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| Product | Description | |
|---|---|---|
| 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase | This enzyme is part of the pathway from urate to (S)-allantoin, which is present in bacteria, plants and animals (but not in humans). Group: Enzymes. Synonyms: OHCU decarboxylase; hpxQ (gene name); PRHOXNB (gene name). Enzyme Commission Number: EC 4.1.1.97. 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-4847; 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase; EC 4.1.1.97; OHCU decarboxylase; hpxQ (gene name); PRHOXNB (gene name). Cat No: EXWM-4847. |  |
| acyl-homoserine-lactone acylase | Acyl-homoserine lactones (AHLs) are produced by a number of bacterial species and are used by them to regulate the expression of virulence genes in a process known as quorum-sensing. Each bacterial cell has a basal level of AHL and, once the population density reaches a critical level, it triggers AHL-signalling which, in turn, initiates the expression of particular virulence genes. Plants or animals capable of degrading AHLs would have a therapeutic advantage in avoiding bacterial infection as they could prevent AHL-signalling and the expression of virulence genes in quorum-sensing bacteria. This quorum-quenching enzyme removes the fatty-acid side chain from the homoserine l...ion, as found in N-(3-oxododecanoyl)-L-homoserine lactone, do not affect this activity. Group: Enzymes. Synonyms: acyl-homoserine lactone acylase; AHL-acylase; AiiD; N-acyl-homoserine lactone acylase; PA2385 protein; quorum-quenching AHL acylase; quorum-quenching enzyme; QuiP. Enzyme Commission Number: EC 3.5.1.97. 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-4489; acyl-homoserine-lactone acylase; EC 3.5.1.97; acyl-homoserine lactone acylase; AHL-acylase; AiiD; N-acyl-homoserine lactone acylase; PA2385 protein; quorum-quenching AHL acylase; quorum-quenching enzyme; QuiP. Cat No: EXWM-4489. | |
| α-N-Acetylgalactosaminidase from Chryseobacterium meningosepticum, Recombinant | 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; α-N-acetylgalactosaminidase; Alpha-N-acetylgalactosaminidase; α-acetylgalactosaminidase; N-acetyl-α-D-galactosaminidase; N-acetyl-α-galactosaminidase; α-NAGAL; α-NAGA; α-GalNAcase. α-NAGA. Mole weight: 47 kDa. Storage: at -20°C. Source: E. coli. Species: Chryseobacterium meningosepticum. EC 3.2.1.49; 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-1259. | |
| Amyloglucosidase, Aspergillus niger | Amyloglucosidase, Aspergillus niger is an enzyme derived from many sources including plants, animals and microorganisms, can be use for industrial production. Amyloglucosidase can be widely used for starch saccharification, brewing and distilling industry [1]. Uses: Scientific research. Group: Natural products. Alternative Names: Amyloglucosidase; 1,4-α-D-Glucan glucohydrolase; Exo-1,4-α-glucosidase. CAS No. 9032-08-0. Pack Sizes: 25 g. Product ID: HY-P2857. |  |
| Aspartate Kinase (Crude Enzyme) | Aspartate kinase (aspartokinase, aspartic kinase) is an enzyme that catalyzes the phosphorylation of the amino acid aspartate. This reaction is the first step in the biosynthesis of three essential amino acids: methionine, lysine, and threonine, known as the "aspartate family". The gene for aspartokinase is present only in microorganisms and plants; it is not present in animals, which must obtain aspartate-family amino acids in their diet. In Escherichia coli, aspartokinase is present as three independently regulated isozymes, each of which is specific to one of the three downstream biochemical pathways. This allows the independent regulation of the rates of methionine, lysin...pression by high concentrations of their end-products. Absence from animals makes these enzymes key targets for new herbicides and biocides and for improvements in nutritional value of crops. This product with the indicated enzyme activity was briefly purified from engineered E. coli. Applications: Agriculture. Group: Enzymes. Synonyms: aspartokinase; AK; β-aspartokinase; aspartic kinase. Enzyme Commission Number: EC 2.7.2.4. CAS No. 9012-50-4. Activity: Undetermined. Appearance: Clear to translucent yellow solution. Storage: at -20 °C or lower, for at least 1 month. Source: E. coli. aspartokinase; AK; β-aspartokinase; aspartic kinase. Pack: 100ml. Cat No: NATE-1827. | |
| betaine-aldehyde dehydrogenase | In many bacteria, plants and animals, the osmoprotectant betaine is synthesized in two steps: (1) choline to betaine aldehyde and (2) betaine aldehyde to betaine. This enzyme is involved in the second step and appears to be the same in plants, animals and bacteria. In contrast, different enzymes are involved in the first reaction. In plants, this reaction is catalysed by EC 1.14.15.7 (choline monooxygenase), whereas in animals and many bacteria it is catalysed by either membrane-bound EC 1.1.99.1 (choline dehydrogenase) or soluble EC 1.1.3.17 (choline oxidase). In some bacteria, betaine is synthesized from glycine through the actions of EC 2.1.1.156 (glycine/sarcosine N-methyltransferase) and EC 2.1.1.157 (sarcosine/dimethylglycine N-methyltransferase). Group: Enzymes. Synonyms: betaine aldehyde oxidase; BADH; betaine aldehyde dehydrogenase; BetB. Enzyme Commission Number: EC 1.2.1.8. CAS No. 9028-90-4. 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-1182; betaine-aldehyde dehydrogenase; EC 1.2.1.8; 9028-90-4; betaine aldehyde oxidase; BADH; betaine aldehyde dehydrogenase; BetB. Cat No: EXWM-1182. | |
| Carboxypeptidase-B from rat, Recombinant | Carboxypeptidase B, recombinant, is intended to use in highly regulated production processes at pharmaceutical companies. Carboxypeptidase B is a widely used metalloprotease, typically isolated from pancreas of different animals, that specifically releases arginine and lysine from the C-terminus of peptides and proteins. Roche has chemically synthesized a gene encoding for the amino acid sequence of the rat Carboxypeptidase B and has transformed the gene into the expression host Pichia pastoris, which expresses the recombinant Carboxypeptidase B as active protease with identical properties compared to the native Carboxypeptidase B. The product is manufactured according to...terial for the production of active pharmaceutical ingredients (api), i.e., insulin. Group: Enzymes. Synonyms: protaminase; pancreatic carboxypeptidase B; tissue carboxypeptidase B; peptidyl-L-lysine [L-arginine] hydrolase. Purity: >85%. CPB1. Activity: >210 U/mg. Stability: At -15 to -25°C within specification range for 24 months. Appearance: Clear, colorless to slightly yellowish solution. Storage: Tris/HCl, 33 mmol/l; ZnCl2, 0.1 mmol/l; pH 7.5-8.5 at +25°C. Source: Pichia pastoris. Species: Rat pancreas. carboxypeptidase B; protaminase; CPB1; pancreatic carboxypeptidase B; tissue carboxypeptidase B; peptidyl-L-lysine [L-arginine]hydrolase; EC 3.4.17.2; 9025-24-5. Cat N | |
| Catalase (Crude Enzyme) | Catalase is a common enzyme found in nearly all living organisms exposed to oxygen (such as bacteria, plants, and animals). It catalyzes the decomposition of hydrogen peroxide to water and oxygen. It is a very important enzyme in protecting the cell from oxidative damage by reactive oxygen species (ROS). Likewise, catalase has one of the highest turnover numbers of all enzymes; one catalase molecule can convert approximately 5 million molecules of hydrogen peroxide to water and oxygen each minute. This product with the indicated enzyme activity was briefly purified from engineered E. coli. Applications: Medicine; synthesis; analysis; biotechnology; industry. Group: Enzymes. Synonyms: hydrogen-peroxide:hydrogen-peroxide oxidoreductase. Enzyme Commission Number: EC 1.11.1.6. CAS No. 9001-5-2. CAT. Activity: Undetermined. Appearance: Clear to translucent yellow solution. Storage: at -20 °C or lower, for at least 1 month. Source: E. coli. hydrogen-peroxide:hydrogen-peroxide oxidoreductase. Pack: 100ml. Cat No: NATE-1795. | |
| choline monooxygenase | The spinach enzyme, which is located in the chloroplast, contains a Rieske-type [2Fe-2S] cluster, and probably also a mononuclear Fe centre. Requires Mg2+. Catalyses the first step of glycine betaine synthesis. In many bacteria, plants and animals, betaine is synthesized in two steps: (1) choline to betaine aldehyde and (2) betaine aldehyde to betaine. Different enzymes are involved in the first reaction. In plants, the reaction is catalysed by this enzyme whereas in animals and many bacteria it is catalysed by either membrane-bound EC 1.1.99.1 (choline dehydrogenase) or soluble EC 1.1.3.17 (choline oxidase). The enzyme involved in the second step, EC 1.2.1.8 (betaine-aldehyde dehydrogenase), appears to be the same in plants, animals and bacteria. In some bacteria, betaine is synthesized from glycine through the actions of EC 2.1.1.156 (glycine/sarcosine N-methyltransferase) and EC 2.1.1.157 (sarcosine/dimethylglycine N-methyltransferase). Group: Enzymes. Enzyme Commission Number: EC 1.14.15.7. CAS No. 118390-76-4. 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-0950; choline monooxygenase; EC 1.14.15.7; 118390-76-4. Cat No: EXWM-0950. | |
| diacylglycerol kinase (CTP) | Requires Ca2+ or Mg2+ for activity. Involved in synthesis of membrane phospholipids and the neutral lipid triacylglycerol. Unlike the diacylglycerol kinases from bacteria, plants, and animals [cf. EC 2.7.1.107, diacylglycerol kinase (ATP)], the enzyme from Saccharomyces cerevisiae utilizes CTP. The enzyme can also use dCTP, but not ATP, GTP or UTP. Group: Enzymes. Synonyms: DAG kinase; CTP-dependent diacylglycerol kinase; diglyceride kinase (ambiguous); DGK1 (gene name); diacylglycerol kinase (CTP dependent). Enzyme Commission Number: EC 2.7.1.174. 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-3005; diacylglycerol kinase (CTP); EC 2.7.1.174; DAG kinase; CTP-dependent diacylglycerol kinase; diglyceride kinase (ambiguous); DGK1 (gene name); diacylglycerol kinase (CTP dependent). Cat No: EXWM-3005. | |
| dihydrofolate reductase | The enzyme from animals and some micro-organisms also slowly reduces folate to 5,6,7,8-tetrahydrofolate. Group: Enzymes. Synonyms: tetrahydrofolate dehydrogenase; DHFR; pteridine reductase:dihydrofolate reductase; dihydrofolate reductase:thymidylate synthase; thymidylate synthetase-dihydrofolate reductase; folic acid reductase; folic reductase; dihydrofolic acid reductase; dihydrofolic reductase; 7,8-dihydrofolate reductase; NADPH-dihydrofolate reductase. Enzyme Commission Number: EC 1.5.1.3. CAS No. 9002-3-3. Dihydrofolate Reductase. 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-1511; dihydrofolate reductase; EC 1.5.1.3; 9002-03-3; tetrahydrofolate dehydrogenase; DHFR; pteridine reductase:dihydrofolate reductase; dihydrofolate reductase:thymidylate synthase; thymidylate synthetase-dihydrofolate reductase; folic acid reductase; folic reductase; dihydrofolic acid reductase; dihydrofolic reductase; 7,8-dihydrofolate reductase; NADPH-dihydrofolate reductase. Cat No: EXWM-1511. | |
| D(+)-Raffinose Pentahydrate | Raffinose is a trisaccharide composed of galactose, glucose, and fructose. It can be found in beans, cabbage, brussels sprouts, broccoli, asparagus, other vegetables, and whole grains. Raffinose can be hydrolyzed to D-galactose and sucrose by the enzyme α-galactosidase (α-GAL), an enzyme not found in the human digestive tract. α-GAL also hydrolyzes other α-galactosides such as stachyose, verbascose, and galactinol, if present. The enzyme does not cleave β-linked galactose, as in lactose.The raffinose family of oligosaccharides (RFOs) are alpha-galactosyl derivatives of sucrose, and the most common are the trisaccharide raffinose, the tetrasaccharide stachyose, and the pentasaccharide verbascose. RFOs are almost ubiquitous in the plant kingdom, being found in a large variety of seeds from many different families, and they rank second only to sucrose in abundance as soluble carbohydrates.Humans and other monogastric animals (pigs and poultry) do not possess the α-GAL enzyme to break down RFOs and these oligosaccharides pass undigested through the stomach and upper intestine. In the lower intestine, they are fermented by gas-producing bacteria that do possess the α-GAL enzyme and make carbon dioxide, methane or hydrogenleading to the flatulence commonly associated with eating beans and other vegetables. α-GAL is present in digestive aids such as the product Beano.Pr |  |
| Enzyme blend for eliminating obnoxious odors of companion animals | A mix of enzymes, plant extracts and buffers designed to eliminate obnoxious odors released from the litter of cats, dogs, birds, rabbits and other companion animals. Applications: Animal. Group: Enzymes. Synonyms: eliminating obnoxious odors; companion animals; eliminate obnoxious odors; cats; dogs; birds; rabbits; Waste Management Enzymes; Waste Enzymes. Waste Management. Appearance: inquire. digesting waste oils; digest grease?fats and oils; Waste Management Enzymes; digesting; digesting waste oils; waste oils. Pack: 25kg/paper barrel (powder form), 30kg/polyster barrel (liquid form). Cat No: WME-2716. | |
| glutamyl-tRNA reductase | This enzyme forms part of the pathway for the biosynthesis of 5-aminolevulinate from glutamate, known as theC5 pathway.The route shown in the diagram is used in most eubacteria, and in all archaebacteria, algae and plants. However, in the α-proteobacteria, EC 2.3.1.37, 5-aminolevulinate synthase, is used in an alternative route to produce the product 5-aminolevulinate from succinyl-CoA and glycine. This route is found in the mitochondria of fungi and animals, organelles that are considered to be derived from an endosymbiotic α-proteobacterium. Although higher plants do not possess EC 2.3.1.37, the protistan Euglena gracilis possesses both the C5 pathway and EC 2.3.1.37. Group: Enzymes. Enzyme Commission Number: EC 1.2.1.70. CAS No. 119940-26-0. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1172; glutamyl-tRNA reductase; EC 1.2.1.70; 119940-26-0. Cat No: EXWM-1172. | |
| interstitial collagenase | The enzyme takes its name from substrates of the interstitial collagen group - types I, II and III, all of which are cleaved in the helical domain. However, α-macroglobulins are cleaved much more rapidly. The enzyme is widely distributed in vertebrate animals. Type example of peptidase family M10. Group: Enzymes. Synonyms: vertebrate collagenase; matrix metalloproteinase 1. Enzyme Commission Number: EC 3.4.24.7. CAS No. 9001-12-1. Matrix Metalloproteinase. 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-4353; interstitial collagenase; EC 3.4.24.7; 9001-12-1; vertebrate collagenase; matrix metalloproteinase 1. Cat No: EXWM-4353. | |
| Lactate Dehydrogenase from Chicken Heart, Recombinant | 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. 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. Purity: > 96% (SDS-PAGE). LDH. Activity: >90%. (>200U/mL). Storage: -20°C. Form: Lyophilized. Source: E. coli. Species: Chicken Heart. 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-0383. | |
| Lactic Dehydrogenase, Recombinant | 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. Group: Enzymes. Synonyms: EC 1.1.1.27; 9001-60-9; lactic acid dehydrogenase; L (+)-nLDH; L-(+)-lactate dehydrogenase; L-lactic dehydrogenase; L-lactic acid dehydrogenase; lactate dehydrogenase; lactate dehydrogenase NAD-dependent; lactic dehydrogenase; NAD-lactate dehydrogenase; L-lactate dehydrogenase; (S)-Lactate:NAD+ oxidoreductase; L-LDH; LAD; LD; LDH; Lactate. Enzyme Commission Number: EC 1.1.1.27. CAS No. 9001-60-9. LDH. Activity: >90%. (>200U/mL). Source: E. coli. EC 1.1.1.27; 9001-60-9; lactic acid dehydrogenase; L (+)-nLDH; L-(+)-lactate dehydrogenase; L-lactic dehydrogenase; L-lactic acid dehydrogenase; lactate dehydrogenase; lactate dehydrogenase NAD-dependent; lactic dehydrogenase; NAD-lactate dehydrogenase; L-lactate dehydrogenase; (S)-Lactate:NAD+ oxidoreductase; L-LDH; LAD; LD; LDH; Lactate. Cat No: NATE-0381. | |
| L-iditol 2-dehydrogenase | This enzyme is widely distributed and has been described in archaea, bacteria, yeast, plants and animals. It acts on a number of sugar alcohols, including (but not limited to) L-iditol, D-glucitol, D-xylitol, and D-galactitol. Enzymes from different organisms or tissues display different substrate specificity. The enzyme is specific to NAD+ and can not use NADP+. Group: Enzymes. Synonyms: polyol dehydrogenase; sorbitol dehydrogenase; L-iditol:NAD+ 5-oxidoreductase; L-iditol (sorbitol) dehydrogenase; glucitol dehydrogenase; L-iditol:NAD+ oxidoreductase; NAD+-dependent sorbitol dehydrogenase; NAD+-sorbitol dehydrogenase. Enzyme Commission Number: EC 1.1.1.14. CAS No. 9028-21-1. SDH. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-0043; L-iditol 2-dehydrogenase; EC 1.1.1.14; 9028-21-1; polyol dehydrogenase; sorbitol dehydrogenase; L-iditol:NAD+ 5-oxidoreductase; L-iditol (sorbitol) dehydrogenase; glucitol dehydrogenase; L-iditol:NAD+ oxidoreductase; NAD+-dependent sorbitol dehydrogenase; NAD+-sorbitol dehydrogenase. Cat No: EXWM-0043. | |
| L-Lactate Dehydrogenase (Crude Enzyme) | Lactate dehydrogenase (LDH or LD) is an enzyme found in nearly all living cells (animals, plants, and prokaryotes). LDH catalyzes the conversion oflactate to pyruvic acid and back, as it converts NAD + to NADH and back. A dehydrogenase is an enzyme that transfers a hydride from one molecule to another. LDH is expressed extensively in body tissues, such as blood cells and heart muscle. Because it is released during tissue damage, it is a marker of common injuries and disease such as heart failure. This product with the indicated enzyme activity was briefly purified from engineered E. coli. Applications: Medicine; synthesis; biotechnology; drug development. Group: Enzymes. Synonyms: lactic acid dehydrogenase; L(+)-nLDH; L-(+)-lactate dehydrogenase; L-lactic dehydrogenase; L-lactic acid dehydrogenase; lactate dehydrogenase; lactate dehydrogenase NAD-dependent; lactic dehydrogenase; NAD. Enzyme Commission Number: EC 1.1.1.27. CAS No. 9001-60-9. LDH. Activity: Undetermined. Appearance: Clear to translucent yellow solution. Storage: at -20 °C or lower, for at least 1 month. Source: E. coli. lactic acid dehydrogenase; L(+)-nLDH; L-(+)-lactate dehydrogenase; L-lactic dehydrogenase; L-lactic acid dehydrogenase; lactate dehydrogenase; lactate dehydrogenase NAD-dependent; lactic dehydrogenase; NAD-lactate dehydrogenase. Pack: 100ml. Cat No: NATE-1793. | |
| L-Lactate Dehydrogenase from Porcine, Recombinant | 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: High purity l-lactate dehydrogenase (porcine) for use in research, biochemical enzyme assays and in vitro diagnostic analysis. Group: Enzymes. Synonyms: EC 1.1.1.27; 9001-60-9; lactic acid dehydrogenase; L (+)-nLDH; L- (+)-lactate dehydrogenase; L-lactic dehydrogenase; L-lactic acid dehydrogenase; lactate dehydrogenase; lactate dehydrogenase NAD-dependent; lactic dehydrogenase; NAD-lactate dehydrogenase; L-lactate dehydrogenase; (S)-Lactate:NAD+ oxidoreductase; L-LDH; LAD; LD; Lactate. Enzyme Commission Number: EC 1.1.1.27. CAS No. 9001-60-9. Activity: ~ 330 U/mg. Storage: > 2 years at 4°C. Form: In 3.2 M ammonium sulphate. Source: Porcine. EC 1.1.1.27; 9001-60-9; lactic acid dehydrogenase; L (+)-nLDH; L- (+)-lactate dehydrogenase; L-lactic dehydrogenase; L-lactic acid dehydrogenase; lactate dehydrogenase; lactate dehydrogenase NAD-dependent; lactic dehydrogenase; NAD-lactate dehydrogenase; L-lactate dehydrogenase; (S)-Lactate:NAD+ oxidoreductase; L-LDH; LAD; LD; Lactate. Cat No: NATE-1105. | |
| L-Lactic Dehydrogenase from Bacillus stearothermophilus, Recombinant | 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. Recombinant, expressed in e. coli, lyophilized powder, > 200 units/mg protein (lowry). 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: > 200 units/mg protein (Lowry). Stability: 2-8°C. Form: lyophilized powder. Source: E. coli. Species: Bacillus stearothermophilus. 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-0382. | |
| NAD+ diphosphatase | This enzyme, described from plants, animals, and bacteria, can act on both reduced and oxidized forms of its substrate, although enzymes from different organisms have different preferences. Also acts on other dinucleotides, including NADP(H), FAD(H2), and the thionicotinamide analogues of NAD+ and NADP+. Group: Enzymes. Synonyms: NPY1 (gene name); nudC (gene name); NUDT7 (gene name); nicotinamide adenine dinucleotide pyrophosphatase; NADP pyrophosphatase; NADH pyrophosphatase; NAD+ phosphohydrolase. Enzyme Commission Number: EC 3.6.1.22. CAS No. 37289-33-1. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4606; NAD+ diphosphatase; EC 3.6.1.22; 37289-33-1; NPY1 (gene name); nudC (gene name); NUDT7 (gene name); nicotinamide adenine dinucleotide pyrophosphatase; NADP pyrophosphatase; NADH pyrophosphatase; NAD+ phosphohydrolase. Cat No: EXWM-4606. | |
| Native Aspergillus melleus Proteinase | A protease (also called peptidase or proteinase) is any enzyme that performs proteolysis, that is, begins protein catabolism by hydrolysis of the peptide bonds that link amino acids together in a polypeptide chain. Proteases have evolved multiple times, and different classes of protease can perform the same reaction by completely different catalytic mechanisms. Proteases can be found in animals, plants, bacteria, archaea and viruses. Applications: Proteinase is an enzyme used to break down proteins by hydrolyzing peptide bonds. proteinase is used to degrade proteins, to study proteinase inhibitors and to study thermal inactivation kinetics. proteinase is used in nucleic acid isolation procedures in incubations. it is used to study proteinase-activated receptors, such as the transducers of proteinase-mediated signaling in inflammation and the immune response. it is from aspergillus melleus and has been used to non-specifically degraded xylanase from streptomyces halstedii. Group: Enzymes. Synonyms: Protease; peptidase; proteinase; 9001-92-7. CAS No. 9001-92-7. Proteinase. Activity: > 3 units/mg solid. Storage: 2-8°C. Source: Aspergillus melleus. Protease; peptidase; proteinase; 9001-92-7. Cat No: NATE-0638. | |
| 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 L-Lactic Dehydrogenase | 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: For use in enzymatic determination of lactate or pyruvate. Group: Enzymes. Synonyms: EC 1.1.1.27; 9001-60-9; lactic acid dehydrogenase; L (+)-nL. Enzyme Commission Number: EC 1.1.1.27. CAS No. 9001-60-9. LDH. Activity: >90%. (>200U/mL). Storage: 2-8°C. Form: Type I, Suspension in 2.2 M ammonium sulfate; Type II, buffered aqueous glycerol solution, Solution in 50% glycerol containing 0.025 M potassium phosphate buffer, pH 7.5; Type III, ammonium sulfate suspension, Crystalline suspension in 2.1 M (NH4)2SO4 solution, pH 6.0; Type IV, buffered aqueous glycerol solution, Solution in 50% glycerol containing 0.025 M potassium phosphate buffer, pH 7.5. Source: Bovine heart. Species: Bovine. EC 1.1.1.27; 9001-60-9; lactic acid dehydrogenase; L (+)-nLDH; L-(+)-lactate dehydrogenase; L-lactic dehydrogenase; L-lactic acid dehydrogenase; lactate dehydrogenase; lactate dehydrogenase NAD-dependent; lactic dehydrogenase; NAD-lactate dehydrogenase; L-lactate dehydrogenase; (S)-Lactate:NAD+ oxidoreductase; L-LDH; LAD; LD; Lactate. Cat No: NATE-0409. | |
| Native Bovine Protease | A protease (also called peptidase or proteinase) is any enzyme that performs proteolysis, that is, begins protein catabolism by hydrolysis of the peptide bonds that link amino acids together in a polypeptide chain. Proteases have evolved multiple times, and different classes of protease can perform the same reaction by completely different catalytic mechanisms. Proteases can be found in animals, plants, bacteria, archaea and viruses. Derived from new zealand-sourced pancreas. Applications: Protease is an enzyme used to break down proteins by hydrolyzing peptide bonds. protease is used to degrade proteins, to study protease inhibitors and to study thermal inactivation kinetics. this product is from bovine pancreas. protease from bovine pancrease (type i) has been used for the extraction of hemicellulose. Group: Enzymes. Synonyms: Protease; peptidase; proteinase; 9001-92-7. CAS No. 9001-92-7. Protease. Activity: > 5 units/mg solid. Storage: -20°C. Source: bovine pancreas. Species: Bovine. Protease; peptidase; proteinase; 9001-92-7. Cat No: NATE-0628. | |
| 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 L-Lactic Dehydrogenase | 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. Group: Enzymes. Synonyms: EC 1.1.1.27; 9001-60-9; lactic acid dehydrogenase; L (+)-nLDH; L-(+)-lactate dehydrogenase; L-lactic dehydrogenase; L-lactic acid dehydrogenase; lactate dehydrogenase; lactate dehydrogenase NAD-dependent; lactic dehydrogenase; NAD-lactate dehydrogenase; L-lactate dehydrogenase; (S)-Lactate:NAD+ oxidoreductase; L-LDH; LAD; LD; Lactate. Enzyme Commission Number: EC 1.1.1.27. CAS No. 9001-60-9. LDH. Activity: >90%. (>200U/mL). Storage: 2-8°C. Form: ammonium sulfate suspension; Crystalline suspension in 1.3 M (NH4)2SO4, pH 6.0. Source: Chicken heart. Species: Chicken. EC 1.1.1.27; 9001-60-9; lactic acid dehydrogenase; L (+)-nLDH; L-(+)-lactate dehydrogenase; L-lactic dehydrogenase; L-lactic acid dehydrogenase; lactate dehydrogenase; lactate dehydrogenase NAD-dependent; lactic dehydrogenase; NAD-lactate dehydrogenase; L-lactate dehydrogenase; (S)-Lactate:NAD+ oxidoreductase; L-LDH; LAD; LD; Lactate. Cat No: NATE-0411. | |
| Native Human Lactate Dehydrogenase | 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 clinical 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 Cardiac Tissue. 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-0380. | |
| Native Human Lactate Dehydrogenase 1 | 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 clinical 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 Cardiac Tissue. 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-0384. | |
| Native Human Lactate Dehydrogenase 2 | 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 clinical 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 Cardiac Tissue. 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-0386. | |
| Native Human Lactate Dehydrogenase 3 | 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 Cardiac Tissue. 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-0388. | |
| 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 Lactate Dehydrogenase from Thermophillic bacteria | 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 test and biosensors; nadh recycling. this enzyme is a potential candidate for biocatalysis, suitable for pharmaceutical development / manufacturing. Group: Enzymes. Synonyms: Lactate dehydrogenase; EC 1.1.1.27; LDH; LD. Enzyme Commission Number: EC 1.1.1.27. CAS No. 9001-60-9. LDH. Storage: Store at -20°C. Form: Frozen Liquid. Source: Thermophillic bacteria. Lactate dehydrogenase; EC 1.1.1.27; LDH; LD. Cat No: DIA-400. | |
| Native Microorganism D-lactate dehydrogenase | 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: This enzyme is useful for enzymatic determination of numerous metabolites, e.g.atp, adp, glucose, creatinine, pyruvate, lactate and glycerol, and of enzyme activities, e.g.gpt, pk and cpk when coupled with the related enzymes. Group: Enzymes. Synonyms: Lactate dehydrogenase; EC 1.1.1.27; LDH; LD. Enzyme Commission Number: EC 1.1.1.27. CAS No. 9001-60-9. Activity: 400U/mg-solid or more. Appearance: White amorphous powder, lyophilized. Storage: Store at -20°C. Form: Freeze dried powder. Source: Microorganism. Lactate dehydrogenase; EC 1.1.1.27; LDH; LD. Cat No: DIA-207. | |
| Native Porcine heart Lactate dehydrogenase | 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: This enzyme is useful for enzymatic determination of numerous metabolites, e.g.atp, adp, glucose, creatinine, pyruvate, lactate and glycerol, and of enzyme activities, e.g.gpt, pk and cpk when coupled with the related enzymes. Group: Enzymes. Synonyms: Lactate dehydrogenase; EC 1.1.1.27; LDH; LD. Enzyme Commission Number: EC 1.1.1.27. CAS No. 9001-60-9. LDH. Mole weight: 115 kDa±6,500. Activity: Grade? 2,000U/ml or more. Stability: Stable at 5°C for at least one year. Appearance: Crystalline suspension in 1.6M ammonium sulfate solution. Source: Porcine heart. Species: Porcine. Lactate dehydrogenase; EC 1.1.1.27; LDH; LD. Cat No: DIA-206. | |
| Native Porcine Lactate Dehydrogenase | 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; manufacturing. Group: Enzymes. Synonyms: Lactate dehydrogenase; EC 1.1.1.27; LDH; LD. Enzyme Commission Number: EC 1.1.1.27. CAS No. 9001-60-9. LDH. Mole weight: ~136,700. Activity: > 100 U/mg. Stability: 2 years. Storage: Store at -20°C. Form: Lyophilized. Source: Porcine Muscle. Species: Porcine. Lactate dehydrogenase; EC 1.1.1.27; LDH; LD. Cat No: NATE-0964. | |
| Native Porcine L-Lactate Dehydrogenase | 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. Dehydrogenase that catalyzes the interconversion of specific for l(+)-lactate to pyruvate. apply this ready-to-use enzyme directly in your diagnostic test. rely on the proven diagnostic quality of this product. Applications: Use l-lactate dehydrogenase in a variety of diagnostic tests for the removal of pyruvate in determinations working with nadh (i.e., triglycerides, lipase,...ehydrogenase; (S)-Lactate:NAD+ oxidoreductase; L-LDH; LAD; LD; Lactate. CAS No. 9001-60-9. LDH. Activity: >550 U/mg. Stability: At +2 to +8°C within specification range for 12 months. Appearance: White suspension in ammonium sulfate, 3.2 mol/l; Tris, 10 mmol/l, pH approximately 6.5. Source: Porcine muscle. Species: Porcine. EC 1.1.1.27; 9001-60-9; lactic acid dehydrogenase; L (+)-nLDH; L-(+)-lactate dehydrogenase; L-lactic dehydrogenase; L-lactic acid dehydrogenase; lactate dehydrogenase; lactate dehydrogenase NAD-dependent; lactic dehydrogenase; NAD-lactate dehydrogenase; L-lactate dehydrogenase; (S)-Lactate:NAD+ oxidoreductase; L-LDH; LAD; LD; Lactate. Cat No: NATE-0982. | |
| Native Porcine L-Lactic Dehydrogenase | 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. Group: Enzymes. Synonyms: EC 1.1.1.27; 9001-60-9; lactic acid dehydrogenase; L (+)-nLDH; L-(+)-lactate dehydrogenase; L-lactic dehydrogenase; L-lactic acid dehydrogenase; lactate dehydrogenase; lactate dehydrogenase NAD-dependent; lactic dehydrogenase; NAD-lactate dehydrogenase; L-lactate dehydrogenase; (S)-Lactate:NAD+ oxidoreductase; L-LDH; LAD; LD; Lactate. Enzyme Commission Number: EC 1.1.1.27. CAS No. 9001-60-9. LDH. Activity: >90%. (>200U/mL). Storage: 2-8°C. Form: ammonium sulfate suspension; Suspension in ammonium sulfate and 0.1 M potassium phosphate, pH 7.0. Source: Porcine heart. Species: Porcine. EC 1.1.1.27; 9001-60-9; lactic acid dehydrogenase; L (+)-nLDH; L-(+)-lactate dehydrogenase; L-lactic dehydrogenase; L-lactic acid dehydrogenase; lactate dehydrogenase; lactate dehydrogenase NAD-dependent; lactic dehydrogenase; NAD-lactate dehydrogenase; L-lactate dehydrogenase; (S)-Lactate:NAD+ oxidoreductase; L-LDH; LAD; LD; Lactate. Cat No: NATE-0412. | |
| Native Rabbit Lactate Dehydrogenase | 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. Group: Enzymes. Synonyms: Lactate dehydrogenase; EC 1.1.1.27; LDH; LD. Enzyme Commission Number: EC 1.1.1.27. CAS No. 9001-60-9. LDH. Mole weight: 140 kDa. Activity: > 250 units per mg protein. Source: Rabbit Muscle. Species: Rabbit. Lactate dehydrogenase; EC 1.1.1.27; LDH; LD. Cat No: DIA-268. | |
| Native Rabbit L-Lactic Dehydrogenase | 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. Lactic dehydrogenase (ldh) has a total molecular weight of 140 kda and is composed of 4 subunits which are designated m subunit (muscle) and h subunit (heart). these subunits may be mixed in any of 5 combinations (m4, m3h1, m2h2, mh3, and h4). skeletal muscle contains ldh that is predominately m4 with some small amounts of m3h and traces of h2h2. the h and m subunits are quite ...reductase; L-LDH; LAD; LD; Lactate. Enzyme Commission Number: EC 1.1.1.27. CAS No. 9001-60-9. LDH. Activity: >90%. (>200U/mL). Storage: 2-8°C. Form: Type I, lyophilized powder; Type II, ; Type III, ammonium sulfate suspension, Crystalline suspension in 3.2 M (NH4)2SO4 solution, pH 6.0. Source: Rabbit muscle. Species: Rabbit. EC 1.1.1.27; 9001-60-9; lactic acid dehydrogenase; L (+)-nLDH; L-(+)-lactate dehydrogenase; L-lactic dehydrogenase; L-lactic acid dehydrogenase; lactate dehydrogenase; lactate dehydrogenase NAD-dependent; lactic dehydrogenase; NAD-lactate dehydrogenase; L-lactate dehydrogenase; (S)-Lactate:NAD+ oxidoreductase; L-LDH; LAD; LD; Lactate. Cat No: NATE-0413. | |
| Native Rhizopus sp. Protease | A protease (also called peptidase or proteinase) is any enzyme that performs proteolysis, that is, begins protein catabolism by hydrolysis of the peptide bonds that link amino acids together in a polypeptide chain. Proteases have evolved multiple times, and different classes of protease can perform the same reaction by completely different catalytic mechanisms. Proteases can be found in animals, plants, bacteria, archaea and viruses. Acidic protease exhibits both proteolytic and lipolytic activities. stable in the acid range of ph 3-5. ph optimum is 3.0. Applications: Protease from rhizopus spp. has been used in a study to assess the amino acid sequences near the amino termini using automated edman degradation. it has also been used in a study to investigate inactivation of the enzyme by reaction with diazoacetyl-dl-norleucine methyl ester in the presence of cupric acetate. Group: Enzymes. Synonyms: Protease; peptidase; proteinase; 9001-92-7. CAS No. 9001-92-7. Protease. Activity: > 0.2 unit/mg solid. Storage: 2-8°C. Form: Supplied as a powder containing dextrin as a stabilizer. Source: Rhizopus sp. Protease; peptidase; proteinase; 9001-92-7. Cat No: NATE-0629. | |
| Native Saccharomyces cerevisiae Alcohol Dehydrogenase | Alcohol dehydrogenases (ADH) are a group of dehydrogenase enzymes that occur in many organisms and facilitate the interconversion between alcohols and aldehydes or ketones with the reduction of nicotinamide adenine dinucleotide (NAD+ to NADH). In Humans and many other animals, they serve to break down alcohols that otherwise are toxic, and they also participate in geneRation of useful aldehyde, ketone, or alcohol groups during biosynthesis of various metabolites. In yeast, plants, and many bacteria, some alcohol dehydrogenases catalyze the opposite reaction as part of fermentation to ensure a constant supply of NAD+. Applications: Alcohol dehydrogenase from sacchar...dehydrogenase; NADH-alcohol dehydrogenase; NADH-aldehyde dehydrogenase; primary alcohol dehydrogenase; yeast alcohol dehydrogenase; EC 1.1.1.1. Enzyme Commission Number: EC 1.1.1.1. CAS No. 9031-72-5. Activity: > 300 units/mg protein. Storage: -20°C. Form: Solids containing <2% Citrate buffer salts. Source: Saccharomyces cerevisiae. aldehyde reductase; ADH; alcohol dehydrogenase (NAD); aliphatic alcohol dehydrogenase; ethanol dehydrogenase; NAD-dependent alcohol dehydrogenase; NAD-specific aromatic alcohol dehydrogenase; NADH-alcohol dehydrogenase; NADH-aldehyde dehydrogenase; primary alcohol dehydrogenase; yeast alcohol dehydrogenase; EC 1.1.1.1. Cat No: NATE-0035. | |
| Native Staphylococcus aureus Nuclease micrococcal | Micrococcal Nuclease is an endo-exonuclease that preferentially digests single-stranded nucleic acids. The rate of cleavage is 30 times greater at the 5' side of A or T than at G or C and results in the production of mononucleotides and oligonucleotides with terminal 3'-phosphates. The enzyme is also active against double-stranded DNA and RNA and all sequences will be ultimately cleaved. Applications: Nuclease from staphyl oc occus aureus has been used in a study to assess coagulase and heat-resistant strains found in animals. it has also been used in a study to investigate the expression characteristic of two genes in s. aureus that encode two thermostable nucleases. Group: Enzymes. Synonyms: Micrococcal Nuclease; EC 3.1.31.1; spleen endonuclease; thermonuclease; nuclease T; micrococcal endonuclease; nuclease T'; staphylococcal nucle. Enzyme Commission Number: EC 3.1.31.1. CAS No. 9013-53-0. MNase. Activity: 100-300 units/mg protein. Storage: -20°C. Source: Staphylococcus aureus. Micrococcal Nuclease; EC 3.1.31.1; spleen endonuclease; thermonuclease; nuclease T; micrococcal endonuclease; nuclease T'; staphylococcal nuclease; spleen phosphodiesterase; Staphylococcus aureus nuclease; Staphylococcus aureus nuclease B; ribonucleate (deoxynucleate) 3'-nucleotidohydrolase; 9013-53-0; Endonuclease micrococcal; MNase. Cat No: NATE-0452. | |
| nitric-oxide synthase (NADPH) | Binds FAD, FMN, heme (iron protoporphyrin IX) and tetrahydrobiopterin. This eukaryotic enzyme, which is found in plants and animals, consists of oxygenase and reductase domains that are linked via a regulatory calmodulin-binding domain. Upon calcium-induced calmodulin binding, the reductase and oxygenase domains form a complex, allowing electrons to flow from NADPH via FAD and FMN to the active center. May produce superoxide under certain conditions. cf. EC 1.14.13.165, nitric-oxide synthase [NAD(P)H dependent]. Group: Enzymes. Synonyms: nitric oxide synthetase; endothelium-derived relaxation factor-forming enzyme; endothelium-derived relaxing factor synthase; NO synthase; NADPH-diaphorase. Enzyme Commission Number: EC 1.14.13.39. CAS No. 125978-95-2. NOSs. 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-0846; nitric-oxide synthase (NADPH); EC 1.14.13.39; 125978-95-2; nitric oxide synthetase; endothelium-derived relaxation factor-forming enzyme; endothelium-derived relaxing factor synthase; NO synthase; NADPH-diaphorase. Cat No: EXWM-0846. | |
| nitric-oxide synthase [NAD(P)H] | Binds heme (iron protoporphyrin IX) and tetrahydrobiopterin. Most of the bacterial and archaeal enzymes consist of only an oxidase domain and function together with bacterial ferredoxins. The enzyme from the Δ-proteobacterium Sorangium cellulosum also includes a reductase domain that binds FAD, FMN and a [2Fe-2S] cluster. The similar enzymes from plants and animals use only NADPH as acceptor (cf. EC 1.14.13.39). Group: Enzymes. Synonyms: nitric oxide synthetase; NO synthase. Enzyme Commission Number: EC 1.14.13.165. 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-0764; nitric-oxide synthase [NAD(P)H]; EC 1.14.13.165; nitric oxide synthetase; NO synthase. Cat No: EXWM-0764. | |
| Nitrilase (Crude Enzyme) | Nitrilase enzymes catalyse the hydrolysis of nitriles to carboxylic acids and ammonia, without the formation of "free" amide intermediates. Nitrilases are involved in natural product biosynthesis and post translational modifications in plants, animals, fungi and certain prokaryotes. Nitrilases can also be used as catalysts in preparative organic chemistry. Among others, nitrilases have been used for the resolution of racemic mixtures. Nitrilase should not be confused with nitrile hydratase (nitrile hydro-lyase; EC 4. 2. 1. 84) which hydrolyses nitriles to amides. Nitrile hydratases are almost invariably co-expressed with an amidase, which converts the amide to the carboxylic acid, consequently it can sometimes be difficult to distinguish nitrilase activity from nitrile hydratase plus amidase activity. This product with the indicated enzyme activity was briefly purified from engineered E. coli. Applications: Synthesis; industry. Group: Enzymes. Synonyms: acetonitrilase; benzonitrilase. Enzyme Commission Number: EC 3.5.5.1. CAS No. 9024-90-2. Nitrilase. Activity: Undetermined. Appearance: Clear to translucent yellow solution. Storage: at -20 °C or lower, for at least 1 month. Source: E. coli. acetonitrilase; benzonitrilase. Pack: 100ml. Cat No: NATE-1842. | |
| Oxalacetic Acid (Oxaloacetic acid) | A four carbon dicarboxylic acid that is an intermediate in the citric acid cycle and glucogenesis. It has been shown to inhibit succinate dehydrogenase. Oxaloacetic acid, in the form of its conjugate base oxaloacetate, is a metabolic intermediate in many processes that occur in animals. It takes part in the: gluconeogenesis, urea cycle, glyoxylate cycle, amino acid synthesis, fatty acid synthesis and citric acid cycle. Gluconeogenesis[1] is a metabolic pathway consisting of a series of eleven enzyme-catalyzed reactions, resulting in the generation of glucose from non-carbohydrates substrates. The beginning of this process takes place in the mitochondrial matrix, where pyruvate molecules are found. A pyruvate molecule is carboxylated by a pyruvate carboxylase enzyme, activated by a molecule each of ATP and water. This reaction results in the formation of oxaloacetate. NADH reduces oxaloacetate to malate. This transformation is needed to transport the molecule out of the mitochondria. On Group: Biochemicals. Alternative Names: Oxobutanedioic Acid; Oxalacetic Acid; 2-Ketosuccinic acid; 2-Oxobutanedioic acid; 2-Oxosuccinic Acid; Ketosuccinic Acid; NSC 284205; NSC 77688; OAA; Oxaloacetic Acid; Oxaloethanoic Acid; Oxosuccinic Acid; α-Ketosuccinic Acid. Grades: Reagent Grade. CAS No. 328-42-7. Pack Sizes: 25g, 50g, 100g, 250g. Molecular Formula: C?H?O?, Molecular Weight: 132.07. US Biological Life Sciences. |  Worldwide |
| pyroglutamyl-peptidase I | A cysteine peptidase, known from bacteria, plants and animals. The enzyme from bacterial sources is used in protein sequencing, and is the type example of peptidase family C15. Group: Enzymes. Synonyms: 5-oxoprolyl-peptidase; pyrase; pyroglutamate aminopeptidase; pyroglutamyl aminopeptidase; L-pyroglutamyl peptide hydrolase; pyrrolidone-carboxyl peptidase; pyrrolidone-carboxylate peptidase; pyrrolidonyl peptidase; L-pyrrolidonecarboxylate peptidase; pyroglutamidase; pyrrolidonecarboxylyl peptidase. Enzyme Commission Number: EC 3.4.19.3. CAS No. 9075-21-2. Pyrase. 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-4088; pyroglutamyl-peptidase I; EC 3.4.19.3; 9075-21-2; 5-oxoprolyl-peptidase; pyrase; pyroglutamate aminopeptidase; pyroglutamyl aminopeptidase; L-pyroglutamyl peptide hydrolase; pyrrolidone-carboxyl peptidase; pyrrolidone-carboxylate peptidase; pyrrolidonyl peptidase; L-pyrrolidonecarboxylate peptidase; pyroglutamidase; pyrrolidonecarboxylyl peptidase. Cat No: EXWM-4088. | |
| selenocysteine lyase | A pyridoxal-phosphate protein. Dithiothreitol or 2-mercaptoethanol can act as the reducing agent in the reaction. The enzyme from animals does not act on cysteine, serine or chloroalanine, while the enzyme from bacteria shows activity with cysteine (cf. EC 2.8.1.7, cysteine desulfurase). Group: Enzymes. Synonyms: selenocysteine reductase; selenocysteine β-lyase. Enzyme Commission Number: EC 4.4.1.16. CAS No. 82047-76-5. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-5318; selenocysteine lyase; EC 4.4.1.16; 82047-76-5; selenocysteine reductase; selenocysteine β-lyase. Cat No: EXWM-5318. | |
| sepiapterin reductase (L-erythro-7,8-dihydrobiopterin forming) | This enzyme catalyses the final step in the de novo synthesis of tetrahydrobiopterin from GTP. The enzyme, which is found in higher animals and some fungi and bacteria, produces the erythro form of tetrahydrobiopterin. cf. EC 1.1.1.325, sepiapterin reductase (L-threo-7,8-dihydrobiopterin forming). Group: Enzymes. Synonyms: SR. Enzyme Commission Number: EC 1.1.1.153. CAS No. 9059-48-7. 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-0058; sepiapterin reductase (L-erythro-7,8-dihydrobiopterin forming); EC 1.1.1.153; 9059-48-7; SR. Cat No: EXWM-0058. | |
| UDP-N-acetylgalactosamine diphosphorylase | The enzyme from plants and animals also has activity toward N-acetyl-α-D-glucosamine 1-phosphate (cf. EC 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase). Group: Enzymes. Enzyme Commission Number: EC 2.7.7.83. 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-3296; UDP-N-acetylgalactosamine diphosphorylase; EC 2.7.7.83. Cat No: EXWM-3296. | |
| UDP-N-acetylglucosamine diphosphorylase | Part of the pathway for acetamido sugar biosynthesis in bacteria and archaea. The enzyme from several bacteria (e.g., Escherichia coli, Bacillus subtilis and Hemophilus influenzae) has been shown to be bifunctional and also to possess the activity of EC 2.3.1.157, glucosamine-1-phosphate N-acetyltransferase. The enzyme from plants and animals is also active toward N-acetyl-α-D-galactosamine 1-phosphate (cf. EC 2.7.7.83, UDP-N-acetylgalactosamine diphosphorylase), while the bacterial enzyme shows low activity toward that substrate. Group: Enzymes. Synonyms: UDP-N-acetylglucosamine pyroph. Enzyme Commission Number: EC 2.7.7.23. CAS No. 9023-6-7. 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-3236; UDP-N-acetylglucosamine diphosphorylase; EC 2.7.7.23; 9023-06-7; UDP-N-acetylglucosamine pyrophosphorylase; uridine diphosphoacetylglucosamine pyrophosphorylase; UTP:2-acetamido-2-deoxy-α-D-glucose-1-phosphate uridylyltransferase; UDP-GlcNAc pyrophosphorylase; GlmU uridylyltransferase; Acetylglucosamine 1-phosphate uridylyltransferase; UDP-acetylglucosamine pyrophosphorylase; uridine diphosphate-N-acetylglucosamine pyrophosphorylase; uridine diphosphoacetylglucosamine phosphorylase; acetylglucosamine 1-phosphate uridylyltransferase. Cat No: EXWM-3236. | |
| Xaa-Pro dipeptidyl-peptidase | The intracellular enzyme from Lactococcus lactis (190-kDa) is the type example of peptidase family S15. The reaction is similar to that catalysed by dipeptidyl-peptidase IV of animals. Group: Enzymes. Synonyms: X-prolyl dipeptidyl aminopeptidase; PepX; X-prolyl dipeptidyl peptidase; X-Pro dipeptidyl-peptidase. Enzyme Commission Number: EC 3.4.14.11. CAS No. 54249-88-6. 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-4045; Xaa-Pro dipeptidyl-peptidase; EC 3.4.14.11; 54249-88-6; X-prolyl dipeptidyl aminopeptidase; PepX; X-prolyl dipeptidyl peptidase; X-Pro dipeptidyl-peptidase. Cat No: EXWM-4045. | |
| 10-[3-(2,2-Diimethyl-1,3-dioxolan-4-yl)-2,3-dihydroxypropyl]-7,8-dimethyl-isoalloxazine | 10-[3-(2,2-Diimethyl-1,3-dioxolan-4-yl)-2,3-dihydroxypropyl]-7,8-dimethyl-isoalloxazine is an intermediate uin the synthesis of Riboflavin 4',5'-Diphosphate which is a diphosphate derivative of Riboflavin (R414995); a nutritional factor found in milk, eggs, malted barley, liver, kidney, heart, and leafy vegetables. Richest natural source is yeast. Minute amounts present in all plant and animal cells. Vitamin (enzyme cofactor). Group: Biochemicals. Grades: Highly Purified. CAS No. 22854-81-5. Pack Sizes: 2.5mg, 5mg. Molecular Formula: C20H24N4O6. US Biological Life Sciences. | Worldwide |
| 10- ( ( (4R, 5R, 6S) -6- ( ( (tert-Butyldiphenylsilyl) oxy) methyl) -5-hydroxy-2, 2-dimethyl-1, 3-dioxan-4-yl) methyl) -7, 8-dimethylbenzo [g]pteridine-2, 4 (3H, 10H) -dione | 10- ( ( (4R, 5R, 6S) -6- ( ( (Tert-butyldiphenylsilyl) oxy) methyl) -5-hydroxy-2, 2-dimethyl-1, 3-dioxan-4-yl) methyl) -7, 8-dimethylbenzo [g]pteridine-2, 4 (3H, 10H) -dioneis an intermediate uin the synthesis of Riboflavin 4',5'-Diphosphate which is a diphosphate derivative of Riboflavin (R414995); a nutritional factor found in milk, eggs, malted barley, liver, kidney, heart, and leafy vegetables. Richest natural source is yeast. Minute amounts present in all plant and animal cells. Vitamin (enzyme cofactor). Group: Biochemicals. Grades: Highly Purified. Pack Sizes: 5mg, 10mg. Molecular Formula: C36H42N4O6Si, Molecular Weight: 654.83. US Biological Life Sciences. | Worldwide |
| 1-acylglycerol-3-phosphate O-acyltransferase | Acyl-[acyl-carrier protein] can also act as an acyl donor. The animal enzyme is specific for the transfer of unsaturated fatty acyl groups. Group: Enzymes. Synonyms: 1-acyl-sn-glycero-3-phosphate acyltransferase; 1-acyl-sn-glycerol 3-phosphate acyltransferase; 1-acylglycero-3-phosphate acyltransferase; 1-acylglycerolphosphate acyltransferase; 1-acylglycerophosphate acyltransferase; lysophosphatidic acid-acyltransferase. Enzyme Commission Number: EC 2.3.1.51. CAS No. 51901-16-7. 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-2231; 1-acylglycerol-3-phosphate O-acyltransferase; EC 2.3.1.51; 51901-16-7; 1-acyl-sn-glycero-3-phosphate acyltransferase; 1-acyl-sn-glycerol 3-phosphate acyltransferase; 1-acylglycero-3-phosphate acyltransferase; 1-acylglycerolphosphate acyltransferase; 1-acylglycerophosphate acyltransferase; lysophosphatidic acid-acyltransferase. Cat No: EXWM-2231. | |
| 1-Deoxy-1-[ (3-hydroxymethyl-4-methyl-6- (2-phenyldiazenyl) phenyl) amino]-D-ribitol | 1-Deoxy-1-[ (3-hydroxymethyl-4-methyl-6- (2-phenyldiazenyl) phenyl) amino]-D-ribitol is an intermediate in the synthesis of 8-Hydroxymethyl Riboflavin which is an impurity of Riboflavin (R414995), a nutritional factor found in milk, eggs, malted barley, liver, kidney, heart, leafy vegetables. Richest natural source is yeast. Minute amounts present in all plant and animal cells. Vitamin (enzyme cofactor). Group: Biochemicals. Grades: Highly Purified. Pack Sizes: 5mg, 10mg. Molecular Formula: C19H25N3O5. US Biological Life Sciences. | Worldwide |
| 1-Deoxy-1-[(3-hydroxymethyl-4-methylphenyl)amino]-D-ribitol | 1-Deoxy-1-[(3-hydroxymethyl-4-methylphenyl)amino]-D-ribitol is an intermediate in the synthesis of 8-Hydroxymethyl Riboflavin which is an impurity of Riboflavin (R414995), a nutritional factor found in milk, eggs, malted barley, liver, kidney, heart, leafy vegetables. Richest natural source is yeast. Minute amounts present in all plant and animal cells. Vitamin (enzyme cofactor). Group: Biochemicals. Grades: Highly Purified. Pack Sizes: 10mg, 25mg. Molecular Formula: C13H21NO5. US Biological Life Sciences. | Worldwide |
| 4-Chloro-DL-phenylalanine | 4-Chloro-DL-phenylalanine is a pharmaceutical intermediate. It acts as a selective and irreversible inhibitor of tryptophan hydroxylase. It is a rate-limiting enzyme in the biosynthesis of serotonin. It has been used experimentally to treat carcinoid syndrome. It is used in scientific research in humans and animals to investigate the effects of serotonin depletion. It binds irreversibly to tryptophan hydroxylase to cause depletion of serotonin in the brain. Uses: 4-chloro-dl-phenylalanine has been used experimentally to treat carcinoid syndrome. it is used in scientific research in humans and animals to investigate the effects of serotonin depletion. it binds irreversibly to tryptophan hydroxylase to cause depletion of serotonin in the brain. Synonyms: CP-10,188; CP10,188; CP 10,188; CP-10188; CP10188; CP 10188; Fenclonine; DL-3-(4-Chlorophenyl)alanine; Fenclonin; NSC 77370; p-Clorophenylalanine.; DL-4-Chlorophenylalanine;p-Chlorophenylalanine;(S)-2-amino-3-(4-chlorophenyl)propanoic acid;2-Amino-3-(4-chlorophenyl)propanoic acid; DL-3-(4-Chlorophenyl)alanine; Fenclonin; Fenclonine; PCP; PCPA; CP-10188. Grades: ≥ 99% (HPLC). CAS No. 7424-00-2. Molecular formula: C9H10ClNO2. Mole weight: 199.63. |  |
| A-740003 | A-740003 is potent, selective and competitive P2X7 receptor antagonist. Its IC50 values are 18 and 40 nM for rat and human receptors respectively measured by agonist-stimulated changes in intracellular calcium concentrations. It displays selectivity over a variety of P2X and P2Y receptors up to a concentration of 100 μM. It reduces nociception in animal models of persistent neuropathic and inflammatory pain. It showed weak or no activity (IC(50) > 10 muM) at other P2 receptors and an array of other neurotransmitter and peptide receptors, ion channels, reuptake sites, and enzymes. It potently blocked agonist-evoked IL-1beta release (IC(50) = 156 nM) and pore formation (IC(50) = 92 nM) in differentiated human THP-1 cells. It produces significant antinociception in animal models of neuropathic and inflammatory pain in vivo. Uses: A-740003 produces significant antinociception in animal models of neuropathic and inflammatory pain in vivo. Synonyms: A-740003; A 740003; A740003; N-[1-[[(Cyanoamino)(5-quinolinylimino)methyl]amino]-2,2-dimethylpropyl]-3,4-dimethoxybenzeneacetamide;N-(1-{[(cyanoimino)(5-quinolinylamino) methyl] amino}-2,2-dimethylpropyl)-2-(3,4-dimethoxyphenyl)acetamide. Grades: >98 %. CAS No. 861393-28-4. Molecular formula: C26H30N6O3. Mole weight: 474.55. | |
| acetylesterase | This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. Group: Enzymes. Synonyms: C-esterase (in animal tissues); acetic ester hydrolase; chloroesterase; p-nitrophenyl acetate esterase; Citrus acetylesterase. Enzyme Commission Number: EC 3.1.1.6. CAS No. 9000-82-2. 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-3488; acetylesterase; EC 3.1.1.6; 9000-82-2; C-esterase (in animal tissues); acetic ester hydrolase; chloroesterase; p-nitrophenyl acetate esterase; Citrus acetylesterase. Cat No: EXWM-3488. | |
| Acid Black 2 | Acid Black 2 is a synthetic dye belonging to the triphenylmethane family. Acid Black 2 is a biochemical reagent that can be used as a biological material or organic compound for life science related research. Uses: Acid black 2 is widely used in a variety of scientific research applications. it is used in the study of cell structure and function, as well as in the study of enzymes and proteins. it is also used in the study of gene expression and in the study of metabolic pathways. nigrosine can also be used in the study of plant and animal physiology, as well as in the study of biochemistry. Additional or Alternative Names: Black 10B; Vondamol Light Black 10B; Dinatrium-4-amino-5-hydroxy-3-[(E)-(4-nitrophenyl)diazenyl]-6-[(E)-phenyldiazenyl]-2,7-naphthalendisulfonat; Fast Sulon Black BN; Metamine Blue Black; Amido Black 10 B; Naphtocard Black 12B ; Aniline blue black; CI NO 0470; Sodium 4-amino-5-hydroxy-3-(4-nitrophenylazo)-6-(phenylazo)naphthalene-2,7-disulphonate; Comacid Blue Black B; Calcocid Blue Black 2R. Product Category: Acid Dyes. Appearance: dark brown granular solid. CAS No. 8005-3-6. Molecular formula: C22H14N6Na2O9S2. Mole weight: 616.491. IUPACName: disodium;4-amino-5-hydroxy-3-[(4-nitrophenyl)diazenyl]-6-phenyldiazenylnaphthalene-2,7-disulfonate. Canonical SMILES: C1=CC=C(C=C1)N=NC2=C(C3=C(C(=C(C=C3C=C2S(=O)(=O)[O-])S(=O)(=O)[O-])N=NC4=CC=C(C=C4)[N+](=O)[O-])N)O.[Na+].[Na+]. Product ID: ACM8005036. Alfa Chemi | |
| Aflatoxin Q1 | Aflatoxin Q1 is a metabolite of Aflatoxin B1. It is created in human body as a in-vivo detoxification process of Aflatoxin B1. Uses: A metabolite of aflatoxin b1; a hepatocarcinogen in many animal models and probably a human carcinogen. it is produced by the predominant forms of cytochrome p 450 enzymes responsible for the biotransformation of afb1. it shows potential predictive value. Synonyms: Cyclopenta[c]furo[3',2':4,5]furo[2,3-h][1]benzopyran-1,11-dione, 2,3,6a,9a-tetrahydro-3-hydroxy-4-methoxy-, (3S,6aR,9aS)-; Cyclopenta(c)furo(3',2':4,5)furo(2,3-h)(1)benzopyran-1,11-dione, 2,3,6a,9a-tetrahydro-3-hydroxy-4-methoxy-, (3S-(3-alpha,6a-alpha,9a-alpha))-; (3S, 6aR, 9aS)-3-hydroxy-4-methoxy-2, 3, 6a, 9a-tetrahydrocyclopenta[c]furo[3', 2':4, 5]furo[2, 3-h]chromene-1, 11-dione. Grades: ≥98%. CAS No. 52819-96-2. Molecular formula: C17H12O7. Mole weight: 328.27. | |
| Ag+-exporting ATPase | A P-type ATPase that exports Ag+ ions from pathogenic microorganisms as well as from some animal tissues. Group: Enzymes. Enzyme Commission Number: EC 3.6.3.53. 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-4692; Ag+-exporting ATPase; EC 3.6.3.53. Cat No: EXWM-4692. | |
| alanine-glyoxylate transaminase | A pyridoxal-phosphate protein. With one component of the animal enzyme, 2-oxobutanoate can replace glyoxylate. A second component also catalyses the reaction of EC 2.6.1.51 serine-pyruvate transaminase. Group: Enzymes. Synonyms: AGT; alanine-glyoxylate aminotransferase; alanine-glyoxylic aminotransferase; L-alanine-glycine transaminase. Enzyme Commission Number: EC 2.6.1.44. CAS No. 9015-67-2. 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-2885; alanine-glyoxylate transaminase; EC 2.6.1.44; 9015-67-2; AGT; alanine-glyoxylate aminotransferase; alanine-glyoxylic aminotransferase; L-alanine-glycine transaminase. Cat No: EXWM-2885. | |
| alcohol dehydrogenase | A zinc protein. Acts on primary or secondary alcohols or hemi-acetals with very broad specificity; however the enzyme oxidizes methanol much more poorly than ethanol. The animal, but not the yeast, enzyme acts also on cyclic secondary alcohols. Group: Enzymes. Synonyms: aldehyde reductase; ADH; alcohol dehydrogenase (NAD); aliphatic alcohol dehydrogenase; ethanol dehydrogenase; NAD-dependent alcohol dehydrogenase; NAD-specific aromatic alcohol dehydrogenase; NADH-alcohol dehydrogenase; NADH-aldehyde dehydrogenase; primary alcohol dehydrogenase; yeast alcohol dehydrogenase. Enzyme Commission Number: EC 1.1.1.1. CAS No. 9031-72-5. Alcohol dehydrogenase. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-0001; alcohol dehydrogenase; EC 1.1.1.1; 9031-72-5; aldehyde reductase; ADH; alcohol dehydrogenase (NAD); aliphatic alcohol dehydrogenase; ethanol dehydrogenase; NAD-dependent alcohol dehydrogenase; NAD-specific aromatic alcohol dehydrogenase; NADH-alcohol dehydrogenase; NADH-aldehyde dehydrogenase; primary alcohol dehydrogenase; yeast alcohol dehydrogenase. Cat No: EXWM-0001. | |
| Alcohol dehydrogenase from E. coli, Recombinant | Alcohol dehydrogenases (ADH) are a group of dehydrogenase enzymes that occur in many organisms and facilitate the interconversion between alcohols and aldehydes or ketones with the reduction of nicotinamide adenine dinucleotide (NAD+ to NADH). In Humans and many other animals, they serve to break down alcohols that otherwise are toxic, and they also participate in geneRation of useful aldehyde, ketone, or alcohol groups during biosynthesis of various metabolites. In yeast, plants, and many bacteria, some alcohol dehydrogenases catalyze the opposite reaction as part of fermentation to ensure a constant supply of NAD+. Applications: High purity recombinant alcohol dehyd...l dehydrogenase; yeast alcohol dehydrogenase; EC 1.1.1.1. Enzyme Commission Number: EC 1.1.1.1. CAS No. 9031-72-5. Alcohol dehydrogenase. Mole weight: ~ 38,642 Da. Activity: 6.7 U/mg protein at pH 8.5 and 25°C. Storage: Store at 4°C. Do not store the enzyme in presence of sodium azide. Form: In 3.2 M ammonium sulphate. Source: E. coli. aldehyde reductase; ADH; alcohol dehydrogenase (NAD); aliphatic alcohol dehydrogenase; ethanol dehydrogenase; NAD-dependent alcohol dehydrogenase; NAD-specific aromatic alcohol dehydrogenase; NADH-alcohol dehydrogenase; NADH-aldehyde dehydrogenase; primary alcohol dehydrogenase; yeast alcohol dehydrogenase; EC 1.1.1.1. Cat No: NATE-0803. | |
| Alcohol dehydrogenase from Equine, Recombinant | Alcohol dehydrogenases (ADH) are a group of dehydrogenase enzymes that occur in many organisms and facilitate the interconversion between alcohols and aldehydes or ketones with the reduction of nicotinamide adenine dinucleotide (NAD+ to NADH). In Humans and many other animals, they serve to break down alcohols that otherwise are toxic, and they also participate in geneRation of useful aldehyde, ketone, or alcohol groups during biosynthesis of various metabolites. In yeast, plants, and many bacteria, some alcohol dehydrogenases catalyze the opposite reaction as part of fermentation to ensure a constant supply of NAD+. Group: Enzymes. Synonyms: aldehyde reductase; ADH; alcohol dehydrogenase (NAD); aliphatic alcohol dehydrogenase; ethanol dehydrogenase; NAD-dependent alcohol dehydrogenase; NAD-specific aromatic alcohol dehydrogenase; NADH-alcoh. Enzyme Commission Number: EC 1.1.1.1. CAS No. 9031-72-5. Alcohol dehydrogenase. Activity: >0.5 U/mg. Storage: Store at -20°C. Source: E. coli. Species: Equine. aldehyde reductase; ADH; alcohol dehydrogenase (NAD); aliphatic alcohol dehydrogenase; ethanol dehydrogenase; NAD-dependent alcohol dehydrogenase; NAD-specific aromatic alcohol dehydrogenase; NADH-alcohol dehydrogenase; NADH-aldehyde dehydrogenase; primary alcohol dehydrogenase; yeast alcohol dehydrogenase; EC 1.1.1.1. Cat No: NATE-1584. | |
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