. Appearance: Solid. Purity: 0.9941. Canonical SMILES: O=C1NOC[C@@H]1N. Density: 1.278. Catalog: ACM339720. |  |
| Native Aerococcuss viridans Pyruvate oxidase | In enzymology, a pyruvate oxidase (EC 1.2.3.3) is an enzyme that catalyzes the chemical reaction: pyruvate + phosphate + O2 <-> acetyl phosphate + CO2 + H2O2. The 3 substrates of this enzyme are pyruvate, phosphate, and O2, whereas its 3 products are acetyl phosphate, CO2, and H2O2. Native pyruvate oxidase (ec 1.2.3.3) was purified from aerococcuss viridans. Applications: Useful for enzymatic determination of ast and alt. Group: Enzymes. Synonyms: pyruvate oxidase; EC 1.2.3.3; pyruvate: oxygen 2-oxidoreductase (phosphorylating); pyruvic oxidase; phosphate-dependent pyruvate oxidase. Enzyme Commission Number: EC 1.2.3.3. CAS No. 9001-96-1. Pyruvate oxidase. Activity: > 25 U/mg. Appearance: Yellowish powder. Storage: Store in tightly closed containers, desiccated, protected from light, at-20°C. Form: Freeze dried powder. Source: Aerococcuss viridans. pyruvate oxidase; EC 1.2.3.3; pyruvate: oxygen 2-oxidoreductase (phosphorylating); pyruvic oxidase; phosphate-dependent pyruvate oxidase. Cat No: DIA-169. | |
| Native Human Aspartate Aminotransferase | Aspartate Aminotransferase (AST), also known as Glutamate Oxaloacetate Transaminase (GOT), is a pyridoxal phosphate-dependant enzyme which exists in two isoenzymes; mitochondrial and cytosolic forms. The AST enzyme plays an important role in amino acid metabolism and in the urea and tricarboxylic acid cycles. In liver about 80% of the enzyme activity is mitochondrial in origin, whereas in serum the enzyme activity is largely cytosolic. In hepatic disease, serum levels are used to assess liver necrosis and for determining prognosis. In patients with acute Myocardial infarction, measurement of AST isoenzymes provides diagnostic information that differs from that obtained by determination of other marker proteins. Creative Enzymes products are not intended for use in pharmaceutical applications. Applications: Research life science elisa assay clinical chemistry. Group: Enzymes. Synonyms: EC 2.6.1.1; glutamic-oxaloacetic transaminase; glutamic-aspartic transaminase; transaminase A; AAT; AspT; 2-oxoglutaRate-glutamate aminotransferase; aspartate α-ketoglutaRate transaminase; aspartate aminotransferase; aspartate-2-oxoglutaRate transaminase; aspartic acid aminotransferas. Enzyme Commission Number: EC 2.6.1.1. CAS No. 9000-97-9. AST. Activity: >50U/ml. Storage: -20°C. Source: Human Cardiac Tissue. Species: Human. EC 2.6.1.1; glutamic-oxaloa | |
| Native Microorganism Pyruvate oxidase | In enzymology, a pyruvate oxidase (EC 1.2.3.3) is an enzyme that catalyzes the chemical reaction: pyruvate + phosphate + O2 <-> acetyl phosphate + CO2 + H2O2. The 3 substrates of this enzyme are pyruvate, phosphate, and O2, whereas its 3 products are acetyl phosphate, CO2, and H2O2. This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with oxygen as acceptor. This enzyme participates in pyruvate metabolism. It has 2 cofactors: FAD, and Thiamin diphosphate. Applications: This enzyme is useful for enzymatic determination of pyruvate, got, gpt in clinical analysis. Group: Enzymes. Synonyms: EC 1.2.3.3; pyruvate: oxygen 2-oxidoreductase (phosphorylating); pyruvic oxidase; phosphate-dependent pyruvate oxidase. Enzyme Commission Number: EC 1.2.3.3. CAS No. 9001-96-1. Pyruvate oxidase. Mole weight: approx. 260 kDa. Activity: Grade? 1.5U/mg-solid or more. Stability: Stable at-20°C for at least one year. Appearance: Yellowish amorphous powder, lyophilized. Source: Microorganism. EC 1.2.3.3; pyruvate: oxygen 2-oxidoreductase (phosphorylating); pyruvic oxidase; phosphate-dependent pyruvate oxidase. Cat No: DIA-215. | |
| Native Microorganisms Pyruvate Oxidase | Pyruvate Oxidase consists of four subunits with identical molecular weights. PoxB reacts with certain aldehydes and phosphate can be replaced by arsenate. Oxygen as well as several artificial compounds can function as electron acceptors. Pyruvate Oxidase is activated by phospholipids as well as monomeric and micellar amphiphiles. Applications: Pyruvate oxidase (poxb) converts pyruvate directly to acetate and co2. it is used to study pyruvate metabolism. it is used to study aerobic metabolism of bacterium, such as lactobacillus plantarumand strept oc occus pneumoniae. pyruvate oxidase is used for enzymatic determination of pyruvate, got, and gpt in clinical analysis. Group: Enzymes. Synonyms: pyruvate oxidase; EC 1.2.3.3; pyruvic oxidase; phosphate-dependent pyruvate oxidase; 9001-96-1; Pyruvate:oxygen oxidoreductase (phosphorylating); PoxB. Enzyme Commission Number: EC 1.2.3.3. CAS No. 9001-96-1. Pyruvate oxidase. Mole weight: mol wt ~260 kDa. Activity: > 1.5 units/mg; > 35 units/mg protein (biuret). Storage: -20°C. Form: Lyophilized powder containing FAD and sugar as stabilizer. Source: Microorganisms. pyruvate oxidase; EC 1.2.3.3; pyruvic oxidase; phosphate-dependent pyruvate oxidase; 9001-96-1; Pyruvate:oxygen oxidoreductase (phosphorylating); PoxB. Cat No: NATE-0613. | |
| Pyridoxal-5'-phosphate monohydrate | Pyridoxal-5'-phosphate monohydrate is a vitamin B6 metabolite that can modify lysyl and valyl residues in proteins. It has the ability to inhibit purinergic receptors and intracellular influx of Ca2+. Pyridoxal-5'-phosphate monohydrate can modify peptides and suppress their precursor ionization efficiency. Research shows that pyridoxal-5'-phosphate-dependent enzymes can be inhibited by cycloserine. Applications: A vitamin b6 metabolite that can modify lysyl and valyl residues in proteins. Group: Coenzymes. Synonyms: Codecarboxylase. CAS No. 41468-25-1. Purity: ≥97%. Mole weight: 265.2. Appearance: Powder. Form: Solid. Codecarboxylase; Pyridoxal-5'-phosphate monohydrate; 41468-25-1. Cat No: COEC-044. | |
| pyruvate oxidase | A flavoprotein (FAD) requiring thiamine diphosphate. Two reducing equivalents are transferred from the resonant carbanion/enamine forms of 2-hydroxyethyl-thiamine-diphosphate to the adjacent flavin cofactor, yielding 2-acetyl-thiamine diphosphate (AcThDP) and reduced flavin. FADH2 is reoxidized by O2 to yield H2O2 and FAD and AcThDP is cleaved phosphorolytically to acetyl phosphate and thiamine diphosphate. Group: Enzymes. Synonyms: pyruvic oxidase; phosphate-dependent pyruvate oxidase. Enzyme Commission Number: EC 1.2.3.3. CAS No. 9001-96-1. Pyruvate oxidase. 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-1210; pyruvate oxidase; EC 1.2.3.3; 9001-96-1; pyruvic oxidase; phosphate-dependent pyruvate oxidase. Cat No: EXWM-1210. | |
| Pyruvate Oxidase from E.coli, Recombinant | Recombinant oxidoreductase that catalyzes the interconversion of pyruvate to acetyl phosphate. Rely in the proven diagnostic quality of this product. Applications: Use pyruvate oxidase in a variety of diagnostic tests, such as for the determination of pyruvate, lactate or aminotransferases. Group: Enzymes. Synonyms: pyruvic oxidase; phosphate-dependent pyruvate oxidase; Pyruvate:oxygen oxidoreductase (phosphorylating); PoxB. CAS No. 9001-96-1. Pyruvate oxidase. Activity: >1.5 U/mg lyophilizate; >3 U/mg protein. Stability: At -15 to -25°C within specification range for 12 months. Store dry. Appearance: Yellow lyophilizate. Source: E. coli. pyruvate oxidase; EC 1.2.3.3; pyruvic oxidase; phosphate-dependent pyruvate oxidase; 9001-96-1; Pyruvate:oxygen oxidoreductase (phosphorylating); PoxB. Cat No: DIA-289. | |
| tRNA nucleotidyltransferase | Brings about the final exonucleolytic trimming of the 3'-terminus of tRNA precursors in Escherichia coli by a phosphorolysis, producing a mature 3'-terminus on tRNA and nucleoside diphosphate. Not identical with EC 2.7.7.8 polyribonucleotide nucleotidyltransferase. Group: Enzymes. Synonyms: phosphate-dependent exonuclease; RNase PH; ribonuclease PH. Enzyme Commission Number: EC 2.7.7.56. CAS No. 116412-36-3. 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-3267; tRNA nucleotidyltransferase; EC 2.7.7.56; 116412-36-3; phosphate-dependent exonuclease; RNase PH; ribonuclease PH. Cat No: EXWM-3267. | |
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