Find where to buy products from suppliers in the USA, including: distributors, industrial manufacturers in America, bulk supplies and wholesalers of raw ingredients & finished goods.
Search for products or services, then visit the American suppliers website for prices, SDS or more information. You can also view suppliers in Australia, NZ or the UK.
| Product | Description | |
|---|---|---|
| Esterase Isoenzyme 1 from Porcine liver, Recombinant | An esterase is a hydrolase that splits esters into acids and alcohols. Applications: Esterase isoenzymes may be used to identify the mon ocytic element in normal and leukemic cells. they may be used for the bi ochemical characterization of different hematopoietic cell lineages and stages of differentiation when studying leukemias and lymphomas. esterase isoenzyme is recombinant and from porcine liver. it is expressed in e. coli. Group: Enzymes. Synonyms: EC 3.1.1.1; Esterase Isoenzyme 1; 9016-18-6; carboxylesterase; ali-esterase; B-esterase; monobutyrase; cocaine esteras. Enzyme Commission Number: EC 3.1.1.1. CAS No. 9016-18-6. Esterase. Activity: > 30.0 U/g. Storage: -20°C. Source: E. coli. Species: Porcine liver. EC 3.1.1.1; Esterase Isoenzyme 1; 9016-18-6; carboxylesterase; ali-esterase; B-esterase; monobutyrase; cocaine esterase; procaine esterase; methylbutyrase; vitamin A esterase; butyryl esterase; carboxyesterase; carboxylate esterase; carboxylic esterase; methylbutyrate esterase; triacetin esterase; carboxyl ester hydrolase; butyrate esterase; methylbutyrase; α-carboxylesterase; propionyl esterase; nonspecific carboxylesterase; esterase D; esterase B; esterase A; serine esterase; carboxylic acid esterase; cocaine esterase. Pack: Bottomless glass bottle. Contents are inside inserted fused cone. Cat No: NATE-0229. |  |
| Esterase Isoenzyme 2 from Porcine liver, Recombinant | An esterase is a hydrolase that splits esters into acids and alcohols. Applications: Esterase isoenzymes may be used to identify the mon ocytic element in normal and leukemic cells. they may be used for the bi ochemical characterization of different hematopoietic cell lineages and stages of differentiation when studying leukemias and lymphomas. esterase isoenzyme 2, is from porcine liver and is recombinant and expressed in e. coli. Group: Enzymes. Synonyms: EC 3.1.1.1; Esterase Isoenzyme 2; 9016-18-6; carboxylesterase; ali-esterase; B-esterase; monobutyrase; cocaine estera. Enzyme Commission Number: EC 3.1.1.1. CAS No. 9016-18-6. Esterase. Activity: > 80 U/g. Storage: -20°C. Source: E. coli. Species: Porcine liver. EC 3.1.1.1; Esterase Isoenzyme 2; 9016-18-6; carboxylesterase; ali-esterase; B-esterase; monobutyrase; cocaine esterase; procaine esterase; methylbutyrase; vitamin A esterase; butyryl esterase; carboxyesterase; carboxylate esterase; carboxylic esterase; methylbutyrate esterase; triacetin esterase; carboxyl ester hydrolase; butyrate esterase; methylbutyrase; α-carboxylesterase; propionyl esterase; nonspecific carboxylesterase; esterase D; esterase B; esterase A; serine esterase; carboxylic acid esterase; cocaine esterase. Pack: Bottomless glass bottle. Contents are inside inserted fused cone. Cat No: NATE-0230. | |
| Esterase Isoenzyme 3 from Porcine liver, Recombinant | An esterase is a hydrolase that splits esters into acids and alcohols. Applications: Esterase isoenzymes may be used to identify the mon ocytic element in normal and leukemic cells. they may be used for the biochemical characterization of different hematopoietic cell lineages and stages of differentiation when studying leukemias and lymphomas. Group: Enzymes. Synonyms: EC 3.1.1.1; ali-esterase; B-esterase; monobutyrase; cocaine esterase; procaine esterase; methylbutyrase; vitamin A esterase; butyryl esterase; carboxyesterase; carboxylate esterase; carboxylic esterase. Enzyme Commission Number: EC 3.1.1.1. CAS No. 9016-18-6. Esterase. Activity: > 0.8 units/mg. Storage: -20°C. Source: E. coli. Species: Porcine liver. EC 3.1.1.1; Esterase Isoenzyme 3; 9016-18-6; carboxylesterase; ali-esterase; B-esterase; monobutyrase; cocaine esterase; procaine esterase; methylbutyrase; vitamin A esterase; butyryl esterase; carboxyesterase; carboxylate esterase; carboxylic esterase; methylbutyrate esterase; triacetin esterase; carboxyl ester hydrolase; butyrate esterase; methylbutyrase; α-carboxylesterase; propionyl esterase; nonspecific carboxylesterase; esterase D; esterase B; esterase A; serine esterase; carboxylic acid esterase; cocaine esterase. Pack: Bottomless glass bottle. Contents are inside inserted fused cone. Cat No: NATE-0231. | |
| Esterase Isoenzyme 5 from Porcine liver, Recombinant | An esterase is a hydrolase that splits esters into acids and alcohols. Applications: Esterase isoenzymes may be used to identify the mon ocytic element in normal and leukemic cells. they may be used for the bi ochemical characterization of different hematopoietic cell lineages and stages of differentiation when studying leukemias and lymphomas. esterase isoenzyme 5 is recombinant and from porcine liver. it is expressed in e. coli. Group: Enzymes. Synonyms: EC 3.1.1.1; Esterase Isoenzyme 5; 9016-18-6; carboxylesterase; ali-esterase; B-esterase; monobutyrase; cocaine e. Enzyme Commission Number: EC 3.1.1.1. CAS No. 9016-18-6. Esterase. Activity: > 0.5 units/mg. Storage: -20°C. Source: E. coli. Species: Porcine liver. EC 3.1.1.1; Esterase Isoenzyme 5; 9016-18-6; carboxylesterase; ali-esterase; B-esterase; monobutyrase; cocaine esterase; procaine esterase; methylbutyrase; vitamin A esterase; butyryl esterase; carboxyesterase; carboxylate esterase; carboxylic esterase; methylbutyrate esterase; triacetin esterase; carboxyl ester hydrolase; butyrate esterase; methylbutyrase; α-carboxylesterase; propionyl esterase; nonspecific carboxylesterase; esterase D; esterase B; esterase A; serine esterase; carboxylic acid esterase; cocaine esterase. Pack: Bottomless glass bottle. Contents are inside inserted fused cone. Cat No: NATE-0232. | |
| Esterase Isoenzyme 6 from Porcine liver, Recombinant | An esterase is a hydrolase that splits esters into acids and alcohols. Applications: Esterase isoenzymes may be used to identify the mon ocytic element in normal and leukemic cells. they may be used for the bi ochemical characterization of different hematopoietic cell lineages and stages of differentiation when studying leukemias and lymphomas. esterase isoenzyme 6 is recombinant and from porcine liver. it is expressed in e. coli. Group: Enzymes. Synonyms: EC 3.1.1.1; Esterase Isoenzyme 6; 9016-18-6; carboxylesterase; ali-esterase; B-esterase; monobutyrase; cocaine e. Enzyme Commission Number: EC 3.1.1.1. CAS No. 9016-18-6. Esterase. Activity: > 1.2 units/mg. Storage: -20°C. Source: E. coli. Species: Porcine liver. EC 3.1.1.1; Esterase Isoenzyme 6; 9016-18-6; carboxylesterase; ali-esterase; B-esterase; monobutyrase; cocaine esterase; procaine esterase; methylbutyrase; vitamin A esterase; butyryl esterase; carboxyesterase; carboxylate esterase; carboxylic esterase; methylbutyrate esterase; triacetin esterase; carboxyl ester hydrolase; butyrate esterase; methylbutyrase; α-carboxylesterase; propionyl esterase; nonspecific carboxylesterase; esterase D; esterase B; esterase A; serine esterase; carboxylic acid esterase; cocaine esterase. Pack: Bottomless glass bottle. Contents are inside inserted fused cone. Cat No: NATE-0233. | |
| 2',3'-cyclic-nucleotide 3'-phosphodiesterase | The brain enzyme acts on 2',3'-cyclic AMP more rapidly than on the UMP or CMP derivatives. An enzyme from liver acts on 2',3'-cyclic CMP more rapidly than on the purine derivatives; it also hydrolyses the corresponding 3',5'-cyclic phosphates, but more slowly. This latter enzyme has been called cyclic-CMP phosphodiesterase. Group: Enzymes. Synonyms: cyclic-CMP phosphodiesterase; 2',3'-cyclic AMP phosphodiesterase; cyclic 2',3'-nucleotide 3'-phosphodiesterase; cyclic 2',3'-nucleotide phosphodiesterase; 2',3'-cyclic nucleoside monophosphate phosphodiesterase; 2',3'-cyclic nucleotide 3'-phosphohydrolase; CNPase; 2',3'-cyclic nucleotide phosphohydrolase; 2':3'-cyclic nucleotide 3'-phosphod. Enzyme Commission Number: EC 3.1.4.37. CAS No. 60098-35-3. 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-3720; 2',3'-cyclic-nucleotide 3'-phosphodiesterase; EC 3.1.4.37; 60098-35-3; cyclic-CMP phosphodiesterase; 2',3'-cyclic AMP phosphodiesterase; cyclic 2',3'-nucleotide 3'-phosphodiesterase; cyclic 2',3'-nucleotide phosphodiesterase; 2',3'-cyclic nucleoside monophosphate phosphodiesterase; 2',3'-cyclic nucleotide 3'-phosphohydrolase; CNPase; 2',3'-cyclic nucleotide phosphohydrolase; 2':3'-cyclic nucleotide 3'-phosphodiesterase; 2':3'-CNMP-3'-ase. Cat No: EXWM-3720. | |
| 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. | |
| 4-hydroxy-2-oxoglutarate aldolase | The enzymes from rat liver and bovine liver act on both enantiomers of 4-hydroxy-2-oxoglutarate. cf. EC 4.1.3.42, L-4-hydroxy-2-oxoglutarate aldolase. Group: Enzymes. Synonyms: 2-oxo-4-hydroxyglutarate aldolase; hydroxyketoglutaric aldolase; 4-hydroxy-2-ketoglutaric aldolase; 2-keto-4-hydroxyglutaric aldolase; 4-hydroxy-2-ketoglutarate aldolase; 2-keto-4-hydroxyglutarate aldolase; 2-oxo-4-hydroxyglutaric aldolase; DL-4-hydroxy-2-ketoglutarate aldolase; hydroxyketoglutarate aldolase; 2-keto-4-hydroxybutyrate aldolase; 4-hydroxy-2-oxoglutarate glyoxylate-lyase; KHGA. Enzyme Commission Number: EC 4.1.3.16. CAS No. 9030-81-3. 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-4901; 4-hydroxy-2-oxoglutarate aldolase; EC 4.1.3.16; 9030-81-3; 2-oxo-4-hydroxyglutarate aldolase; hydroxyketoglutaric aldolase; 4-hydroxy-2-ketoglutaric aldolase; 2-keto-4-hydroxyglutaric aldolase; 4-hydroxy-2-ketoglutarate aldolase; 2-keto-4-hydroxyglutarate aldolase; 2-oxo-4-hydroxyglutaric aldolase; DL-4-hydroxy-2-ketoglutarate aldolase; hydroxyketoglutarate aldolase; 2-keto-4-hydroxybutyrate aldolase; 4-hydroxy-2-oxoglutarate glyoxylate-lyase; KHGA. Cat No: EXWM-4901. | |
| 6-pyruvoyltetrahydropterin synthase | Catalyses triphosphate elimination and an intramolecular redox reaction in the presence of Mg2+. It has been identified in human liver. This enzyme is involved in the de novo synthesis of tetrahydrobiopterin from GTP, with the other enzymes involved being EC 1.1.1.153 (sepiapterin reductase) and EC 3.5.4.16 (GTP cyclohydrolase I). Group: Enzymes. Synonyms: 2-amino-4-oxo-6-[(1S,2R)-1,2-dihydroxy-3-triphosphooxypropyl]-7,8-dihydroxypteridine triphosphate lyase; 6-[(1S,2R)-1,2-dihydroxy-3-triphosphooxypropyl]-7,8-dihydropterin triphosphate-lyase (6-pyruvoyl-5,6,7,8-tetrahydropterin-forming). Enzyme Commission Number: EC 4.2.3.12. CAS No. 97089-82-2. 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-5132; 6-pyruvoyltetrahydropterin synthase; EC 4.2.3.12; 97089-82-2; 2-amino-4-oxo-6-[(1S,2R)-1,2-dihydroxy-3-triphosphooxypropyl]-7,8-dihydroxypteridine triphosphate lyase; 6-[(1S,2R)-1,2-dihydroxy-3-triphosphooxypropyl]-7,8-dihydropterin triphosphate-lyase (6-pyruvoyl-5,6,7,8-tetrahydropterin-forming). Cat No: EXWM-5132. | |
| Acaterin | Acarbose is an acyl-CoA isolated from Pseudomonas species. A92. In the presence of oxidized low-density lipoprotein in macrophages J744, the synthesis of cholesterol enzymes is inhibited, with an IC50 of 45 μmol/L, and the IC50 for inhibiting ACAT in rat liver microsomes is 120 μmol/L. Inhibition of ACAT is non-competitive Sexual. Synonyms: (2R)-4-[(1R)-1-hydroxyoctyl]-2-methyl-2H-furan-5-one; 3-(1-Hydroxyoctyl)-5-methyl-2(5H)-furanone. Grades: >98%. CAS No. 144398-20-9. Molecular formula: C13H22O3. Mole weight: 226.31. |  |
| Aldehyde Dehydrogenase 2 from Human, Recombinant | ALDH2 is part of the aldehyde dehydrogenase family of proteins which catalyze the chemical transformation from acetaldehyde to acetic acid. ALDH2 is the second enzyme of the major oxidative pathway of alcohol metabolism. ALDH2 has 2 major liver isoforms: cytosolic and mitochondrial, which differ by their electrophoretic mobilities, kinetic properties, and subcellular localizations. Nearly all Caucasians have 2 major isozymes, whereas roughly 50% of Orientals have only the cytosolic isozyme, omitting the mitochondrial isozyme. The extremely higher rate of acute alcohol intoxication with Orientals compared to Caucasians is due to the fact of the absence of mitochondrial... & having a molecular mass of 54.5 kda. the aldh2 is purified by proprietary chromatographic techniques. Group: Enzymes. Synonyms: ALDM; ALDHI; ALDH-E2; MGC1806; ALDH2; Aldehyde dehydrogenase mitochondrial; ALDH class 2. Purity: Greater than 90.0% as determined by SDS-PAGE. ALDH2. Mole weight: 54.5 kDa. Activity: > 0.14 units/ml. Stability: Store vial at -20°C to -80°C. When stored at the recommended temperature, this protein is stable for 12 months. Please prevent freeze-thaw cycles. Appearance: Sterile Filtered clear solution. Source: E. coli. Species: Human. ALDM; ALDHI; ALDH-E2; MGC1806; ALDH2; Aldehyde dehydrogenase mitochondrial; ALDH class 2. Cat No: NATE-0804. | |
| aldehyde oxidase | Contains molybdenum, [2Fe-2S] centres and FAD. The enzyme from liver exhibits a broad substrate specificity, and is involved in the metabolism of xenobiotics, including the oxidation of N-heterocycles and aldehydes and the reduction of N-oxides, nitrosamines, hydroxamic acids, azo dyes, nitropolycyclic aromatic hydrocarbons, and sulfoxides.The enzyme is also responsible for the oxidation of retinal, an activity that was initially attributed to a distinct enzyme (EC 1.2.3.11, retinal oxidase). Group: Enzymes. Synonyms: quinoline oxidase; retinal oxidase. Enzyme Commission Number: EC 1.2.3.1. CAS No. 9029-7-6. 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-1206; aldehyde oxidase; EC 1.2.3.1; 9029-07-6; quinoline oxidase; retinal oxidase. Cat No: EXWM-1206. | |
| Alizarin | Alizarin is a natural dye. Alizarin can be extracted from the roots of madder plant. Alizarin activates AMPK and VEGFR2/eNOS pathway. Alizarin regulates PI3K/Akt and inhibits NF-κB pathway. Alizarin enhances CYP1A1 enzyme activity. Alizarin has protective effects on hypertension and vascular endothelial dysfunction. Alizarin has anti-tumor activity against multiple cancers including pancreatic cancer, breast cancer, osteosarcoma and liver cancer. Alizarin has been widely used as a pigment in textile fabrics and paintings [1] [2] [3] [4] [5] [6] [7]. Uses: Scientific research. Group: Natural products. CAS No. 72-48-0. Pack Sizes: 10 mM * 1 mL; 500 mg; 1 g; 5 g. Product ID: HY-N0563. |  |
| Aspartate Transaminase (Crude Enzyme) | (AST) or aspartate aminotransferase, also known as AspAT/ASAT/AAT or serum glutamic oxaloacetic transaminase(SGOT), is a pyridoxal phosphate (PLP)-dependent transaminase enzyme (EC 2. 6. 1. 1) that was first described by Arthur Karmen and colleagues in 1954. AST catalyzes the reversible transfer of an α-amino group between aspartate and glutamate and, as such, is an important enzyme in amino acid metabolism. AST is found in the liver, heart, skeletal muscle, kidneys, brain, and red blood cells. Serum AST level, serum ALT (alanine transaminase) level, and their ratio (AST/ALT ratio) are commonly measured clinically as biomarkers for liver health. The tests are part of blood panels. This product with the indicated enzyme activity was briefly purified from engineered E. coli. Applications: Synthesis; medicine; biotechnology. Group: Enzymes. Synonyms: 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 a. Enzyme Commission Number: EC 2.6.1.1. CAS No. 9000-97-9. AST. Activity: Undetermined. Appearance: Clear to translucent yellow solution. Storage: at -20 °C or lower, for at least 1 month. Source: E. coli. glutamic-oxaloacetic transamina | |
| β-D-fucosidase | Enzymes from some sources also hydrolyse β-D-galactosides and/or β-D-glucosides and/or α-L-arabinosides. The activity of EC 3.2.1.37 xylan 1,4-β-xylosidase, is an associated activity found in some sources (e.g. liver). Group: Enzymes. Synonyms: β-fucosidase. Enzyme Commission Number: EC 3.2.1.38. CAS No. 9025-34-7. 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-3900; β-D-fucosidase; EC 3.2.1.38; 9025-34-7; β-fucosidase. Cat No: EXWM-3900. | |
| Bifendate | Bifendate is a synthetic intermediate of schisandrin C, a dibenzocyclooctadiene derivative derived from lignans used in traditional medicine and also a anti-HBV drug used in the treatment of chronic hepatitis B. It has been used in some countries as a hepatoprotectant adjuvant in the treatment of liver diseases, such as chronic viral hepatitis or drug-induced hepatic damage. Uses: Cytochrome p-450 enzyme inhibitors. Synonyms: 7,7'-Dimethoxy-[4,4'-Bi-1,3-benzodioxole]-5,5'-dicarboxylic Acid 5,5'-Dimethyl Ester; DDB; Dimethyl 4,4'-Dimethoxy-5,6,5',6'-di(methylenedioxy)biphenyl-2,2'-dicarboxylate; Dimethyl dicarboxylate Biphenyl; α-DDB. Grades: 97.0%~103.0%. CAS No. 73536-69-3. Molecular formula: C20H18O10. Mole weight: 418.36. | |
| Bovine Catalase-polyethylene glycol | PEG labeled catalase is one of PEGylated catalase conjugates. Catalase is a common enzyme found in nearly all living organisms exposed to oxygen. It catalyzes the decomposition of hydrogen peroxide to water and oxygen. Catalase is an important enzyme in protecting the cell from oxidative damage by reactive oxygen species. PEG modified catalase shows better stability with good reactivity. We provide a variety of chemically functionalized and bio-conjugated catalase with different functionality. These functionalized catalase conjugates were purified by size exclusion chromatography to ensure adequate applications both in-vitro and in-vivo. Group: Enzymes. Synonyms: PEG-Catalase; Catalase-polyethylene glycol; CAT-PEG. CAS No. 9001-5-2. CAT. Mole weight: ~250 KDa. Activity: 2000-5000 units/mg before conjugation; 20~50 PEG5000 on each catalase molecule. Storage: Store at -20°C. Form: Lyophilized powder. Source: Bovine liver. Species: Bovine. PEG-Catalase; Catalase-polyethylene glycol; CAT-PEG. Pack: Package size based on protein content. Cat No: NATE-0111. | |
| CATALASE | CATALASE. Synonyms: equilase;Catalase-Agarose;H2O2 oxidoreductase;Catalase from A. niger, lyophil.;Catalase from bovine liver, lyophil.;Catalase-peroxidase;CATALASE FROM BOVINE LIVERCA.65000 U/MG PROTEIN SUSPENSION;CATALASE FROM ASPERGILLUSNIGER CA.2000 U/MG LYOPH.SALT-FREE. CAS No. 9001-5-2. Pack Sizes: 1 kg. Product ID: CDF4-0037. Molecular formula: C9H10O3. Category: Enzyme Preparations. Product Keywords: Food Ingredients; Enzyme Preparations; CATALASE; CDF4-0037; 9001-05-2; C9H10O3; 232-577-1; 9001-05-2. Purity: 0.99. Color: Deep Brown. EC Number: 232-577-1. Physical State: Suspension. Storage: -20°C. Product Description: CAT (catalase) is an endogenous antioxidant enzyme, thus conferring protection to cells against damage by ROS (reactive oxygen species). In humans, this gene is localized to chromosome 11p13, which is composed of 12 introns and 13 exons. |  |
| Catalase from bovine liver | Catalase from bovine liver. Synonyms: H2O2:H2O2 oxidoreductase. CAS No. 9001-5-2. Product ID: CDC10-0039. Category: Antioxidant Cosmetic Chemicals. Product Keywords: Cosmetic Ingredients; Antioxidant Cosmetic Chemicals; Catalase from bovine liver; CDC10-0039; 9001-05-2; H2O2:H2O2 oxidoreductase; MFCD00081483; 9001-05-2. Physical State: aqueous suspension. Quality Level: 200. Storage: 2-8°C. Application: Catalase from bovine liver has been used for measuring the hydrogen peroxide conetent in cancer tissue homogenates. It has also been used to test the effect of organophosphate insecticide chlorpyrifos-ethyl (CE) [0,0-diethyl 0 (3,5,6-trichloro-2-pyridyl) phosphorothioate] on its enzyme activity. Density: 1.06 g/mL at 20 °C. Product Description: Catalase from bovine liver contains 506 residues. It is a tetramer and each monomer corresponds to a molecular weight of 61 kDa. The active site in each momomer comprises nicotinamide adenine dinucleotide phosphate (NADPH) and iron binding region. | |
| CAY10594 | Phospholipase D (PLD) is an enzyme which cleaves the head group from phospholipids, producing the second messenger phosphatidic acid. There are two mammalian isoforms of PLD, which are PLD1 and PLD2. CAY10594 is a potent phospholipase D2 inhibitor (PLD2), which also prevents the invasive migration of breast cancer cells. It ameliorates acetaminophen-induced acute liver injury by regulating the phosphorylated-GSK-3β/JNK axis. Synonyms: CAY 10594; CAY-10594. Grades: ≥98%. CAS No. 1130067-34-3. Molecular formula: C26H28N4O2. Mole weight: 428.5. | |
| Cepharanthine | Cepharanthine is a natural product that can be isolated from the plant Stephania?cephalantha?Hayata. Cepharanthine has anti-severe acute respiratory syndrome coronavirus 2 (anti-SARS-CoV-2) activities. Cepharanthine has good effective in suppressing viral proliferation (half maximal (50%) inhibitory concentration ( IC 50 ) and 90% inhibitory concentration ( IC 90 ) values of 1.90 and 4.46?μM [1]. Cepharanthine can also effectively reverses P-gp-mediated multidrug resistance in K562 cells and increase enhances the sensitivity of anticancer agents in xenograft mice model [2] [3]. Cepharanthine shows inhibitory effects of human liver cytochrome P450 enzymes CYP3A4, CYP2E1 and CYP2C9. Cepharanthine has antitumor, anti-inflammatory and antinociceptive effects [4] [5] [6] [7] [8]. Uses: Scientific research. Group: Natural products. CAS No. 481-49-2. Pack Sizes: 10 mM * 1 mL; 50 mg. Product ID: HY-N6972. | |
| Chlorotrianisene | Chlorotrianisene is a powerful synthetic, non-steroidal estrogenic compound which is metabolized by liver microsomal enzymes primarily to the mono-O-demethylated derivative. It binds to the estrogen receptor on various estrogen receptor bearing cells. It was used for the treatment of menopause, deficiencies in ovary function, and prostate cancer. It belongs triphenylethylene group. It was derived from estrobin (DBE) and is a relatively weak estrogen. It is a selective estrogen receptor modulator (SERM), with predominantly estrogenic but also antiestrogenic effects, and was arguably the first SERM to ever be introduced. It has been listed. Uses: Chlorotrianisene was used for the treatment of menopause, deficiencies in ovary function, and prostate cancer. Synonyms: 1, 1', 1''-(1-Chloro-1-ethenyl-2-ylidene)-tris(4-methoxybenzene); 1-[2-Chloro-1, 2-bis(4-methoxyphenyl)vinyl]-4-methoxybenzene; Chlortrianisestrol; Chlortrianizen; Khlortrianizen; Hormonisene; Anisene; Metace; Rianil; Tace; 1-[1-Chloro-2, 2-bis(4-methoxyphenyl)ethenyl]; Chlorotrianisene; Chlortrianisestrol; Chlortrianizen; Chlorotrianisine; Chlorestrolo; Chlorotrianizen; Khlortrianizen; Clorestrolo; Clorotrisin; Hormonisene; Anisene; Metace; Rianil; Tace. Grades: 95%. CAS No. 569-57-3. Molecular formula: C23H21ClO3. Mole weight: 380.87. | |
| Collagenase AF-1 GMP Grade | Collagenase AF-1 GMP Grade, often in combination with Neutral Protease AF GMP Grade, is suitable for the dissociation of sensitive cells from several tissues, such as pancreas, liver and dental pulp. It has been shown to be highly effective for the isolation of islets of Langerhans from human pancreas intended for transplantation. Applications: Collagenase af-1 gmp grade is suitable for cell isolation from several tissue types intended for clinical applications. it is often used in combination with neutral protease af gmp grade. Group: Enzymes. Synonyms: Collagenase AF-1; Collagenase; Collagenase AF-1 GMP; Collagenase GMP. Enzyme Commission Number: EC 3.4.24.3. CAS No. 9001-12-1. Collagenase. Activity: ≥ 3.00 U/mg. Storage: 2 to 8 °C. Form: Lyophilized powder. Source: Clostridium histolyticum. Collagenase AF-1; Collagenase; Collagenase AF-1 GMP; Collagenase GMP. Cat No: NATE-1919. | |
| Creatine monohydrate | Creatine is a nitrogenous compound that acts as a high-energy reservoir for the rapid regeneration of ATP. Approximately 95% of creatine is found in skeletal muscle, primarily as phosphocreatine. Creatine can be acquired through dietary consumption or formed from L-arginine, glycine, and L-methionine in a multi-step reaction that occurs in the kidneys and liver. Creatine is then transported to muscle tissue. Creatine is also being investigated as a treatment of neuromuscular diseases, where it may aid in neuroprotection and by improving the cellular bioenergetic state. Applications: Involved with rapid atp production primarily in skeletal muscle tissue via the action of creatine kinase(s). Group: Coenzymes. Synonyms: N-Amidinosarcosine monohydrate. CAS No. 6020-87-7. Mole weight: 149.15. Form: Solid. N-Amidinosarcosine monohydrate; Creatine monohydrate; 6020-87-7. Cat No: COEC-096. | |
| Cytochrome P450 Reductase from Human, Recombinant | Cytochrome P450 reductase is a membrane bound enzyme required for electron transfer from NADP to cytochrome P450 in microsomes. It can also provide electron transfer to heme oxygenase and cytochrome B5. The cytochrome P450 enzyme system is mainly involved in the detoxification of xenobiotics in the liver. It also participates in the activation of procarcinogens and the metabolism of endogeneous substrates such as steroids. Applications: Human cytochrome p450 reductase has been used in a study to assess the biocatalytic synthesis and structure elucidation of cyclized metabolites of the deacetylase inhibitor panobinostat. human cytochrome p450 reductase has also been u...AD-cytochrome c reductase; NADPH-dependent cytochrome c reductase; NADPH:P-450 reductase. Enzyme Commission Number: EC 1.6.2.4. CAS No. 9023-3-4. Purity: >90% (SDS-PAGE). CPR. Mole weight: 76.5 kDa. Activity: >30 U/mg. Storage: Store at -70°C. Form: Supplied in a solution containing 10 mM potassium phosphate, pH 7.4, 0.1 mM EDTA, 0.5 mM DTT, 20% (v/v) glycerol. Source: Baculovirus infected insect cells. Species: Human. EC 1.6.2.4; NADPH:ferrihemoprotein oxidoreductase; NADPH:hemoprotein oxidoreductase; NADPH:P450 oxidoreductase; P450 reductase; CPR; 9039-06-9; FAD-cytochrome c reductase; NADPH-dependent cytochrome c reductase; NADPH:P-450 reductase. Cat No: NATE-1586. | |
| dihydroorotate dehydrogenase (quinone) | This Class 2 dihydroorotate dehydrogenase enzyme contains FMN. The enzyme is found in eukaryotes in the mitochondrial membrane, in cyanobacteria, and in some Gram-negative and Gram-positive bacteria associated with the cytoplasmic membrane. The reaction is the only redox reaction in the de-novo biosynthesis of pyrimidine nucleotides. The best quinone electron acceptors for the enzyme from bovine liver are ubiquinone-6 and ubiquinone-7, although simple quinones, such as benzoquinone, can also act as acceptor at lower rates. Methyl-, ethyl-, tert-butyl and benzyl (S)-dihydroorotates are also substrates, but methyl esters of (S)-1-methyl and (S)-3-methyl and (S)-1,3-dimethyldihydroorotates are not. Class 1 dihydroorotate dehydrogenases use either fumarate (EC 1.3.98.1), NAD+ (EC 1.3.1.14) or NADP+ (EC 1.3.1.15) as electron acceptor. Group: Enzymes. Synonyms: dihydroorot. Enzyme Commission Number: EC 1.3.5.2. CAS No. 59088-23-2. 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-1386; dihydroorotate dehydrogenase (quinone); EC 1.3.5.2; 59088-23-2; dihydroorotate:ubiquinone oxidoreductase; (S)-dihydroorotate:(acceptor) oxidoreductase; (S)-dihydroorotate:acceptor oxidoreductase; DHOdehase (ambiguous); DHOD (ambiguous); DHODase (ambiguous); DHODH. Cat No: EXWM-1386. | |
| DT Diaphorase from human, Recombinant | DT Diaphorase is a flavoenzyme that catalyzes the oxidation of reduced di-and triphosphopyridine nucleotides. It contains one mole of FAD per mole of enzyme. The enzyme found in rat liver catalyzes the oxidation of NADH and NADPH by various dyes and quinones. The molecular weight is found to be approximately 48 kDa Da. The pH optimum of the enzyme purified from rat liver is found to be 5.0. It is a cytosolic enzyme that catalyzes the two-electron reduction of various quinones. It catalyzes the conversion of vitamin K to vitamin K hydroquinone for utilization in the post-translational γ-glutamyl carboxylation reactions. These reactions are necessary for several proteins involved in blood coagulation. Applications: Human dt diaphorase has been used in a study to assess the development of novel quinone phosphorodiamidate prodrugs. human dt diaphorase has also been used to investigate its crystal structure for the development of a model for its interaction with the cytotoxic prodrug 5-(aziridin-1-yl)-2,4-dinitrobenzamide (cb1954). Group: Enzymes. Synonyms: menadione reductase; phylloquinone reductase; quinone reductase; dehydrogenase, reduced nicotinamide adenine dinucleotide (phosphate, quinone); DT-diaphorase; flavoprotein NAD (P)H-q. Enzyme Commission Number: EC 1.6.99.2. Diaphorase. Mole weight: monomer mol wt 31 kDa. Storage: 2-8°C. F | |
| DT Diaphorase from rat, Recombinant | DT Diaphorase is a flavoenzyme that catalyzes the oxidation of reduced di-and triphosphopyridine nucleotides. It contains one mole of FAD per mole of enzyme. The enzyme found in rat liver catalyzes the oxidation of NADH and NADPH by various dyes and quinones. The molecular weight is found to be approximately 48 kDa Da. The pH optimum of the enzyme purified from rat liver is found to be 5.0. It is a cytosolic enzyme that catalyzes the two-electron reduction of various quinones. It catalyzes the conversion of vitamin K to vitamin K hydroquinone for utilization in the post-translational γ-glutamyl carboxylation reactions. These reactions are necessary for several proteins involved in blood coagulation. Applications: Dt diaphorase from rat has been used in a study to investigate the two-electron reduction of quinones by rat liver. dt diaphorase from rat has also been used in a study to investigate colon cancer chemopreventive efficacy of silibinin through perturbation of xenobiotic metabolizing enzymes. Group: Enzymes. Synonyms: menadione reductase; phylloquinone reductase; quinone reductase; dehydrogenase, reduced nicotinamide adenine dinucleotide (phosphate, quinone); DT-diaphorase; flavoprotein NAD (P)H-qui. Enzyme Commission Number: EC 1.6.99.2. Purity: ~90% (SDS-PAGE). Diaphorase. Mole weight: monomer mol wt 31 kDa. Storage: 2-8°C. Form | |
| Entacapone | Entacapone is a potent, reversible, peripherally acting and orally active catechol-O-methyltransferase (COMT) inhibitor. Entacapone inhibits COMT from rat brain, erythrocytes and liver with IC 50 values of 10 nM, 20 nM, and 160 nM, respectively. Entacapone is selective for COMT over other catecholamine metabolizing enzymes, including MAO-A, MAO-B, phenolsulphotransferase M (PST-M) and PST-P (IC 50 s>50 μM). Entacapone can be used for the research of Parkinson's disease [1]. Entacapone serves as a inhibitor of FTO demethylation with an IC 50 of 3.5 μM, can be used for the research of metabolic disorders [2]. Uses: Scientific research. Group: Signaling pathways. CAS No. 130929-57-6. Pack Sizes: 10 mM * 1 mL; 5 mg; 10 mg; 50 mg; 100 mg. Product ID: HY-14280. | |
| fructokinase | Fructokinase, also known as D-fructokinase or D-fructose (D-mannose) kinase, is an enzyme (EC 2.7.1.4) of the liver, intestine, and kidney cortex. Fructokinase is in a family of enzymes called transferases, meaning that this enzyme transfers functional groups; it is also considered a phosphotransferase (or, frequently, a kinase) since it specifically transfers a phosphate group. Fructokinase specifically catalyzes the transfer of a phosphate group from ATP (the substrate) to fructose as the initial step in its utilization. The main role of fructokinase is in carbohydrate metabolism, more specifically, sucrose and fructose metabolism. The reaction equation is as follows: ATP + D-fructose = ADP + D-fructose 6-phosphate. This is notable because in most tissues this reaction is catalyzed by hexokinase (EC 2.7.1.1). Group: Enzymes. Synonyms: fructokinase (phosphorylating); D-fructokinase; D-fructose(D-mannose)kinase. Enzyme Commission Number: EC 2.7.1.4. CAS No. 9030-51-7. 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-3069; fructokinase; EC 2.7.1.4; 9030-51-7; fructokinase (phosphorylating); D-fructokinase; D-fructose(D-mannose)kinase. Cat No: EXWM-3069. | |
| (-)-γ-cadinene synthase [(2Z,6E)-farnesyl diphosphate cyclizing] | Isolated from the liverwort Heteroscyphus planus. cf EC 4.2.3.92 (+)-γ-cadinene synthase. Group: Enzymes. Synonyms: (-)-γ-cadinene cyclase. Enzyme Commission Number: EC 4.2.3.62. 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-5223; (-)-γ-cadinene synthase [(2Z,6E)-farnesyl diphosphate cyclizing]; EC 4.2.3.62; (-)-γ-cadinene cyclase. Cat No: EXWM-5223. | |
| glycine N-phenylacetyltransferase | Not identical with EC 2.3.1.13 (glycine N-acyltransferase).This enzyme was purified from bovine liver mitochondria. L-asparagine, L-glutamine and L-arginine are alternative substrates to glycine, but have higher Km values. Group: Enzymes. Synonyms: arylacetyl-CoA N-acyltransferase; arylacetyltransferase; GAT (gene name). Enzyme Commission Number: EC 2.3.1.192. 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-2135; glycine N-phenylacetyltransferase; EC 2.3.1.192; arylacetyl-CoA N-acyltransferase; arylacetyltransferase; GAT (gene name). Cat No: EXWM-2135. | |
| Hempseed Extract | Hempseed Extract. Applications: It contain polysaccharide,promote the functional recovery of the human immunity ststem.indirect antiviral and anti-neoplastic effection and lessens the side effects of radiation and chemotherapy. it can protect livers, lower the enzyme(cpt), prolong the life, calm the nerves, strengthen the stomach, improve looks and so on. Group: Others. Synonyms: Hempseed Extract; Poria cocos ?Schw.? Wolf. Purity: 10:1 by TLC. Appearance: Off white fine powder. Storage: 2 years under well storage situation and stored away from direct sun light. Source: Fruit. Species: Poria cocos ?Schw.? Wolf. Hempseed Extract; Poria cocos ?Schw.? Wolf; plant extract. Pack: 25KG/Drum with double plastic bag of foodstuff inside. Cat No: EXTW-197. | |
| hexadecanol dehydrogenase | The liver enzyme acts on long-chain alcohols from C8 to C16. The Euglena enzyme also oxidizes the corresponding aldehydes to fatty acids. Group: Enzymes. Enzyme Commission Number: EC 1.1.1.164. CAS No. 62213-59-6. 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-0067; hexadecanol dehydrogenase; EC 1.1.1.164; 62213-59-6. Cat No: EXWM-0067. | |
| leucine transaminase | A pyridoxal-phosphate protein. This enzyme differs from EC 2.6.1.42, branched-chain-amino-acid transaminase, in that it does not act on L-valine or L-isoleucine, although it does act on L-methionine. The mitochondrial form from rat liver differs in physical characteristics from the cytoplasmic form. Group: Enzymes. Synonyms: L-leucine aminotransferase; leucine 2-oxoglutarate transaminase; leucine aminotransferase; leucine-α-ketoglutarate transaminase. Enzyme Commission Number: EC 2.6.1.6. CAS No. 9030-37-9. 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-2901; leucine transaminase; EC 2.6.1.6; 9030-37-9; L-leucine aminotransferase; leucine 2-oxoglutarate transaminase; leucine aminotransferase; leucine-α-ketoglutarate transaminase. Cat No: EXWM-2901. | |
| Lipase A from Candida Antarctica, Recombinant | Lipase A from Candida Antarctica catalyzes hydrolysis of tertiary alcohols to form glycerol and fatty acids and shows selectivity for the N-acylation of β-amino esters. Group: Enzymes. Synonyms: EC 3.1.1.3; lipase; triglyceride lipase; tributyrase; butyrinase; glycerol ester hydrolase; tributyrinase; Tween hydrolase; steapsin; triacetinase; tributyrin esterase; Tweenase; amno N-AP; Takedo 1969-4-9; Meito . Enzyme Commission Number: EC 3.1.1.3. CAS No. 9001-62-1. Lipase. Activity: ~2 units/mg. Storage: 2-8°C. Form: powder; beige. Source: Aspergillus oryzae. Species: Candida Antarctica. EC 3.1.1.3; lipase; triglyceride lipase; tributyrase; butyrinase; glycerol ester hydrolase; tributyrinase; Tween hydrolase; steapsin; triacetinase; tributyrin esterase; Tweenase; amno N-AP; Takedo 1969-4-9; Meito MY 30; Tweenesterase; GA 56; capalase L; triglyceride hydrolase; triolein hydrolase; tween-hydrolyzing esterase; amano CE; cacordase; triglyceridase; triacylglycerol ester hydrolase; amano P; amano AP; PPL; glycerol-ester hydrolase; GEH; meito Sangyo OF lipase; hepatic lipase; lipazin; post-heparin plasma protamine-resistant lipase; salt-resistant post-heparin lipase; heparin releasable hepatic lipase; amano CES; amano B; tributyrase; triglyceride lipase; liver lipase; hepatic monoacylglycerol acyltransferase; 9001-62-1. Cat No: NATE-0397. | |
| Lisinopril dihydrate | The hydrate form of Lisinopril. Lisinopril is an angiotensin-converting enzyme (ACE) inhibitor with a number of properties distinguish it from other ACE inhibitors: It is hydrophilic, has a long half-life and tissue penetration, and is not metabolized by the liver. Uses: Cardiotonic agents. Synonyms: (S)-1-[N2-(1-Carboxy-3-phenylpropyl)-L-lysyl]-L-proline Dihydrate; MK-521; Acerbon; Alapril; Carace; Coric; Novatec; Prinil; Prinivil; Tensopril; Vivatec; Zestril. Grades: 98%. CAS No. 83915-83-7. Molecular formula: C21H35N3O7. Mole weight: 441.52. | |
| long-chain acyl-CoA dehydrogenase | Contains FAD as prosthetic group. One of several enzymes that catalyse the first step in fatty acids β-oxidation. The enzyme from pig liver can accept substrates with acyl chain lengths of 6 to at least 16 carbon atoms. The highest activity was found with C12, and the rates with C8 and C16 were 80 and 70%, respectively. The enzyme from rat can accept substrates with C8-C22. It is most active with C14 and C16, and has no activity with C4, C6 or C24. cf. EC 1.3.8.1, short-chain acyl-CoA dehydrogenase, EC 1.3.8.8, medium-chain acyl-CoA dehydrogenase, and EC 1.3.8.9, very-long-chain acyl-CoA dehydrogenase. Group: Enzymes. Synonyms: palmitoyl-CoA dehydrogenase; palmitoyl-coenzyme A dehydrogenase; long-chain acyl-coenzyme A dehydrogenase; long-chain-acyl-CoA:(acceptor) 2,3-oxidoreductase; ACADL (gene name). Enzyme Commission Number: EC 1.3.8.8. CAS No. 59536-74-2. 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-1415; long-chain acyl-CoA dehydrogenase; EC 1.3.8.8; 59536-74-2; palmitoyl-CoA dehydrogenase; palmitoyl-coenzyme A dehydrogenase; long-chain acyl-coenzyme A dehydrogenase; long-chain-acyl-CoA:(acceptor) 2,3-oxidoreductase; ACADL (gene name). Cat No: EXWM-1415. | |
| long-chain-fatty-acid-CoA ligase | Acts on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. The liver enzyme acts on acids from C6 to C20; that from brain shows high activity up to C24. Group: Enzymes. Synonyms: acyl-CoA synthetase; fatty acid thiokinase (long chain); acyl-activating enzyme; palmitoyl-CoA synthase; lignoceroyl-Co. Enzyme Commission Number: EC 6.2.1.3. CAS No. 9013-18-7. ACS3. 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-5687; long-chain-fatty-acid-CoA ligase; EC 6.2.1.3; 9013-18-7; acyl-CoA synthetase; fatty acid thiokinase (long chain); acyl-activating enzyme; palmitoyl-CoA synthase; lignoceroyl-CoA synthase; arachidonyl-CoA synthetase; acyl coenzyme A synthetase; acyl-CoA ligase; palmitoyl coenzyme A synthetase; thiokinase; palmitoyl-CoA ligase; acyl-coenzyme A ligase; fatty acid CoA ligase; long-chain fatty acyl coenzyme A synthetase; oleoyl-CoA synthetase; stearoyl-CoA synthetase; long chain fatty acyl-CoA synthetase; long-chain acyl CoA synthetase; fatty acid elongase; LCFA synthetase; pristanoyl-CoA synthetase; ACS3; long-chain acyl-CoA synthetase I; long-chain acyl-CoA synthetase II; fatty acyl-coenzyme A synthetase; long-chain acyl-coenzyme A synthetase; FAA1. Cat No: EXWM-5687. | |
| medium-chain acyl-CoA dehydrogenase | Contains FAD as prosthetic group. One of several enzymes that catalyse the first step in fatty acids β-oxidation. The enzyme from pig liver can accept substrates with acyl chain lengths of 4 to 16 carbon atoms, but is most active with C8 to C12 compounds. The enzyme from rat does not accept C16 at all and is most active with C6-C8 compounds. cf. EC 1.3.8.1, short-chain acyl-CoA dehydrogenase, EC 1.3.8.8, long-chain acyl-CoA dehydrogenase, and EC 1.3.8.9, very-long-chain acyl-CoA dehydrogenase. Group: Enzymes. Synonyms: fatty acyl coenzyme A dehydrogenase (ambiguous); acyl coenzyme A dehydrogenase (ambiguous); acyl dehydrogenase (ambiguous); fatty-acyl-CoA dehydrogenase (ambiguous); acyl CoA dehydrogenase (ambiguous); general acyl CoA dehydrog. Enzyme Commission Number: EC 1.3.8.7. 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-1414; medium-chain acyl-CoA dehydrogenase; EC 1.3.8.7; fatty acyl coenzyme A dehydrogenase (ambiguous); acyl coenzyme A dehydrogenase (ambiguous); acyl dehydrogenase (ambiguous); fatty-acyl-CoA dehydrogenase (ambiguous); acyl CoA dehydrogenase (ambiguous); general acyl CoA dehydrogenase (ambiguous); medium-chain acyl-coenzyme A dehydrogenase; acyl-CoA:(acceptor) 2,3-oxidoreductase (ambiguous); ACADM (gene name). Cat No: EXWM-1414. | |
| Monoamine Oxidase (Crude Enzyme) | L-Monoamine oxidases (MAO) are a family of enzymes that catalyze the oxidation of monoamines. They are found bound to the outer membrane of mitochondria in most cell types in the body. The enzyme was originally discovered by Mary Bernheim in the liver and was named tyramine oxidase. They belong to the protein family of flavin-containing amine oxidoreductases. This product with the indicated enzyme activity was briefly purified from engineered E. coli. Applications: Synthesis; drug development; analysis; medicine. Group: Enzymes. Synonyms: equilase; caperase; optidase; catalase-peroxidase; CAT. Enzyme Commission Number: EC 1.4.3.4. CAS No. 9001-66-5. Monoamine Oxidase. Activity: Undetermined. Appearance: Clear to translucent yellow solution. Storage: at -20 °C or lower, for at least 1 month. Source: E. coli. equilase; caperase; optidase; catalase-peroxidase; CAT. Pack: 100ml. Cat No: NATE-1808. | |
| NADPH dehydrogenase (quinone) | A flavoprotein. The enzyme from Escherichia coli is specific for NADPH and is most active with quinone derivatives and ferricyanide as electron acceptors.Menaquinone can act as acceptor. The enzyme from hog liver is inhibited by dicoumarol and folic acid derivatives but not by 2,4-dinitrophenol. Group: Enzymes. Synonyms: reduced nicotinamide adenine dinucleotide phosphate (quinone) dehydrogenase; NADPH oxidase; NADPH2 dehydrogenase (quinone). Enzyme Commission Number: EC 1.6.5.10. CAS No. 37256-37-4. 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-1588; NADPH dehydrogenase (quinone); EC 1.6.5.10; 37256-37-4; reduced nicotinamide adenine dinucleotide phosphate (quinone) dehydrogenase; NADPH oxidase; NADPH2 dehydrogenase (quinone). Cat No: EXWM-1588. | |
| Native Bacillus licheniformis Proteinase | Proteinase catabolizes proteins by hydrolysis of peptide bonds. Proteases are inactivated by serine active-site inhibitors, such as phenylmethylsulfonyl fluoride (PMSF) and diisopropylfluorophosphate. Subtilisin is a non-glycosylated single polypeptide chain without disulfide bonds and has a molecular weight of 27 kda. Applications: The enzyme from creative enzymes has been used to optimize release of all mit ochondrial populations from homogenized ventricular tissue of rat heart. it has also been used in the pre-hybridisation treatment of formalin fixed, paraffin wax-embedded liver specimens for detecting human and viral dna. this is a proteolytic enzyme isolated from th...ls to study the silencing of cardiac mit ochondrial nhe1. Group: Enzymes. Synonyms: protease; peptidase; proteinase; EC 3.4.21.62; 9014-01-1; Alkaline Protease; Protease from Bacillus licheniformis; Proteinase from Bacillus licheniformis; Subtilo peptidase A. Enzyme Commission Number: EC 3.4.21.62. CAS No. 9001-92-7. Purity: crystallization. Proteinase. Mole weight: 27 KDa. Activity: 7.0-14.0 units/mg solid. Storage: -20°C. Form: lyophilized powder. Source: Bacillus licheniformis. protease; peptidase; proteinase; EC 3.4.21.62; 9014-01-1; Alkaline Protease; Protease from Bacillus licheniformis; Proteinase from Bacillus licheniformis; Subtilo peptidase A. Cat No: NATE-0639. | |
| Native Bovine Catalase | Catalase activates the decomposition of hydrogen peroxide, a reactive oxygen species, into water and oxygen. It functions as a natural antioxidant, protecting cells against oxidative damage to proteins, lipids and nucleic acids. Catalase has also been used to study the role reactive oxygen species play in gene expression and apoptosis. Group: Enzymes. Synonyms: EC 1.11.1.6; Catalase; catalase; equilase; caperase; optidase; catalase-peroxidase; CAT; H2O2:H2O2 oxidoreductase; 9001-05-2. Enzyme Commission Number: EC 1.11.1.6. CAS No. 9001-5-2. CAT. Activity: Type 1 (Suspension) > 20,000 units per mg; Type 2 (Filtered) > 40,000 units per mg; Type 3 (Lyophilized) > 3,000 units per mg. Storage: All preparations are stable for 12 months at 2-8°C. Lyophilized preparations should be protected from moisture. Form: A partially purified, lyophilized powder. Source: Bovine Liver. Species: Bovine. EC 1.11.1.6; Catalase; catalase; equilase; caperase; optidase; catalase-peroxidase; CAT; H2O2:H2O2 oxidoreductase; 9001-05-2. Cat No: NATE-0105. | |
| Native Bovine Deoxyribonuclease II | Deoxyribonuclease II, also called as acid DNAse, hydrolyzes deoxyribonucleotide linkages in native and denatured DNA yielding products with 3'-phosphates. In vitro, its optimum pH range is 4.5-5.0. It also acts upon p-nitrophenyl-phosphodiesters at pH 5.6-5.9. The molecular weight is approximately 38 kDa Da. Applications: Dnase ii from creative enzymes has been used in the dissociation medium during the preparation of embryonic cardiac myocytes from rat heart. deoxyribonuclease ii from bovine spleen has been used in a study that conducted a partial purification of deoxyribonucleases from eggs and liver of xenopus laevis. deoxyribonuclease ii from bovine spleen has also been used in a study to investigate nucleic acid and protein synthesis of splenic lymphocytes. Group: Enzymes. Synonyms: DNASE2; deoxyribonuclease II; EC 3.1.22.1; 9025-64-3; DNase II; pancreatic DNase II; deoxyribonucleate 3'-nucleotidohydrolase; DNase II; pancreati. Enzyme Commission Number: EC 3.1.22.1. CAS No. 9025-64-3. DNASE2. Activity: > 1,000 units/mg protein. Storage: -20°C. Form: essentially salt-free, lyophilized powder. Source: Bovine spleen. Species: Bovine. DNASE2; deoxyribonuclease II; EC 3.1.22.1; 9025-64-3; DNase II; pancreatic DNase II; deoxyribonucleate 3'-nucleotidohydrolase; DNase II; pancreatic DNase II; acid deoxyribonuclease; acid Dnase. Cat No: NATE-0201. | |
| Native Bovine Glutamate Dehydrogenase | 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 [NAD(P)+]; EC 1.4.1.3; GLDH; glutamic dehydrogenase; glutamate dehydrogenase [NAD(P)]; L-glutamate: NAD(P)+ oxidoreductase (deaminating); L-GLDH; Glutamate Dehydrogenase from bovine liver; L-Glutamic Dehydrogenase; glutamate dehydrogenase. Enzyme Commission Number: EC 1.4.1.3. CAS No. 9001-46-1. GLDH. Mole weight: 260 kDa (gel). Activity: > 500U /mg protein. Appearance: White/off white powder. Storage: -20°C. Form: Freeze dried powder. Source: Bovine liver. Species: Bovine. glutamate dehydrogenase [NAD(P)+]; EC 1.4.1.3; GLDH; glutamic dehydrogenase; glutamate dehydrogenase [NAD(P)]; L-glutamate: NAD(P)+ oxidoreductase (deaminating); L-GLDH; Glutamate Dehydrogenase from bovine liver; L-Glutamic Dehydrogenase; glutamate dehydrogenase. Cat No: DIA-146. | |
| Native Bovine Kidney Alkaline Phosphatase | Alkaline Phosphatase is a hydrolase enzyme responsible for removing phosphate groups in the 5- and 3- positions from many types of molecules, including nucleotides, proteins, and alkaloids. In humans, alkaline phosphatase is present in all tissues throughout the entire body, but is particularly concentrated in liver, bile duct, kidney, bone, and the placenta. The optimal pH for the enzyme activity is 10.0 in standard conditions. Group: Enzymes. Synonyms: Alkaline phosphatase; ALP; ALKP; ALPase; Alk Phos; EC 3.1.3.1; Alkaline phosphomonoesterase; Glycerophosphatase; Phosphomonoesterase. Enzyme Commission Number: EC 3.1.3.1. CAS No. 9001-78-9. Activity: > 750 U/mg solid. Storage: Store at -20°C. Form: Freeze dried powder. Source: Bovine Kidney. Species: Bovine. Alkaline phosphatase; ALP; ALKP; ALPase; Alk Phos; EC 3.1.3.1; Alkaline phosphomonoesterase; Glycerophosphatase; Phosphomonoesterase. Cat No: NATE-0946. | |
| Native Bovine Liver Alkaline Phosphatase | Alkaline phosphatases (APs) are highly ubiquitous enzymes, present in all species from bacteria to man. In humans, APs are encoded by a multi-gene family composed of four loci; i.e., tissue-nonspecific AP, also called bone/liver/kidney AP, intestinal. The sequence and complexity of the AP genes from other vertebrates and lower species are now being elucidated. The biological function of AP isozymes is still unknown. In vitro, the enzymes behave as phosphotransferases at neutral pH. The use of phosphate acceptor molecules (diethanolamine, tris, 2-amino-2-methyl-1-propanol) in the buffered substrate solutions increases the reaction rates and, thus, the sensitivity of assays based on AP determinations. Group: Enzymes. Synonyms: Alkaline phosphatase; ALP; ALKP; ALPase; Alk Phos; EC 3.1.3.1; Alkaline phosphomonoesterase; Glycerophosphatase; Phosphomonoesterase. Enzyme Commission Number: EC 3.1.3.1. CAS No. 9001-78-9. Activity: 100 U/mg protein. Storage: Store at -20° C. Form: Freeze-dried powder. Source: Bovine Liver. Species: Bovine. Alkaline phosphatase; ALP; ALKP; ALPase; Alk Phos; EC 3.1.3.1; Alkaline phosphomonoesterase; Glycerophosphatase; Phosphomonoesterase; AP. Cat No: NATE-1871. | |
| Native Bovine Protein Disulfide Isomerase | Protein Disulfide Isomerase (PDI) has the C-terminal ER retention sequence Lys-Asp-Glu-Leu. It has active, intracellular traffic to different cell compartments. PDI supports internalization of Chlamydia, cholera and diphtheria toxins in some hosts. PDI is required for Sindbis virus infection and aids in reducing HIV gp120 protein thiols. PDI facilitates formation of the correct disulfide bonds by promoting rapid reshuffling of disulfide pairings. Protein disulfide isomerase (pdi) from bovine liver is a homodimer with a molecular weight of 107 kda (gel filtration) and the molecular weight of the monomer has been reported at 57 kda (sds-page). the enzyme is a glycoprotein ... is mainly l ocated in the er, where it assists in protein-folding and thiol-disulfide exchanges. it is used to study functional role of pdi in parasite infection and the interaction between macrophage pdi and l. chagasi. Group: Enzymes. Synonyms: Protein disulfide isomerase; PDI; EC 5.3.4.1; 37318-49-3; S-S rearrangase. Enzyme Commission Number: EC 5.3.4.1. CAS No. 37318-49-3. Purity: >95% (SDS-PAGE). PDI. Activity: 100-400 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing potassium phosphate buffer salts and stabilizer. Source: Bovine liver. Species: Bovine. Protein disulfide isomerase; PDI; EC 5.3.4.1; 37318-49-3; S-S rearrangase. Cat No: NATE-0533. | |
| Native Bovine Protein Phosphatase 2C | Protein Phosphatase 2C is a Mg2+-dependent serine/threonine protein phosphatase with a molecular mass of 42-45 kDa, involved in regulating numerous cellular processes. It is ubiquitously expressed and has been isolated from many mammalian tissues including liver, brain, skeletal muscle, retina, and blood platelets. There are two major isotypes associated with this enzyme, 2C1 and 2C2, also known as 2Ca and 2Cb, respectively. Both isozymes appear to be equally Mg2+-dependent and respond similarly to specific substrates. Both are monomers that demonstrate ~75% sequence homology. The molecular masses are similar; 44 kDa and 42 kDa for 2C1 and 2C2, respectively. Additional Type 2C serine/threonine protein phosphatases include 2Cg, 2Cd, Wip1, and NERPP2C, many of which have multiple isozyme members. Group: Enzymes. Synonyms: Protein Phosphatase 2C; PP2C. Protein Phosphatase. Activity: ~1000 units/mg protein. Stability: -70°C. Form: buffered aqueous glycerol solution. Source: Bovine kidney. Species: Bovine. Protein Phosphatase 2C; PP2C. Pack: vial of 1 μg. Cat No: NATE-0619. | |
| Native Bovine Pyruvate Carboxylase | Pyruvate carboxylase catalyzes the carboxylation of pyruvate to oxaloacetate. Pyruvate carboxylase is a mitochondrial protein that has a biotin prosthetic group that requiries magnesium or manganese and acetyl CoA. Applications: Pyruvate is critical for gluconeogenesis, lipogenesis, glyceroneogenesis, neurotransmitter biosynthesis and glucose-induced insulin, and is used to study these pr ocesses. the enzyme from creative enzymes has been used as a positive control during the assay of pyruvate carboxylase activity in cell-free extracts of corynebacterium glutamicum. Group: Enzymes. Synonyms: Pyruvate carboxylase; PC; EC 6.4.1.1; 9014-19-1; pyruvic carboxylase. Enzyme Commission Number: EC 6.4.1.1. CAS No. 9014-19-1. PC. Activity: 5-25 units/mg protein (BCA). Storage: -20°C. Form: buffered aqueous glycerol solution; Solution in 50% glycerol containing 0.05 M Tris-HCl, pH 7.4, 2 mM magnesium acetate and 1 mM EDTA. Source: Bovine liver. Species: Bovine. Pyruvate carboxylase; PC; EC 6.4.1.1; 9014-19-1; pyruvic carboxylase. Cat No: NATE-0508. | |
| Native Candida Rugosa Cholesterol Esterase | Cholesterol esterase (CE) is also known as cholesterol ester hydrolase. This enzyme catalyzes the following reaction: Sterol Ester --------> Sterol + Fatty Acid.Cholesterol esterase activity has been demonstrated in pancreas, intestine, liver and kidney. The enzyme is inactivated by proteolytic enzymes but stabilized by proteolytic enzyme inhibitors and by bile salts. CE from rat pancreas has a molecular weight of 65,000-69,000. In the presence of bile salts, it aggregates to a hexamer which is possibly the active form of the enzyme. Group: Enzymes. Synonyms: cholesterol esterase; cholesteryl ester synthase; triterpenol esterase; cholesteryl esterase; cholesteryl ester hydrolase; sterol ester hydrolase; cholesterol ester hydrolase; cholesterase; acylcholesterol lipase; sterol esterase; CE. Enzyme Commission Number: EC 3.1.1.13. CAS No. 9026-00-0. Purity: 0.9. Cholesterol Esterase. Activity: 25-100 U/mg. Storage: Store at -20° C. Form: Freeze-dried powder. Source: Candida Rugosa. cholesterol esterase; cholesteryl ester synthase; triterpenol esterase; cholesteryl esterase; cholesteryl ester hydrolase; sterol ester hydrolase; cholesterol ester hydrolase; cholesterase; acylcholesterol lipase; sterol esterase; CE. Cat No: NATE-1679. | |
| Native Chicken α-N-Acetylgalactosaminidase | α-N-acetylgalactosaminidase (EC 3.2.1.49) is a glycoside hydrolase from bacteria and animals, also known as nagalase. The human gene that codes for this enzyme is NAGA. Mutations in this gene and the deficiency in alpha-N-acetylgalactosaminidase activity have been identified as the cause of Schindler disease. Group: Enzymes. Synonyms: EC 3.2.1.49; 9075-63-2; α-N-acetylgalactosaminidase; Alpha-N-acetylgalactosaminidase; α-acetylgalactosaminidase; N-acetyl-α-D-galactosaminidase; N-acetyl-α-galactosaminidase; α-NAGAL; α-NAGA; α-GalNAcase. Enzyme Commission Number: EC 3.2.1.49. CAS No. 9075-63-2. α-NAGA. Source: Chicken Liver. Species: Chicken. EC 3.2.1.49; 9075-63-2; α-N-acetylgalactosaminidase; Alpha-N-acetylgalactosaminidase; α-acetylgalactosaminidase; N-acetyl-α-D-galactosaminidase; N-acetyl-α-galactosaminidase; α-NAGAL; α-NAGA; α-GalNAcase. Cat No: NATE-0755. | |
| Native Chicken Malic Dehydrogenase (oxalacetate-decarboxylating) | Malic dehydrogenase (MDH) exists as two isoforms within eukaryotic cells, one that is expressed in the mitochondria and functions in the TCA cycle and one in the cytoplasm that converts malate from the mitochondria back into oxaloacetate. Malic dehydrogenase (mdh) exists as two isoforms within eukaryotic cells, one that is expressed in the mit ochondria and functions in the tca cycle and one in the cytoplasm that converts malate from the mit ochondria back into oxaloacetate. Applications: Malic dehydrogenase has been used in a study to assess the dietary manganese requirement of juvenile yellow catfish (pelteobagrus fulvidraco) and effects on whole body minera...ctivity: 10-30 units/mg protein (modified Warburg-Christian). Storage: 2-8°C. Form: ammonium sulfate suspension; Suspension in 2.9 M (NH4)2SO4 solution containing 10 mM potassium phosphate, 0.5 mM 2-mercaptoethanol, 10 mM manganese chloride, and 3 mM Na4EDTA, pH 6.0. Source: Chicken liver. Species: Chicken. malic enzyme (ambiguous); pyruvic-malic carboxylase (ambiguous); malate dehydrogenase (decarboxylating, NADP+); NADP+-linked decarboxylating malic enzyme; NADP+-malic enzyme; NADP+-specific malic enzyme; NADP-specific malate dehydrogenase; malate dehydrogenase (NADP+, decarboxylating); L-malate:NADP+oxidoreductase; EC 1.1.1.40; 9028-47-1. Cat No: NATE-0446. | |
| Native E. coli Alanine Aminotransferase | Alanine transaminase (ALT) is a transaminase enzyme (EC 2.6.1.2). It is also called alanine aminotransferase (ALAT) and was formerly called serum glutamate-pyruvate transaminase (SGPT) or serum glutamic-pyruvic transaminase (SGPT). ALT is found in plasma and in various body tissues, but is most common in the liver. It catalyzes the two parts of the alanine cycle. Serum ALT level, serum AST (aspartate transaminase) level, and their ratio (AST/ALT ratio) are commonly measured clinically as biomarkers for liver health. The tests are part of blood panels. Group: Enzymes. Synonyms: Alanine transami. Enzyme Commission Number: EC 2.6.1.2. CAS No. 9000-86-6. Purity: > 95% (SDS-PAGE). ALT. Mole weight: 54,479 of subunit deduced from gene sequence. Activity: > 1,000 U/mL. Storage: -20°C. Form: Liquid. Source: E. coli. Alanine transaminase; ALT; EC 2.6.1.2; alanine aminotransferase; ALAT; glutamic-pyruvic transaminase; glutamic-alanine transaminase; GPT; β-alanine aminotransferase; alanine-α-ketoglutarate aminotransferase; alanine-pyruvate aminotransferase; glutamic acid-pyruvic acid transaminase; glutamic-pyruvic aminotransferase; L-alanine aminotransferase; L-alanine transaminase; L-alanine-α-ketoglutarate aminotransferase; pyruvate transaminase; pyruvate-alanine aminotransferase; pyruvate-glutamate transaminase. Cat No: NATE-0064. | |
| Native Guinea pig Transglutaminase | Transglutaminase from guinea pig liver consists of a single polypeptide chain of 691 amino acid residues. It has six potential glycosylation sites (Asn-X-Ser or Asn-X-Thr), but it is not glycosylated. The molecular mass is approximately 76.6 kDa. It is calcium dependent and has several calcium binding sites. The enzyme is inhibited by iodoacetamide and N-ethylmaleimide in the presence of calcium. It catalyzes the incorporation of small molecular weight amines into γ-glutamine sites of proteins. In the absence of small molecular weight amines, it catalyzes the cross linking of proteins that results in the formation of γ-glutamyl-ε-lysine side chain peptide...h as huntington?s disease and alzheimer?s disease.transglutaminase has also been used in a study to develop a nonradioactive dot blot assay for transglutaminase activity. Group: Enzymes. Synonyms: transglutaminase; EC 2.3.2.13; 80146-85-6; transglutaminase; Factor XIIIa; fibrinoligase; fibrin stabilizing factor; glutaminylpeptide γ-glutamyltransferase; polyamine transglutaminase; tissue transglutaminase; R-glutaminyl-peptide:amine γ-glutamyl transferase; protein-glutamine γ-glutamyltransferase. Enzyme Commission Number: EC 2.3.2.13. CAS No. 80146-85-6. Transglutaminase. Activity: > 1.5 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing Tr | |
| 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 Human Cathepsin B | Cathepsin B has been found to cleave procaspase 1 and procaspase 11 and to induce apoptosis in digitonin-permeabilized cells. Translocation of cathepsin B from the cytoplasm to the nucleus contributes to bile salt induced apoptosis of rat hepatocytes. Levels of cathepsin B in PC12 cells significantly decrease 12 to 24 hours after apoptosis is induced. Group: Enzymes. Synonyms: CTSB; cathepsin B; cathepsin B1; APPS; CPSB; EC 3.4.22.1; 9047-22-7; cathepsin II; CatB. Enzyme Commission Number: EC 3.4.22.1. CAS No. 9047-22-7. Cathepsin B. Activity: > 2 ,000 units/mg protein (E1%/280). Storage: -20°C. Form: buffered aqueous solution. Solution in 50 mM sodium acetate, pH 5.0, with 1 mM EDTA. Source: Human liver. Species: Human. CTSB; cathepsin B; cathepsin B1; APPS; CPSB; EC 3.4.22.1; 9047-22-7; cathepsin II; CatB. Cat No: NATE-0168. | |
| Native Human Cathepsin H | Cathepsin H is a protein that in humans is encoded by the CTSH gene. The protein encoded by this gene is a lysosomal cysteine proteinase important in the overall degradation of lysosomal proteins. It is composed of a dimer of disulfide-linked heavy and light chains, both produced from a single protein precursor. The encoded protein, which belongs to the peptidase C1 protein family, can act both as an aminopeptidase and as an endopeptidase. Increased expression of this gene has been correlated with malignant progression of prostate tumors. Two transcript variants encoding different isoforms have been found for this gene. Group: Enzymes. Synonyms: CTSH; cathepsin H; CPSB; ACC-4; ACC-5; ACC4; ACC5; CPSB; minichain. Purity: > 95% (SDS-PAGE). CTSH. Mole weight: 28 kDa. Storage: -40°C. Form: Liquid. Source: Human Liver. Species: Human. CTSH; cathepsin H; CPSB; ACC-4; ACC-5; ACC4; ACC5; CPSB; minichain. Cat No: NATE-0176. | |
| Native Human Lactate Dehydrogenase 4 | A lactate dehydrogenase (LDH or LD) is an enzyme found in nearly all living cells (animals, plants, and prokaryotes). LDH catalyzes the conversion of pyruvate to lactate and back, as it converts NADH to NAD+ and back. A dehydrogenase is an enzyme that transfers a hydride from one molecule to another. Applications: Diagnostic controls, calibrators & standards; clinical chemistry; testing/assay validation; life science; validation studies; manufacturing. Group: Enzymes. Synonyms: LDH-4 isoenzyme; 1H3M isoenzyme; ld4 isoenyzme. Enzyme Commission Number: EC 1.1.1.27. CAS No. 9001-60-9. LDH. Activity: > 35 U/mg protein (> 110 U/mL). Stability: 2 years. Storage: 2-8°C. Form: Liquid; Suspension in 3.1 M ammonium sulfate, 20 mM tris chloride, 1 mM DTT, 1 mM EDTA, pH 7.5. Source: Human Liver. Species: Human. LDH-4 isoenzyme; 1H3M isoenzyme; ld4 isoenyzme; Lactate dehydrogenase; EC 1.1.1.27; LDH; LD. Cat No: NATE-0965. | |
| Native Human Lactate Dehydrogenase 5 | A lactate dehydrogenase (LDH or LD) is an enzyme found in nearly all living cells (animals, plants, and prokaryotes). LDH catalyzes the conversion of pyruvate to lactate and back, as it converts NADH to NAD+ and back. A dehydrogenase is an enzyme that transfers a hydride from one molecule to another. Applications: Research linical chemistry life science. Group: Enzymes. Synonyms: EC 1.1.1.27; 9001-60-9; lactate dehydrogenase; LDH; LD; (S)-Lactate:NAD+ oxidoreductase, L-LDH; LAD; L-Lactic Dehydrogenase; lactic acid dehydrogenase; L (+)-nLDH; L-(+)-lactate dehydrogenase; L-lactic acid dehydrogenase; lactate dehydrogenase NAD-dependent; lactic dehydrogenase; NAD-lactate dehydrogenase. Enzyme Commission Number: EC 1.1.1.27. CAS No. 9001-60-9. LDH. Activity: >90%. (>200U/mL). Storage: 4°C. Source: Human Liver. Species: Human. EC 1.1.1.27; 9001-60-9; lactate dehydrogenase; LDH; LD; (S)-Lactate:NAD+ oxidoreductase, L-LDH; LAD; L-Lactic Dehydrogenase; lactic acid dehydrogenase; L (+)-nLDH; L-(+)-lactate dehydrogenase; L-lactic acid dehydrogenase; lactate dehydrogenase NAD-dependent; lactic dehydrogenase; NAD-lactate dehydrogenase. Cat No: NATE-0390. | |
| Native Microorganism Sorbitol Dehydrogenase | Sorbitol dehydrogenase (or SDH) is a cytosolic enzyme. In humans this protein is encoded by the SORD gene. Sorbitol dehydrogenase is an enzyme in carbohydrate metabolism converting sorbitol, the sugar alcohol form of glucose, into fructose. Together with aldose reductase, it provides a way for the body to produce fructose from glucose without using ATP. Sorbitol dehydrogenase uses NAD+ as a cofactor; its reaction is sorbitol + NAD+--> fructose + NADH + H+. A zinc ion is also involved in catalysis. Organs that use it most frequently include the liver and seminal vesicle; it is found in all kinds of organisms from bacteria to humans. A secondary use is the metabolism of d... 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. Mole weight: ca. 68,000; Subunit molecular weight : ca. 26,000. Appearance: Lyophilized. Storage: Stable at -20 °C for at least one year. Source: Microorganism. Sorbitol Dehydrogenase; SDH; EC 1.1.1.14; 9028-21-1; L-iditol 2-dehydrogenase; 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: NATE-1909. | |
| Native Mucor miehei Lipase | Triacylglycerol lipase is an enzyme with system name triacylglycerol acylhydrolase. This enzyme catalyses the following chemical reaction:triacylglycerol + H2O<-> diacylglycerol + a carboxylate. Applications: Lipase from mucor miehei can be used to drive the synthesis of flavor esters. lipase from mucor miehei has been used in a study to assess the nonthermal effect of microwave irradiation in nonaqueous enzymatic esterification. it has also been used in a study to investigate the hydrolysis of virgin coconut oil using immobilized lipase in a batch reactor. Group: Enzymes. Synonyms: Triacylglycerol acylhydrolase; Triacylglycerol lipase. Enzyme Commission Number: EC 3.1.1.3. CAS ...rol ester hydrolase; tributyrinase; Tween hydrolase; steapsin; triacetinase; tributyrin esterase; Tweenase; amno N-AP; Takedo 1969-4-9; Meito MY 30; Tweenesterase; GA 56; capalase L; triglyceride hydrolase; triolein hydrolase; tween-hydrolyzing esterase; amano CE; cacordase; triglyceridase; triacylglycerol ester hydrolase; amano P; amano AP; PPL; glycerol-ester hydrolase; GEH; meito Sangyo OF lipase; hepatic lipase; lipazin; post-heparin plasma protamine-resistant lipase; salt-resistant post-heparin lipase; heparin releasable hepatic lipase; amano CES; amano B; tributyrase; triglyceride lipase; liver lipase; hepatic monoacylglycerol acyltransferase; 9001-62-1. Cat No: NATE-1609. | |
| Native Porcine Esterase | An esterase is a hydrolase that splits esters into acids and alcohols. Applications: Porcine liver esterase is used to catalyze the hydrolysis of pentaacetyl catechin and epicatechin for use in pharmaceutical and industrial applications. pig liver esterase is commonly used for kinetic resolutions and assymetric synthesis in organic chemistry. esterase from porcine liver has been used in a study to assess the effect of 5-aminolaevulinic acid peptide prodrugs on photosensitization for photodynamic therapy. esterase from porcine liver has also been used in a study to investigate how site-specific atherogenic gene expression correlates with subsequent variable lesion development in c...ms: EC 3.1.1.1; ali-esterase; B-esterase; monobutyrase; cocaine esterase; procaine esterase; methylbutyrase; vitamin A esterase; butyryl esterase; carboxyesterase; carboxylate esterase; carboxylic esterase; methylbutyRate esterase; triacetin esterase; carboxyl ester hydrolase; butyRate esterase; methylbutyrase; α-carboxylesterase; propionyl esterase; nonspecific carboxylesterase; esterase D; esterase B; esterase A; serine esterase; carboxylic acid esterase; cocaine esterase; 9016-18-6. Enzyme Commission Number: EC 3.1.1.1. CAS No. 9016-18-6. Esterase. Activity: Type I, > 15 units/mg solid; Type II, > 50 units/mg; Type III, > 150 units/mg protein (biuret). Storage: -20°C. For | |
| Native Porcine NAD(P)H Dehydrogenase (quinone) | DT Diaphorase is a flavoenzyme that catalyzes the oxidation of reduced di-and triphosphopyridine nucleotides. It contains one mole of FAD per mole of enzyme. The enzyme found in rat liver catalyzes the oxidation of NADH and NADPH by various dyes and quinones. The molecular weight is found to be approximately 48 kDa Da. The pH optimum of the enzyme purified from rat liver is found to be 5.0. It is a cytosolic enzyme that catalyzes the two-electron reduction of various quinones. It catalyzes the conversion of vitamin K to vitamin K hydroquinone for utilization in the post-translational γ-glutamyl carboxylation reactions. These reactions are necessary for several pr...hydrogenase; NAD (P)H menadione reductase; NAD (P)H-quinone dehydrogenase; NAD (P)H-quinone oxidoreductase; NAD (P)H: (quinone-acceptor)oxidoreductase. CAS No. 9032-20-6. Diaphorase. Activity: >25 U/mg. Stability: At +2 to +8°C within specification range for 12 months. Appearance: Yellow suspension in ammonium sulfate, 3.2 mol/l. Source: Porcine heart. Species: Porcine. menadione reductase; phylloquinone reductase; quinone reductase; dehydrogenase, reduced nicotinamide adenine dinucleotide (phosphate, quinone); DT-diaphorase; flavoprotein NAD (P)H-quinone reductase; menadione oxidoreductase; NAD (P)H dehydrogenase; NAD (P)H menadione reductase; NAD (P)H-quinone dehydro | |
| Native Rabbit Esterase | An esterase is a hydrolase that splits esters into acids and alcohols. Applications: Esterase from rabbit liver has been used in a study to investigate a toxic effect of carbamate insecticides. esterase from rabbit liver has also been used in a study to investigate the effect of simvastatin on expression and activity of a lipoprotein-ass ociated phospholipase a. the enzyme from creative enzymes has been used to study the effect of divalent metal ions on the activity of esterase. Group: Enzymes. Synonyms: EC 3.1.1.1; ali-esterase; B-esterase; monobutyrase; cocaine esterase; procaine esterase; methylbutyrase; vitamin A esterase; butyryl esterase; ca. Enzyme Commission Number: EC 3.1.1.1. CAS No. 9016-18-6. Esterase. Activity: > 75 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing Tris buffer salts. Source: Rabbit liver. Species: Rabbit. EC 3.1.1.1; ali-esterase; B-esterase; monobutyrase; cocaine esterase; procaine esterase; methylbutyrase; vitamin A esterase; butyryl esterase; carboxyesterase; carboxylate esterase; carboxylic esterase; methylbutyRate esterase; triacetin esterase; carboxyl ester hydrolase; butyRate esterase; methylbutyrase; α-carboxylesterase; propionyl esterase; nonspecific carboxylesterase; esterase D; esterase B; esterase A; serine esterase; carboxylic acid esterase; cocaine esterase; 9016-18-6. Cat No: NATE-0238. | |
| Native Rabbit Glucose-6-Phosphatase | Glucose 6-phosphatase (EC 3.1.3.9, G6Pase) is an enzyme that hydrolyzes glucose-6-phosphate, resulting in the creation of a phosphate group and free glucose. Glucose is then exported from the cell via glucose transporter membrane proteins. This catalysis completes the final step in gluconeogenesis and glycogenolysis and therefore plays a key role in the homeostatic regulation of blood glucose levels. Applications: Glucose-6-phosphatase was used to study the effects of clausena anisata (wild hook leaf) extracts on selected diabetes-related metabolizing enzymes. Group: Enzymes. Synonyms: EC 3.1.3.9; glucose 6-phosphate phosphatase; G6Pase; 9001-39-2; glucose-6-phosphatase. Enzyme Commission Number: EC 3.1.3.9. CAS No. 9001-39-2. Purity: Protein ~30 % (balance mostly sucrose). G6Pase. Activity: > 0.05 units/mg protein. Storage: -20°C. Form: powder with sucrose. Source: Rabbit liver. Species: Rabbit. EC 3.1.3.9; glucose 6-phosphate phosphatase; G6Pase; 9001-39-2; glucose-6-phosphatase. Cat No: NATE-0269. | |
| Native Rat Sorbitol Dehydrogenase | Sorbitol dehydrogenase (or SDH) is a cytosolic enzyme. In humans this protein is encoded by the SORD gene. Sorbitol dehydrogenase is an enzyme in carbohydrate metabolism converting sorbitol, the sugar alcohol form of glucose, into fructose. Together with aldose reductase, it provides a way for the body to produce fructose from glucose without using ATP. Sorbitol dehydrogenase uses NAD+ as a cofactor; its reaction is sorbitol + NAD+--> fructose + NADH + H+. A zinc ion is also involved in catalysis. Organs that use it most frequently include the liver and seminal vesicle; it is found in all kinds of organisms from bacteria to humans. A secondary use is the metabolism of dietar...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. Purity: Purified. SDH. Activity: Reported in U/mg. Storage: -20°C. Form: Lyophilized. Source: Rat Liver. Species: Rat. Sorbitol Dehydrogenase; SDH; EC 1.1.1.14; 9028-21-1; L-iditol 2-dehydrogenase; 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: NATE-0667. | |
| Native Rat 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 rat liver can be used for studying the uptake and reduction of a-lipoic acid... NADP-thioredoxin reductase; NADPH-thioredoxin reductase; thioredoxin reductase (NADPH); NADPH2:oxidized thioredoxin oxidoreductase; thioredoxin-disulfide reductase; EC 1.8.1.9; TrxR; 9074-14-0. Enzyme Commission Number: EC 1.8.1.9. CAS No. 9074-14-0. TrxR. Activity: > 100 units/mg protein (Bradford). Storage: -20°C. Form: buffered aqueous glycerol solution; Solution in 50 mM Tris-HCl, pH 7.5, 300 mM NaCl, 1 mM EDTA, and 10% glycerol. Source: Rat liver. Species: Rat. NADP-thioredoxin reductase; NADPH-thioredoxin reductase; thioredoxin reductase (NADPH); NADPH2:oxidized thioredoxin oxidoreductase; thioredoxin-disulfide reductase; EC 1.8.1.9; TrxR; 9074-14-0. Cat No: NATE-0713. | |
| Native Sheep Sorbitol Dehydrogenase | Sorbitol dehydrogenase is an enzyme in carbohydrate metabolism converting sorbitol, the sugar alcohol form of glucose, into fructose. Together with aldose reductase, it provides a way for the body to produce fructose from glucose without using ATP. Sorbitol dehydrogenase uses NAD+ as a cofactor; its reaction is sorbitol + NAD+--> fructose + NADH + H+. A zinc ion is also involved in catalysis. Organs that use it most frequently include the liver and seminal vesicle; it is found in all kinds of organisms from bacteria to humans. A secondary use is the metabolism of dietary sorbitol, though sorbitol is known not to be absorbed as well in the intestine as its related compounds ...rogenase; glucitol dehydrogenase; L-iditol:NAD+ oxidoreductase; NAD+-dependent sorbitol dehydrogenase; NAD+-sorbitol dehydrogenase; L-iditol 2-dehydrogenase. Enzyme Commission Number: EC 1.1.1.14. CAS No. 9028-21-1. SDH. Activity: > 20 units/mg protein. Storage: -20°C. Form: lyophilized powder; Contains maltose. Source: Sheep liver. Species: Sheep. Sorbitol dehydrogenase; SDH; 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; L-iditol 2-dehydrogenase. Cat No: NATE-0668. | |
Our database is helping our users find suppliers everyday.
