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| Product | Description | |
|---|---|---|
| 4-hydroxysphinganine ceramide fatty acyl 2-hydroxylase | The enzyme, characterized from yeast and mammals, catalyses the hydroxylation of carbon 2 of long- or very-long-chain fatty acids attached to (4R)-4-hydroxysphinganine during de novo ceramide synthesis. The enzymes from yeast and from mammals contain an N-terminal cytochrome b5 domain that acts as the direct electron donor to the desaturase active site. The newly introduced 2-hydroxyl group has R-configuration. cf. EC 1.14.18.7, dihydroceramide fatty acyl 2-hydroxylase. Group: Enzymes. Synonyms: FA2H (gene name); SCS7 (gene name). Enzyme Commission Number: EC 1.14.18.6. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-0968; 4-hydroxysphinganine ceramide fatty acyl 2-hydroxylase; EC 1.14.18.6; FA2H (gene name); SCS7 (gene name). Cat No: EXWM-0968. |  |
| 5-Hydroxymethylcytidine | 5-Hydroxymethylcytosine is a DNA pyrimidine nitrogen base. It is formed from the DNA base cytosine by adding a methyl group and then a hydroxy group. It is important in epigenetics, because the hydroxymethyl group on the cytosine can possibly switch a gene on and off. It was first seen in bacteriophages in 1952.[1][2] However, in 2009 it was found to be abundant in human and mouse brains,[3] as well as in embryonic stem cells.[4] In mammals, it can be generated by oxidation of 5-methylcytosine, a reaction mediated by the Tet family of enzymes. 5-Hydroxymethylcytidine is a product in DNA hydroxymethylation. The concentrations of 5-Hydroxymethylcytidine in the brain were used to study Alzheimers disease. Group: Biochemicals. Grades: Highly Purified. CAS No. 19235-17-7. Pack Sizes: 25mg. US Biological Life Sciences. |  Worldwide |
| acyl-CoA (8-3)-desaturase | The enzyme introduces a cis double bond at carbon 5 of acyl-CoAs that contain a double bond at position 8. The enzymes from algae, mosses, mammals and the protozoan Leishmania major catalyse the desaturation of dihomo-γ-linoleate [(8Z,11Z,14Z)-icosa-8,11,14-trienoate] and (8Z,11Z,14Z,17Z)-icosa-8,11,14,17-tetraenoate to generate arachidonate and (5Z,8Z,11Z,14Z,17Z)-icosa-5,8,11,14,17-pentaenoate, respectively. The enzyme contains a cytochrome b5 domain that acts as the direct electron donor to the desaturase active site and does not require an external cytochrome. cf. EC 1.14.19.37, acyl-CoA 5-desaturase. Group: Enzymes. Synonyms: FADS1 (gene name); acyl-CoA 5-desaturase (methylene-interrupted). Enzyme Commission Number: EC 1.14.19.44. 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-1009; acyl-CoA (8-3)-desaturase; EC 1.14.19.44; FADS1 (gene name); acyl-CoA 5-desaturase (methylene-interrupted). Cat No: EXWM-1009. | |
| β-Enolase from Human, Recombinant | Beta-enolase, also known as ENO3, is one of the three enolase isoenzymes found in mammals. This isoenzyme, a homodimer, is found in skeletal muscle cells in the adult. ENO3 play a role in converting phosphoglyceric acid to phosphenolpyruvic acid in the glycolytic pathway. Mutations in its gene can be associated with metabolic myopathies that may result from decreased stability of the enzyme. Recombinant human ENO3 protein, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography techniques. Group: Enzymes. Synonyms: 2-phospho-D-glycerate hydro-lyase; Beta-enolase; ENO3; Enolase 3; Muscle-specific enolase. Purity: > 95% (SDS-PAGE). Enolase. Mole weight: 49 kDa. Storage: Store at -70°C. Form: Liquid; 0.5 mg/mL solution in 20 mM Tris-HCl (pH 8.0) containing 1 mM DTT, 20% glycerol and 0.1 mM NaCl. Source: E. coli. Species: Human. 2-phospho-D-glycerate hydro-lyase; Beta-enolase; ENO3; Enolase 3; Muscle-specific enolase. Cat No: NATE-0941. | |
| chymosin | Neonatal gastric enzyme with high milk clotting and weak general proteolytic activity, formed from prochymosin. Found among mammals with postnatal uptake of immunoglobulins. In peptidase family A1(pepsin A family). Group: Enzymes. Synonyms: rennin (but this should be avoided since it leads to confusion with renin). Enzyme Commission Number: EC 3.4.23.4. CAS No. 9001-98-3. Rennin. 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-4276; chymosin; EC 3.4.23.4; 9001-98-3; rennin (but this should be avoided since it leads to confusion with renin). Cat No: EXWM-4276. | |
| diphthine methyl ester synthase | This eukaryotic enzyme is part of the biosynthetic pathway of diphthamide. Different from the archaeal enzyme, which performs only 3 methylations, producing diphthine (cf. EC 2.1.1.98). The relevant histidine of elongation factor 2 is His715 in mammals and His699 in yeast. The order of the 4 methylations is not known. Group: Enzymes. Synonyms: S-adenosyl-L-methionine:elongation factor 2 methyltransferase (ambiguous); diphthine methyltransferase (ambiguous); Dph5 (ambiguous). Enzyme Commission Number: EC 2.1.1.314. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1922; diphthine methyl ester synthase; EC 2.1.1.314; S-adenosyl-L-methionine:elongation factor 2 methyltransferase (ambiguous); diphthine methyltransferase (ambiguous); Dph5 (ambiguous). Cat No: EXWM-1922. | |
| galactokinase | Part of the Leloir pathway for galactose metabolism. The enzymes from mammals and from the bacterium Escherichia coli have no activity with N-acetyl-α-D-galactosamine. Group: Enzymes. Synonyms: galactokinase (phosphorylating); ATP:D-galactose-1-phosphotransferase. Enzyme Commission Number: EC 2.7.1.6. CAS No. 9030-53-9. GALK. 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-3090; galactokinase; EC 2.7.1.6; 9030-53-9; galactokinase (phosphorylating); ATP:D-galactose-1-phosphotransferase. Cat No: EXWM-3090. | |
| hydroperoxy icosatetraenoate isomerase | Binds Fe2+. The enzyme from mammals accepts a range of hydroperoxyicosatetraenoates producing one or several different hydroxyepoxyicosatrienoates. The human enzyme has highest activity with (12R)-HPETE producing (5Z,8R,9E,11R,12R,14Z)-8-hydroxy-11,12-epoxyicosa-5,9,14-trienoate, followed by (12S)-HPETE producing (5Z,8Z,10R,11S,12S,14Z)-10-hydroxy-11,12-epoxyicosa-5,8,14-trienoate and (5Z,8R,9E,11S,12S,14Z)-8-hydroxy-11,12-epoxyicosa-5,9,14-trienoate. The mouse enzyme has highest activity with (8S)-HPETE, producing (5Z,8S,9S,10R,11Z,14Z)-10-hydroxy-8,9-epoxyicosa-5,11,14-trienoate. The enzymes also have the activity of EC 4.2.1.152, hydroperoxy icosatetraenoate dehydratase. Group: Enzymes. Synonyms: epidermal lipoxygenase-3 (ambiguous); eLOX3 (ambiguous). Enzyme Commission Number: EC 5.4.4.7. 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-5548; hydroperoxy icosatetraenoate isomerase; EC 5.4.4.7; epidermal lipoxygenase-3 (ambiguous); eLOX3 (ambiguous). Cat No: EXWM-5548. | |
| insulysin | A 110 kDa cytosolic enzyme, known from mammals and the fruit fly, Drosophila melanogaster. Inhibited by bacitracin, chelating agents EDTA and 1,10-phenanthroline, and by thiol-blocking reagents such as N-ethylmaleimide, but not by phosphoramidon. In peptidase family M16 (pitrilysin family). Group: Enzymes. Synonyms: insulinase; insulin-degrading enzyme; insulin protease; insulin proteinase; insulin-degrading neutral proteinase; insulin-specific protease; insulin-glucagon protease; metalloinsulinase; IDE. Enzyme Commission Number: EC 3.4.24.56. CAS No. 9013-83-6. IDE. 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-4338; insulysin; EC 3.4.24.56; 9013-83-6; insulinase; insulin-degrading enzyme; insulin protease; insulin proteinase; insulin-degrading neutral proteinase; insulin-specific protease; insulin-glucagon protease; metalloinsulinase; IDE. Cat No: EXWM-4338. | |
| L-Glutamate Decarboxylase (Crude Enzyme) | Glutamate decarboxylase or glutamic acid decarboxylase (GAD) is an enzyme that catalyzes the decarboxylation of glutamate to GABA and CO 2. In mammals, GAD exists in two isoforms encoded by two different genes - GAD1 and GAD2. These isoforms are GAD67 and GAD65 with molecular weights of 67 and 65 kDa, respectively. GAD1 and GAD2 are expressed in the brain where GABA is used as a neurotransmitter, GAD2 is also expressed in the pancreas. At least two more forms, GAD25 and GAD44 (embryonic; EGAD) are described in the developing brain. They are coded by the alternative transcripts of GAD1, I-80 and I-86: GAD25 is coded by both, GAD44 - only by I-80.This product with the indicated enzyme activity was briefly purified from engineered E. coli. Applications: Medicine; synthesis; diagnostics; food industry. Group: Enzymes. Synonyms: L-glutamic acid. Enzyme Commission Number: EC 4.1.1.15. CAS No. 9024-58-2. Activity: Undetermined. Appearance: Clear to translucent yellow solution. Storage: at -20 °C or lower, for at least 1 month. Source: E. coli. L-glutamic acid decarboxylase; L-glutamic decarboxylase; cysteic acid decarboxylase; L-glutamate α-decarboxylase; aspartate 1-decarboxylase; aspartic α-decarboxylase; L-aspartate-α-decarboxylase; γ-glutamate decarboxylase; L-glutamate 1-carboxy-lyase. Pack: 100ml. Cat No: NATE-1846. | |
| lipid-phosphate phosphatase | Requires Mg2+ for maximal activity. The enzyme from mammals is a bifunctional enzyme: the N-terminal domain exhibits lipid-phosphate-phosphatase activity and the C-terminal domain has the activity of EC 3.3.2.10, soluble epoxide hydrolase (sEH). The best substrates for this enzyme are 10-hydroxy-9-(phosphonooxy)octadecanoates, with the threo- form being a better substrate than the erythro- form. The phosphatase activity is not found in plant sEH or in EC 3.3.2.9, microsomal epoxide hydrolase, from mammals. Group: Enzymes. Synonyms: hydroxy fatty acid phosphatase; dihydroxy fatty acid phosphatase; hydroxy lipid phosphatase; sEH (ambiguous); soluble epoxide hydrolase (ambiguous). Enzyme Commission Number: EC 3.1.3.76. 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-3681; lipid-phosphate phosphatase; EC 3.1.3.76; hydroxy fatty acid phosphatase; dihydroxy fatty acid phosphatase; hydroxy lipid phosphatase; sEH (ambiguous); soluble epoxide hydrolase (ambiguous). Cat No: EXWM-3681. | |
| methylglyoxal reductase (NADPH) | The enzyme from the yeast Saccharomyces cerevisiae catalyses the reduction of a keto group in a number of compounds, forming enantiopure products. Among the substrates are methylglyoxal (which is reduced to (S)-lactaldehyde), 3-methylbutanal, hexane-2,5-dione and 3-chloro-1-phenylpropan-1-one. The enzyme differs from EC 1.1.1.78, methylglyoxal reductase (NADH), which is found in mammals, by its coenzyme requirement, reaction direction, and enantiomeric preference. Group: Enzymes. Synonyms: lactaldehyde dehydrogenase (NADP+); GRE2 (gene name); methylglyoxal reductase (NADPH-dependent); lactaldehyde:NADP+ oxidoreductase. Enzyme Commission Number: EC 1.1.1.283. CAS No. 78310-66-4. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-0191; methylglyoxal reductase (NADPH); EC 1.1.1.283; 78310-66-4; lactaldehyde dehydrogenase (NADP+); GRE2 (gene name); methylglyoxal reductase (NADPH-dependent); lactaldehyde:NADP+ oxidoreductase. Cat No: EXWM-0191. | |
| mitochondrial processing peptidase | Known from the mitochondrial matrix of fungi and mammals. Formed from two subunits, both homologous with pitrilysin, and the products of the MAS1 and MAS2 genes in yeast. In peptidase family M16 (pitrilysin family). Group: Enzymes. Synonyms: processing enhancing peptidase (for one of two subunits); mitochondrial protein precursor-processing proteinase; matrix peptidase; matrix processing peptidase; matrix processing proteinase; mitochondrial protein precursor-processing proteinase; MPP. Enzyme Commission Number: EC 3.4.24.64. CAS No. 86280-61-7. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4347; mitochondrial processing peptidase; EC 3.4.24.64; 86280-61-7; processing enhancing peptidase (for one of two subunits); mitochondrial protein precursor-processing proteinase; matrix peptidase; matrix processing peptidase; matrix processing proteinase; mitochondrial protein precursor-processing proteinase; MPP. Cat No: EXWM-4347. | |
| Native Aspergillus oryzae α-Amylase | α-Amylase is a protein enzyme EC 3.2.1.1 that hydrolyses alpha bonds of large, alpha-linked polysaccharides, such as starch and glycogen, yielding glucose and maltose. It is the major form of amylase found in Humans and other mammals. It is also present in seeds containing starch as a food reserve, and is secreted by many fungi. Applications: Α-amylase is used to hydrolyze α bonds of α-linked polysaccharides, such as starch and glycogen. α-amylase has been used in various plant studies, such as metabolism studies in arabidopsis. amylases from aspergillus oryzae are commonly used as baking additives to prevent staling in the baking industry, clarify haze from fruit juices and alcoholic beverages, and to produce glucose and maltose syrup products. Group: Enzymes. Synonyms: glycogenase; αamylase, α-amylase; 1,4-α-D-glucan glucanohydrolase; EC 3.2.1.1; 9001-19-8; endoamylase; Taka-amylase A. Enzyme Commission Number: EC 3.2.1.1. CAS No. 9001-19-8. α-Amylase. Mole weight: Mr ~51 kDa. Activity: > 150 units/mg protein (biuret); ~1.5 units/mg; ~30 units/mg. Storage: -20°C. Form: powder containing dextrin. Source: Aspergillus oryzae. glycogenase; αamylase, α-amylase; 1,4-α-D-glucan glucanohydrolase; EC 3.2.1.1; 9001-19-8; endoamylase; Taka-amylase A. Cat No: NATE-0740. | |
| Native Bacillus amyloliquefaciens α-Amylase | α-Amylase is a protein enzyme EC 3.2.1.1 that hydrolyses alpha bonds of large, alpha-linked polysaccharides, such as starch and glycogen, yielding glucose and maltose. It is the major form of amylase found in Humans and other mammals. It is also present in seeds containing starch as a food reserve, and is secreted by many fungi. Applications: Α-amylase is used to hydrolyze α bonds of α-linked polysaccharides, such as starch and glycogen. this product is from bacillus amyloliquefaciens and is supplied as a liquid. α-amylase has been used in various plant studies, such as metabolism studies in arabidopsis. α-amylase from bacillus amy...ng sugars, which are then used for ethanol fermentation by saccharomyces cerevisiae fncc 3012. the enzyme catalyzes amylolysis of gelatinised waxy maize starch to produce reducing sugars. Group: Enzymes. Synonyms: glycogenase; αamylase, α-amylase; 1,4-α-D-glucan glucanohydrolase; EC 3.2.1.1; 9001-19-8; endoamylase; Taka-amylase A. Enzyme Commission Number: EC 3.2.1.1. CAS No. 9001-19-8. α-Amylase. Mole weight: 55 kDa. Activity: > 250 units/g. Form: liquid. Source: Bacillus amyloliquefaciens. glycogenase; αamylase, α-amylase; 1,4-α-D-glucan glucanohydrolase; EC 3.2.1.1; 9001-19-8; endoamylase; Taka-amylase A. Cat No: NATE-0741. | |
| Native Bacillus licheniformis α-Amylase | α-Amylase is a protein enzyme EC 3.2.1.1 that hydrolyses alpha bonds of large, alpha-linked polysaccharides, such as starch and glycogen, yielding glucose and maltose. It is the major form of amylase found in Humans and other mammals. It is also present in seeds containing starch as a food reserve, and is secreted by many fungi. Applications: Α-amylase is used to hydrolyze α bonds of α-linked polysaccharides, such as starch and glycogen. this product is from bacillus licheniformis and is type xii-a. α-amylase, from creative enzymes, has been used in various plant studies, such as metabolism studies in arabidopsis. Group: Enzymes. Synonyms: glycogenase; αamylase, α-amylase; 1,4-α-D-glucan glucanohydrolase; EC 3.2.1.1; 9001-19-8; endoamylase; Taka-amylase A. Enzyme Commission Number: EC 3.2.1.1. CAS No. 9001-19-8. α-Amylase. Activity: Type XII-A, saline solution, > 500 units/mg protein (biuret); Type B, liquid. Source: Bacillus licheniformis. glycogenase; αamylase, α-amylase; 1,4-α-D-glucan glucanohydrolase; EC 3.2.1.1; 9001-19-8; endoamylase; Taka-amylase A. Cat No: NATE-0742. | |
| Native Bacillus stearothermophilus Phosphofructokinase | Phosphofructokinase is a kinase enzyme that phosphorylates fructose 6-phosphate in glycolysis. The enzyme-catalysed transfer of a phosphoryl group from ATP is an important reaction in a wide variety of biological processes. One enzyme that utilizes this reaction is phosphofructokinase (PFK), which catalyses the phosphorylation of fructose-6-phosphate to fructose-1,6-bisphosphate, a key regulatory step in the glycolytic pathway. PFK exists as a homotetramer in bacteria and mammals (where each monomer possesses 2 similar domains) and as an octomer in yeast (where there are 4 alpha-(PFK1) and 4 beta-chains (PFK2), the latter, like the mammalian monomers, possessing 2 ...cs reagent. Applications: Useful for enzymatic determiantion of fructose-6-phosphate. Group: Enzymes. Synonyms: PFKWII; EC 2.7.1.11; PFK; phosphofructokinase; 6-phosphofructokinase; Phosphofructokinase I; Phosphohexokinase. Enzyme Commission Number: EC 2.7.1.11. CAS No. 9001-80-3. PFK. Mole weight: 72 kDa (gel filtration); 35 kDa (SDS-PAGE). Activity: > 250 U/mg. Appearance: White to pale yellow powder. Storage: Storage at-20°C in the presence of a desiccant is recommended. Form: Freeze dried powder. Source: Bacillus stearothermophilus. PFKWII; EC 2.7.1.11; PFK; phosphofructokinase; 6-phosphofructokinase; Phosphofructokinase I; Phosphohexokinase. Cat No: NATE-0551. | |
| Native Bacillus subtilis Xylanase Enzyme (Food Grade) | Xylanase is the name given to a class of enzymes which degrade the linear polysaccharide beta-1,4-xylan into xylose, thus breaking down hemicellulose, one of the major components of plant cell walls. As such, it plays a major role in micro-organisms thriving on plant sources for the degradation of plant matter into usable nutrients. Xylanases are produced by fungi, bacteria, yeast, marine algae, protozoans, snails, crustaceans, insect, seeds, etc., (mammals do not produce xylanases). Xylanase which made from the best strain of bacillus subtilis. it is a kind of purified endo-bacteria-xylanase. it can be applied in the flour treatment for bread powder and steam brea...and chewy. 2) in the storage of bread, the appropriate xylanase can retrad bread staling, improve the water holding capacity of the bread and optimize the gluten network, thereby, preventing water loss and re-allocate, stabilize the organizational structure of the bread. Group: Enzymes. Synonyms: EC 3.2.1.8; endo-(1?4)-β-xylan 4-xylanohydrolase; endo-1,4-xylanase; xylanase; β-1,4-xylanase; endo-1,4-xylanase; endo-β-1,4-xylanase; endo-1,4-β-D-xylanase; 1,4-β-xylan xylanohydrolase; β-xylanase; β-1,4-xylan xylanohydrolase; endo-1,4-β-xylanase; β-D-xylanase; endo-1,4-β-xylanase. Enzyme Commission Number: EC 3.2.1.8. CAS | |
| Native 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 Brewer's bottom yeast Orotidine-5'-monophosphate pyrophosphorylase | Orotate phosphoribosyltransferase (OPRTase) or Orotic acid phosphoribosyltransferase is an enzyme involved in pyrimidine biosynthesis. It catalyzes the formation of orotidine 5'-monophosphate (OMP) from orotate and phosphoribosyl pyrophosphate. In yeast and bacteria, orotate phosphoribosyltransferase is an independent enzyme with a unique gene coding for the protein, whereas in mammals and other multicellular organisms, the catalytic function is carried out by a domain of the bifunctional enzyme UMP synthase. Applications: This is the preferred enzyme for assaying orotidine 5?-monophosphate and for the production of omp analogs from the corresponding orot...ty: ~25 units/mg protein (modified Warburg-Christian). Storage: -20°C. Form: Lyophilized powder containing approx. 50% buffer salts. Source: Brewer's bottom yeast. orotidylic acid phosphorylase; orotidine-5'-phosphate pyrophosphorylase; OPRTase; orotate phosphoribosyl pyrophosphate transferase; orotic acid phosphoribosyltransferase; orotidine 5'-monophosphate pyrophosphorylase; orotidine monophosphate pyrophosphorylase; orotidine phosphoribosyltransferase; orotidylate phosphoribosyltransferase; orotidylate pyrophosphorylase; orotidylic acid pyrophosphorylase; orotidylic phosphorylase; orotidylic pyrophosphorylase; EC 2.4.2.10; 9030-25-5. Cat No: NATE-0498. | |
| Native Human α-Amylase | α-Amylase is a protein enzyme EC 3.2.1.1 that hydrolyses alpha bonds of large, alpha-linked polysaccharides, such as starch and glycogen, yielding glucose and maltose. It is the major form of amylase found in Humans and other mammals. It is also present in seeds containing starch as a food reserve, and is secreted by many fungi. Applications: Α-amylase is used to hydrolyze α bonds of α-linked polysaccharides, such as starch and glycogen. α-amylase has been used in various plant studies, such as metabolism studies in arabidopsis. α-amylase from human saliva has been used to study the development of nutraceuticals, which may aid the treatment of diabetes and obesity. Group: Enzymes. Synonyms: glycogenase; αamylase, α-amylase; 1,4-α-D-glucan glucanohydrolase; EC 3.2.1.1; 9001-19-8; endoamylase; Taka-amylase A. Enzyme Commission Number: EC 3.2.1.1. CAS No. 9001-19-8. α-Amylase. Activity: 1,000-3,000 units/mg protein; 300-1,500 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing (NH4)2SO4 and sodium Citrate. Source: Human saliva. Species: Human. glycogenase; αamylase, α-amylase; 1,4-α-D-glucan glucanohydrolase; EC 3.2.1.1; 9001-19-8; endoamylase; Taka-amylase A. Cat No: NATE-0743. | |
| Native Human Neuron Specific Enolase | Neuron specific enolase (NSE) is an enzyme that in humans is encoded by the ENO2 gene. Gamma-enolase is a phosphopyruvate hydratase. Gamma-enolase is one of the three enolase isoenzymes found in mammals. This isoenzyme, a homodimer, is found in mature neurons and cells of neuronal origin. A switch from alpha enolase to gamma enolase occurs in neural tissue during development in rats and primates. Applications: Neuron-specific enolase from human brain has been used in a study to assess human amniotic mesenchymal stem cells in the treatment of focal cerebral ischemia. it has also been used in a study to investigate sinonasal teratocarcinosarcoma with rhabdoid features. Group: Enzymes. Synonyms: EC 4.2.1.11; Neuron Specific Enolase; NSE; enolase; 2-phosphoglycerate dehydratase; 14-3-2-protein; nervous-system specific enolase; phosphoenolpyruvate hydra. Enzyme Commission Number: EC 4.2.1.11. CAS No. 9014-8-8. Enolase. Storage: -20°C. Form: buffered aqueous solution. Source: Human brain. Species: Human. EC 4.2.1.11; Neuron Specific Enolase; NSE; enolase; 2-phosphoglycerate dehydratase; 14-3-2-protein; nervous-system specific enolase; phosphoenolpyruvate hydratase; 2-phosphoglycerate dehydratase; 2-phosphoglyceric dehydratase; 2-phosphoglycerate enolase; γ-enolase; 2-phospho-D-glycerate hydro-lyase; phosphopyruvate hydratase. Cat No: DIA-225. | |
| Native Phosphofructokinase from Thermophillic bacteria | Phosphofructokinase is a kinase enzyme that phosphorylates fructose 6-phosphate in glycolysis. The enzyme-catalysed transfer of a phosphoryl group from ATP is an important reaction in a wide variety of biological processes. One enzyme that utilizes this reaction is phosphofructokinase (PFK), which catalyses the phosphorylation of fructose-6-phosphate to fructose-1,6-bisphosphate, a key regulatory step in the glycolytic pathway. PFK exists as a homotetramer in bacteria and mammals (where each monomer possesses 2 similar domains) and as an octomer in yeast (where there are 4 alpha-(PFK1) and 4 beta-chains (PFK2), the latter, like the mammalian monomers, possessing 2 similar domains). This protein may use the morpheein model of allosteric regulation. Applications: Diagnostic tests. Group: Enzymes. Synonyms: PFKWII; EC 2.7.1.11; PFK; phosphofructokinase; 6-phosphofructokinase; Phosphofructokinase I; Phosphohexokinase. Enzyme Commission Number: EC 2.7.1.11. CAS No. 9001-80-3. PFK. Storage: Store at -20°C. Form: Frozen Liquid. Source: Thermophillic bacteria. PFKWII; EC 2.7.1.11; PFK; phosphofructokinase; 6-phosphofructokinase; Phosphofructokinase I; Phosphohexokinase. Cat No: DIA-403. | |
| Native Porcine α-Amylase | α-Amylase is a protein enzyme EC 3.2.1.1 that hydrolyses alpha bonds of large, alpha-linked polysaccharides, such as starch and glycogen, yielding glucose and maltose. It is the major form of amylase found in Humans and other mammals. It is also present in seeds containing starch as a food reserve, and is secreted by many fungi. Applications: Α-amylase is used to hydrolyze α bonds of α-linked polysaccharides, such as starch and glycogen. this product is from porcine pancreas and is type i-a. α-amylase, from creative enzymes, has been used in various plant studies, such as metabolism studies in arabidopsis. Group: Enzymes. Synonyms: glycogenase; αamylase, α-amylase; 1,4-α-D-glucan glucanohydrolase; EC 3.2.1.1; 9001-19-8; endoamylase; Taka-amylase A. Enzyme Commission Number: EC 3.2.1.1. CAS No. 9001-19-8. α-Amylase. Mole weight: 51-54 kDa. Activity: > 1000 units/mg protein (E1%/280); > 10 units/mg solid; 700-1400 units/mg protein (E1%/280). Storage: 2-8°C. Form: saline suspension. Suspension in 2.9 M NaCl solution containing 3 mM CaCl2. Source: Porcine pancreas. Species: Porcine. glycogenase; αamylase, α-amylase; 1,4-α-D-glucan glucanohydrolase; EC 3.2.1.1; 9001-19-8; endoamylase; Taka-amylase A. Cat No: NATE-0745. | |
| Native Rat Histamine N-Methyl Transferase | (HNMT) is the enzyme which catalyzes the n-methylation of histamine as follows: Histamine + S-Adenosyl methionine ------> (SAM)methyladed Histamine. The mechanism involves the transfer of an active methyl group from S-Adenosyl methionine (SAM) to histamine. Histamine is present in most of mammalian tissues and HNMT is the enzyme responsible for inactivation of histamine in mammals. Methylation is major route of histamine metabolism. HNMT has been used to measure histamine by radio-enzymatic method. HNMT has been purified from rat kidney. Molecular weight equals 33,400, pH optimum is 8.00-8.25. We have also purified it from bovine kidney which seems to be very similar to rat kidney. Group: Enzymes. Synonyms: Histamine N-Methyl Transferase; HNMT; EC 2.1.1.8. Enzyme Commission Number: EC 2.1.1.8. CAS No. 9029-80-5. HNMT. Mole weight: 33.4 kDa. Activity: 50-100 U/mg. Stability: Store at -20°C (-4°F). Form: Freeze-dried powder. Source: Rat Kidney. Species: Rat. Histamine N-Methyl Transferase; HNMT; EC 2.1.1.8. Cat No: NATE-0898. | |
| Nitric Oxide Synthase, Inducible from mouse, Recombinant | Nitric oxide synthases (NOSs) are a family of enzymes catalyzing the production of nitric oxide (NO) from L-arginine. NO is an important cellular signaling molecule. It helps modulate vascular tone, insulin secretion, airway tone, and peristalsis, and is involved in angiogenesis and neural development. It may function as a retrograde neurotransmitter. Nitric oxide is mediated in mammals by the calcium-calmodulin controlled isoenzymes eNOS (endothelial NOS) and nNOS (neuronal NOS). The inducible isoform, iNOS, is involved in immune response, binds calmodulin at physiologically relevant concentrations, and produces NO as an immune defense mechanism, as NO is a free ...DPH); Inducible Nitric Oxide Synthase; NOS II; iNOS; macNOS; EC 1.14.13.39; NOSs. Enzyme Commission Number: EC 1.14.13.39. CAS No. 125978-95-2. NOSs. Mole weight: mol wt 130 kDa (homodimer); mol wt 130 kDa (subunit, homodimer). Storage: -70°C. Form: buffered aqueous solution; Solution in 50 mM HEPES, pH 7.4, with 10% glycerol, 8 μM tetrahydrobiopterin. Source: E. coli. Species: Mouse. nitric oxide synthetase; endothelium-derived relaxation factor-forming enzyme; endothelium-derived relaxing factor synthase; NO synthase; NADPH-diaphorase; nitric-oxide synthase (NADPH); Inducible Nitric Oxide Synthase; NOS II; iNOS; macNOS; EC 1.14.13.39; NOSs. Cat No: NATE-0489. | |
| proline dehydrogenase | A flavoprotein (FAD). The electrons from L-proline are transferred to the FAD cofactor, and from there to a quinone acceptor. In many organisms, ranging from bacteria to mammals, proline is oxidized to glutamate in a two-step process involving this enzyme and EC 1.2.1.88, L-glutamate γ-semialdehyde dehydrogenase. Both activities are carried out by the same enzyme in enterobacteria. Group: Enzymes. Synonyms: L-proline dehydrogenase; L-proline:(acceptor) oxidoreductase. Enzyme Commission Number: EC 1.5.5.2. CAS No. 9050-70-8. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1557; proline dehydrogenase; EC 1.5.5.2; 9050-70-8; L-proline dehydrogenase; L-proline:(acceptor) oxidoreductase. Cat No: EXWM-1557. | |
| Pyrroloquinoline quinone disodium salt | The disodium salt form of Pyrroloquinoline quinone which is a cofactor related to the enzyme-catalyzed redox reactions glucose and methanol dehydrogenase. Pyrroloquinoline quinone disodium salt is isolated from cultures of methylotropic bacteria and tissues of mammals. Nutritional supplement in health care products. Uses: Ingredient of health care products. Synonyms: Methoxatin disodium salt; Methoxatin Disodium; PQQ; Disodium 4,5-dihydro-4,5-dioxo-1H-pyrrolo(2,3-f)quinoline-2,7,9-tricarboxylate. Grades: 95%. CAS No. 122628-50-6. Molecular formula: C14H4N2Na2O8. Mole weight: 374.17. |  |
| soluble epoxide hydrolase | Catalyses the hydrolysis of trans-substituted epoxides, such as trans-stilbene oxide, as well as various aliphatic epoxides derived from fatty-acid metabolism. It is involved in the metabolism of arachidonic epoxides (epoxyicosatrienoic acids; EETs) and linoleic acid epoxides. The EETs, which are endogenous chemical mediators, act at the vascular, renal and cardiac levels to regulate blood pressure. The enzyme from mammals is a bifunctional enzyme: the C-terminal domain exhibits epoxide-hydrolase activity and the N-terminal domain has the activity of EC 3.1.3.76, lipid-phosphate phosphatase. Like EC 3.3.2.9, microsomal epoxide hydrolase, it is probable that the reaction involves...se). Group: Enzymes. Synonyms: epoxide hydrase (ambiguous); epoxide hydratase (ambiguous); arene-oxide hydratase (ambiguous); aryl epoxide hydrase (ambiguous); trans-stilbene oxide hydrolase; sEH; cytosolic epoxide hydrolase. Enzyme Commission Number: EC 3.3.2.10. CAS No. 9048-63-9. 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-3995; soluble epoxide hydrolase; EC 3.3.2.10; 9048-63-9; epoxide hydrase (ambiguous); epoxide hydratase (ambiguous); arene-oxide hydratase (ambiguous); aryl epoxide hydrase (ambiguous); trans-stilbene oxide hydrolase; sEH; cytosolic epoxide hydrolase. Cat No: EXWM-3995. | |
| sphingolipid 4-desaturase | The enzyme, which has been characterized from plants, fungi, and mammals, generates a trans double bond at position 4 of sphinganine bases in sphingolipids. The preferred substrate is dihydroceramide, but the enzyme is also active with dihydroglucosylceramide. Unlike EC 1.14.19.29, sphingolipid 8-desaturase, this enzyme does not contain an integral cytochrome b5 domain and requires an external cytochrome b5. The product serves as an important signalling molecules in mammals and is required for spermatide differentiation. Group: Enzymes. Synonyms: dehydroceramide desaturase. Enzyme Commission Number: EC 1.14.19.17. 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-0979; sphingolipid 4-desaturase; EC 1.14.19.17; dehydroceramide desaturase. Cat No: EXWM-0979. | |
| tissue kallikrein | Formed from tissue prokallikrein by activation with trypsin. In peptidase family S1 (trypsin family). A large number of tissue kallikrein-related sequences have been reported for rats and mice, though fewer seem to exist in other mammals. The few that have been isolated and tested on substrates include mouse γ-renin (EC 3.4.21.54), submandibular proteinase A, epidermal growth-factor-binding protein, nerve growth factor γ-subunit, rat tonin, submaxillary proteinases A and B, T-kininogenase, kallikreins k7 and k8 and human prostate-specific antigen (γ-seminoprotein,). Group: Enzymes. Synonyms: glandular kallikrein; pancreatic kallikrein; submandibular kallikrein; submaxillary kallikrein; kidney kallikrein; urinary kallikrein; kallikrein; salivary kall. Enzyme Commission Number: EC 3.4.21.35. CAS No. 389069-73-2. Kallikrein. 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-4129; tissue kallikrein; EC 3.4.21.35; 389069-73-2; glandular kallikrein; pancreatic kallikrein; submandibular kallikrein; submaxillary kallikrein; kidney kallikrein; urinary kallikrein; kallikrein; salivary kallikrein; kininogenin; kininogenase; callicrein; glumorin; padreatin; padutin; kallidinogenase; bradykininogenase; depot-padutin; urokallikrein; dilminal D; onokrein P. Cat No: EXWM-4129. | |
| UTP-glucose-1-phosphate uridylyltransferase | UTP--glucose-1-phosphate uridylyltransferase is an enzyme found in yeast, plants, and mammals as it is a key player in carbohydrate metabolism. It has been studied significantly in plants as sugar metabolism and production is seen as important for understanding growth from an agricultural standpoint. Recently, human UDP-glucose pyrophosphorylase has been studied and crystallized, revealing a different type of regulation than other organisms previously studied. Its significance is derived from the many uses of UDP-Glucose including galactose usage, glycogen synthesis, glycoprotein synthesis, and glycolipid synthesis. Group: Enzymes. Synonyms: UDP glucose pyrophosphorylase; glucose-1-phosphate uridylyltransferase; UDPG phosphorylase; UDP. Enzyme Commission Number: EC 2.7.7.9. CAS No. 9026-22-6. UDPG pyrophosphorylase. 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-3303; UTP-glucose-1-phosphate uridylyltransferase; EC 2.7.7.9; 9026-22-6; UDP glucose pyrophosphorylase; glucose-1-phosphate uridylyltransferase; UDPG phosphorylase; UDPG pyrophosphorylase; uridine 5'-diphosphoglucose pyrophosphorylase; uridine diphosphoglucose pyrophosphorylase; uridine diphosphate-D-glucose pyrophosphorylase; uridine-diphosphate glucose pyrophosphorylase. Cat No: EXWM-3303. | |
| 17β-estradiol 17-dehydrogenase | The enzyme oxidizes or reduces the hydroxy/keto group on C17 of estrogens and androgens in mammals and regulates the biological potency of these steroids. The mammalian enzyme is bifunctional and also catalyses EC 1.1.1.270, 3β-hydroxysteroid 3-dehydrogenase. The enzyme also acts on (S)-20-hydroxypregn-4-en-3-one and related compounds, oxidizing the (S)-20-group, but unlike EC 1.1.1.149, 20α-hydroxysteroid dehydrogenase, it is Si-specific with respect to NAD(P)+. Group: Enzymes. Synonyms: 20α-hydroxysteroid dehydrogenase; 17β,20α-hydroxysteroid dehydrogenase; 17β-estradiol dehydrogenase; estradiol dehydrogenase; estrogen 17-oxidoreductase; 17β-HSD; HSD17B7. Enzyme Commission Number: EC 1.1.1.62. CAS No. 9028-61-9. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-0348; 17β-estradiol 17-dehydrogenase; EC 1.1.1.62; 9028-61-9; 20α-hydroxysteroid dehydrogenase; 17β,20α-hydroxysteroid dehydrogenase; 17β-estradiol dehydrogenase; estradiol dehydrogenase; estrogen 17-oxidoreductase; 17β-HSD; HSD17B7. Cat No: EXWM-0348. | |
| 1,8-cineole 2-exo-monooxygenase | A heme-thiolate protein (P-450). The mammalian enzyme, expressed in liver microsomes, performs a variety of oxidation reactions of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. cf. EC 1.14.13.97 (taurochenodeoxycholate 6-hydroxylase), EC 1.14.13.67 (quinine 3-monooxygenase) and EC 1.14.13.32 (albendazole monooxygenase). Group: Enzymes. Synonyms: CYP3A4. Enzyme Commission Number: EC 1.14.13.157. 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-0757; 1,8-cineole 2-exo-monooxygenase; EC 1.14.13.157; CYP3A4. Cat No: EXWM-0757. | |
| 2-(3-amino-3-carboxypropyl)histidine synthase | A [4Fe-4S] enzyme that modifies a histidine residue of the translation elongation factor 2 (EF2) via a 3-amino-3-carboxypropyl radical. The enzyme is present in archae and eukaryotes but not in eubacteria. The relevant histidine of EF2 is His715 in mammals, His699 in yeast and His600 in Pyrococcus horikoshii. Part of diphthamide biosynthesis. Group: Enzymes. Synonyms: Dph2. Enzyme Commission Number: EC 2.5.1.108. 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-2724; 2-(3-amino-3-carboxypropyl)histidine synthase; EC 2.5.1.108; Dph2. Cat No: EXWM-2724. | |
| 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. | |
| 3α,7α,12α-trihydroxy-5β-cholestanoyl-CoA 24-hydroxylase | Requires ATP. The reaction in mammals possibly involves dehydrogenation to give a 24(25)-double bond followed by hydration. However, in amphibians such as the Oriental fire-bellied toad (Bombina orientalis), it is probable that the product is formed via direct hydroxylation of the saturated side chain of (25R)-3α,7α,12α-trihydroxy-5β-cholestan-26-oate and not via hydration of a 24(25) double bond. In microsomes, the free acid is preferred to the coenzyme A ester, whereas in mitochondria, the coenzyme A ester is preferred to the free-acid form of the substrate. Group: Enzymes. Synonyms: trihydroxycoprostanoyl-CoA oxidase; THC-CoA oxidase; THCA-CoA oxidase; 3α,7α,12α-trihydroxy-5β-cholestanoyl-CoA oxidase; 3α,. Enzyme Commission Number: EC 1.17.99.3. CAS No. 119799-47-2. 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-1103; 3α,7α,12α-trihydroxy-5β-cholestanoyl-CoA 24-hydroxylase; EC 1.17.99.3; 119799-47-2; trihydroxycoprostanoyl-CoA oxidase; THC-CoA oxidase; THCA-CoA oxidase; 3α,7α,12α-trihydroxy-5β-cholestanoyl-CoA oxidase; 3α,7α,12α-trihydroxy-5β-cholestan-26-oate 24-hydroxylase. Cat No: EXWM-1103. | |
| 3α-hydroxysteroid 3-dehydrogenase | The enzyme acts on multiple 3α-hydroxysteroids, such as androsterone and 5 α-dihydrotestosterone. The mammalian enzymes are involved in inactivation of steroid hormones, while the bacterial enzymes are involved in steroid degradation. This entry stands for enzymes whose stereo-specificity with respect to NAD+ or NADP+ is not known. [cf. EC 1.1.1.50, 3α-hydroxysteroid 3-dehydrogenase (Si-specific) and EC 1.1.1.213, 3α-hydroxysteroid 3-dehydrogenase (Re-specific)]. Group: Enzymes. Synonyms: 3α-hydroxysteroid dehydrogenase; AKR1C4 (gene name); AKR1C2 (gene name); hsdA (gene name). Enzyme Commission Number: EC 1.1.1.357. 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-0273; 3α-hydroxysteroid 3-dehydrogenase; EC 1.1.1.357; 3α-hydroxysteroid dehydrogenase; AKR1C4 (gene name); AKR1C2 (gene name); hsdA (gene name). Cat No: EXWM-0273. | |
| 3β-hydroxysteroid 3-dehydrogenase | The enzyme acts on multiple 3β-hydroxysteroids. Participates in the biosynthesis of zemosterol and cholesterol, where it catalyses the reaction in the opposite direction to that shown. The mammalian enzyme is bifunctional and also catalyses EC 1.1.1.62, 17β-estradiol 17-dehydrogenase. Group: Enzymes. Synonyms: 3-keto-steroid reductase; 3-KSR; HSD17B7 (gene name); ERG27 (gene name). Enzyme Commission Number: EC 1.1.1.270. CAS No. 42616-29-5. 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-0177; 3β-hydroxysteroid 3-dehydrogenase; EC 1.1.1.270; 42616-29-5; 3-keto-steroid reductase; 3-KSR; HSD17B7 (gene name); ERG27 (gene name). Cat No: EXWM-0177. | |
| 3-oxo-5α-steroid 4-dehydrogenase (NADP+) | The enzyme catalyses the conversion of assorted 3-oxo-Δ4 steroids into their corresponding 5α form. Substrates for the mammalian enzyme include testosterone, progesterone, and corticosterone. Substrates for the plant enzyme are brassinosteroids such as campest-4-en-3-one and (22α)-hydroxy-campest-4-en-3-one. cf. EC 1.3.99.5, 3-oxo-5α-steroid 4-dehydrogenase (acceptor). Group: Enzymes. Synonyms: cholestenone 5α-reductase; testosterone Δ4-5&. Enzyme Commission Number: EC 1.3.1.22. CAS No. 37255-34-8. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1297; 3-oxo-5α-steroid 4-dehydrogenase (NADP+); EC 1.3.1.22; 37255-34-8; cholestenone 5α-reductase; testosterone Δ4-5α-reductase; steroid 5α-reductase; 3-oxosteroid Δ4-dehydrogenase; 5α-reductase; steroid 5α-hydrogenase; 3-oxosteroid 5α-reductase; testosterone Δ4-hydrogenase; 4-ene-3-oxosteroid 5α-reductase; reduced nicotinamide adenine dinucleotide phosphate:Δ4-3-ketosteroid 5α-oxidoreductase; 4-ene-5α-reductase; Δ4-3-ketosteroid 5α-oxidoreductase; cholest-4-en-3-one 5α-reductase; testosterone 5α-reductase; 3-oxo-5α-steroid 4-dehydrogenase. Cat No: EXWM-1297. | |
| 4-α-glucanotransferase | This entry covers the former separate entry for EC 2.4.1.3 (amylomaltase). The plant enzyme has been termed D-enzyme. An enzymic activity of this nature forms part of the mammalian and yeast glycogen debranching system (see EC 3.2.1.33 amylo-α-1,6-glucosidase). Group: Enzymes. Synonyms: disproportionating enzyme; dextrin glycosyltransferase; D-enzyme; debranching enzyme maltodextrin glycosyltransferase; amylomaltase; dextrin transglycosylase; 1,4-α-D-glucan:1,4-α-D-glucan 4-α-D-glycosyltransferase. Enzyme Commission Number: EC 2.4.1.25. CAS No. 9032-9-1. Amylomaltase. 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-2479; 4-α-glucanotransferase; EC 2.4.1.25; 9032-09-1; disproportionating enzyme; dextrin glycosyltransferase; D-enzyme; debranching enzyme maltodextrin glycosyltransferase; amylomaltase; dextrin transglycosylase; 1,4-α-D-glucan:1,4-α-D-glucan 4-α-D-glycosyltransferase. Cat No: EXWM-2479. | |
| 4-Bromo-3-hydroxybenzoic Acid | 4-Bromo-3-hydroxybenzoic acid is a potent inhibitor of the enzyme histidine decarboxylase with resultant inhibition of histamine formation in mammals. Synonyms: 4-bromo-3-hydroxybenzoic acid; 4-bromo-3-hydroxybenzoic acid. Grades: > 98 %. CAS No. 14348-38-0. Molecular formula: C7H5BrO3. Mole weight: 217.02. | |
| 5-Bromo-4-chloro-3-indolyl b-D-mannopyranoside | 5-Bromo-4-chloro-3-indolyl b-D-mannopyranoside is a compound widely used in the biomedical industry as an artificial chromogenic substrate. It is primarily employed in the detection and visualization of β-D-glucosidase enzyme activity. This compound finds applications in various biochemical assays, including determination of bacterial and mammalian β-D-glucosidase levels, providing valuable insights into drug discovery and disease research. Synonyms: X-Mannose. CAS No. 129787-67-3. Molecular formula: C14H15BrClNO6. Mole weight: 408.63. | |
| 5-Hydroxymethylcytosine | 5-Hydroxymethylcytosine (5hmC) is an oxidized forms of 5-methylcytosine (5mC) in mammalian DNA. 5-Hydroxymethylcytosine is produced from 5mC in an enzymatic pathway involving three 5mC oxidases, Ten-eleven translocation (TET)1, TET2, and TET3. The conversion of 5mC into 5hmC can be the first step in a pathway leading towards DNA demethylation. 5-Hydroxymethylcytosine is associated with gene transcription and frequently used as a mark to investigate dynamic DNA methylation conversion during mammalian development [1]. Uses: Scientific research. Group: Natural products. Alternative Names: 5hmC. CAS No. 1123-95-1. Pack Sizes: 5 mg; 10 mg; 25 mg. Product ID: HY-W018324. |  |
| 6-Chloro-5-(2,3-dichlorophenoxy)-2-methylthio-benzimidazole (Triclabendazole) | Triclabendazole is a member of the benzimidazole family of anthelmintics. It is effective against F. hepatica helminths that cause fascioliasis, reducing secreted protease enzyme activities that are critical for the invasion, migration, nutrition, and survival of the parasite.1 In yeast and mammalian cells, triclabendazole was shown to inhibit adenylyl cyclase in the Ras-adenylyl cyclase-protein kinase A nutrient-sensing pathway and to prevent apoptosis induced by the Parkinsons disease-related protein α-synuclein, demonstrating a protective role during various cellular stresses.2,3. Group: Biochemicals. Alternative Names: 5-Chloro-6- (2, 3-dichlorophenoxy) -2- methyl thiobenzimidazole; CGA-89317, egaten; Fasinex; Triclabendazole. Grades: Highly Purified. CAS No. 68786-66-3. Pack Sizes: 25g, 50g, 100g. Molecular Formula: C14H9Cl3N2OS, Molecular Weight: 359.66. US Biological Life Sciences. | Worldwide |
| 7, 12-Dimethylbenz [a]anthracene | A highly potent carcinogen that is activated by microsomal enzymes to a diol epoxide metabolite that binds covalently to DNA in mammalian cells, leading ultimately to tumor induction. Group: Biochemicals. Grades: Highly Purified. CAS No. 57-97-6. Pack Sizes: 1g. US Biological Life Sciences. | Worldwide |
| 8R-Brassicasterol | 8R-Brassicasterol is a by-product in the synthesis of Brassicasterol (B676850). Brassicasterol is a phytosterol found in canola oil, rapeseed oil, marine algae and shellfish. This compound has been shown to inhibit sterol Δ24-reductase, an enzyme involved in the mammalian cholesterol biosynthesis pathway. Group: Biochemicals. Grades: Highly Purified. Pack Sizes: 5mg, 10mg. Molecular Formula: C28H46O. US Biological Life Sciences. | Worldwide |
| Abl Kinase Mutant active human, Recombinant | Abelson murine leukemia viral oncogene homolog 1 also known as ABL1 is a protein that, in humans, is encoded by the ABL1 gene (previous symbol ABL) located on chromosome 9. c-Abl is sometimes used to refer to the version of the gene found within the mammalian genome, while v-Abl refers to the viral gene. Human abelson murine leukemia viral oncogene homolog 1 (abl-1) (genbank accession no. nm_007313), amino acids 248-531 with t334i mutation and n-terminal his-tag, mw = 33 kda, expressed in a baculovirus-infected sf9 cell expression system. Group: Enzymes. Synonyms: ABL1; JTK7; c-ABL; p150; Abl Kinase; ABL; bcr/abl; c-ABL1; v-abl. Abl Kinase. Mole weight: mol wt 33 kDa. Stability: -70°C. Form: aqueous solution. Source: Baculovirus infected Sf9 cells. Species: Human. ABL1; JTK7; c-ABL; p150; Abl Kinase; ABL; bcr/abl; c-ABL1; v-abl. Cat No: NATE-0013. | |
| ABTS Chromophore Diammonium Salt | ABTS Chromophore Diammonium Salt can inhibit catalase, a mammalian antioxidant enzyme which degrades hydrogen peroxide into water and oxygen species. Synonyms: 2,2'-(1,2-Hydrazinediylidene)bis[3-ethyl-2,3-dihydro-6-benzothiazolesulfonic Acid Ammonium Salt (1:2); 2,2'-Azinobis[3-ethyl-2,3-dihydro-6-benzothiazolesulfonic Acid Diammonium Salt; 3-Ethyl-2-oxo-6-Benzothiazolinesulfonic Acid Azine Diammonium Salt; 2,2'-Azino-bis-(3-ethyl-benzthiazoline-6-sulfonate) Diammonium Salt; 2,2'-Azinobis(3-ethylbenzothiazoline-6-sulfonic acid) Diammonium Salt; ABTS Diammonium Salt; Diammonium 2,2'-Azinobis(3-ethyl-6-benzothiazolinesulfonate); Diammonium 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonate). Grades: ≥98%. CAS No. 30931-67-0. Molecular formula: C18H24N6O6S4. Mole weight: 548.68. | |
| acetoacetate decarboxylase | Acetoacetate decarboxylase (AAD or ADC) is an enzyme involved in both the ketone body production pathway in humans and other mammals, and solventogenesis in bacteria. Acetoacetate decarboxylase plays a key role in solvent production by catalyzing the decarboxylation of acetoacetate, yielding acetone and carbon dioxide. This enzyme has been of particular interest because it is a classic example of how pKa values of ionizable groups in the enzyme active site can be significantly perturbed. Specifically, the pKa value of lysine 115 in the active site is unusually low, allowing for the formation of a Schiff base intermediate and catalysis. Group: Enzymes. Synonyms: acetoacetic acid decarboxylase; acetoacetate carboxy-lyase. Enzyme Commission Number: EC 4.1.1.4. CAS No. 9025-03-0. 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-4784; acetoacetate decarboxylase; EC 4.1.1.4; 9025-03-0; acetoacetic acid decarboxylase; acetoacetate carboxy-lyase. Cat No: EXWM-4784. | |
| Acetyl-CoA Carboxylase 1 from Human, Recombinant | Acetyl-CoA Carboxylase (ACC) regulates the metabolism of fatty acids. This enzyme catalzes the formation of Malonyl CoA through the irreversible carboxylation of acetyl CoA. There are two main isoforms of Acetyl-CoA carboxylase expressed in mammals, Acetyl-CoA carboxylase 1 (ACACA) and Acetyl-CoA carboxylase 2 (ACACB). ACACA has broad tissue distribution but is enriched in tissues critical for fatty acid sythesis such as adipose tissue. ACACB is enriched in tissues such as skeletal muscle and heart that are critical for fatty acid oxidation. The Acetyl-CoA Carboxylase enzymes are activated by Citrate, glutamate, and dicarboxylic acids and negatively regulated by long ...he study of enzyme kinetics, screening inhibitors, and selectivity profiling. Group: Enzymes. Synonyms: ACAC; ACACA; ACC1; ACC; ACCA; acetyl-CoA carboxylase alpha; acetyl coenzyme A carboxylase; acetyl-CoA carboxylase. Enzyme Commission Number: EC 6.4.1.2. CAS No. 9023-93-2. ACC. Mole weight: 292.5 kDa. Activity: > 20 units/μg protein. Storage: Store at -70°C. Avoid multiple freeze-thaw cycles. Form: Supplied as a solution in 50 mM Tris-HCl, pH 8.0, 275 mM NaCl, 10% glycerol, 1 mM EDTA and 2 mM DTT. Source: Sf9 cells. Species: Human. ACAC; ACACA; ACC1; ACC; ACCA; acetyl-CoA carboxylase alpha; acetyl coenzyme A carboxylase; acetyl-CoA carboxylase. Cat No: NATE-0942. | |
| Acetyl-CoA Carboxylase 2 from Human, Recombinant | Acetyl-CoA Carboxylase (ACC) regulates the metabolism of fatty acids. This enzyme catalzes the formation of Malonyl CoA through the irreversible carboxylation of acetyl CoA. There are two main isoforms of Acetyl-CoA carboxylase expressed in mammals, Acetyl-CoA carboxylase 1 (ACACA) and Acetyl-CoA carboxylase 2 (ACACB). ACACA has broad tissue distribution but is enriched in tissues critical for fatty acid sythesis such as adipose tissue. ACACB is enriched in tissues such as skeletal muscle and heart that are critical for fatty acid oxidation. The Acetyl-CoA Carboxylase enzymes are activated by Citrate, glutamate, and dicarboxylic acids and negatively regulated by long ...ercise. the enzyme also may be used for acc regulation study in anti-obesity and anti-type 2 diabetes therapeutics. Group: Enzymes. Synonyms: ACACB; ACC2; acetyl-CoA carboxylase beta; acetyl coenzyme A carboxylase; acetyl-CoA carboxylase. Enzyme Commission Number: EC 6.4.1.2. CAS No. 9023-93-2. ACC. Mole weight: 277 kDa. Activity: > 25 units/μg protein. Storage: Store at -70°C. Avoid multiple freeze-thaw cycles. Form: Supplied as a solution in 50 mM Tris-HCl, pH 8.0, 275 mM NaCl, 10% glycerol, 1 mM EDTA and 2 mM DTT. Source: Sf9 cells. Species: Human. ACACB; ACC2; acetyl-CoA carboxylase beta; acetyl coenzyme A carboxylase; acetyl-CoA carboxylase. Cat No: NATE-0943. | |
| Acetyl-Coenzyme A acetyltransferase 2 from Human, Recombinant | ACAT2 enzyme participates in lipid metabolism. ACAT2 takes part in lipoprotein assembly, catalyzing cholesterol esterification in mammalian cells. ACAT2 is an integral membrane protein that localizes to the endoplasmic reticulum of human intestinal cells. ACAT2 deficiency contributes to severe mental retardation and hypotonus. Acat2 recombinant human produced in e. coli is a single, non-glycosylated polypeptide chain containing 433 amino acids (1-397 a.a.) and having a molecular mass of 45.4 kda. the acat2 is fused to 36 amino acid his-tag at n-terminus and purified by proprietary chromatographic techniques. Group: Enzymes. Synonyms: Acetyl-CoA acetyltransferase cytosolic; Cytosolic acetoacetyl-CoA thiolase; ACAT2; Acetyl CoA transferase-like protein; ACAT-2. Purity: Greater than 95.0% as determined by SDS-PAGE. ACAT-2. Mole weight: 45.4 kDa. Stability: ACAT2 Human although stable at 4°C for 1 week, should be stored desiccated below -18°C. Please prevent freeze thaw cycles. Appearance: Sterile Filtered clear solution. Source: E. coli. Species: Human. Acetyl-CoA acetyltransferase cytosolic; Cytosolic acetoacetyl-CoA thiolase; ACAT2; Acetyl CoA transferase-like protein; ACAT-2. Cat No: NATE-0798. | |
| Acidic Mammalian Chitinase Inhibitor, Bisdionin F | A cell-permeable, competitive Acidic Mammalian Chitinase (AMCase) Inhibitor (IC50=0.92uM and Ki=0.42uM for hAMCase, and IC50=2.2uM for mAMCase, in vitro) that demonstrates 20-fold selectivity for hAMCase over hCHIT1. It is shown to decrease chitinase enzymatic activity (5mg/kg, i.p.) in the lungs of control PBS- and OVA-challenged mice. Furthermore, it attenuates lung chitinase activity, reduces eosinophil influx, and improves ventilatory function, in vivo, in a murine model of allergic inflammation. It also causes neutrophilia in the lungs of OVA-challenged mice. Group: Biochemicals. Alternative Names: AMCase Inhibitor, 3,7-dimethyl-1-(3-(3-methyl-2,6-dioxo-2,3,6,7-tetrahydro-1H-purin-1-yl)propyl)-1H-purine-2,6(3H,7H)-dione. Grades: Highly Purified. CAS No. 917877-86-2. Pack Sizes: 5mg. US Biological Life Sciences. | Worldwide |
| Adenosine deaminase Bovine, Recombinant | Adenosine deaminase is an enzyme (EC 3.5.4.4) involved in purine metabolism. It is needed for the breakdown of adenosine from food and for the turnover of nucleic acids in tissues. Present in virtually all mammalian cells, its primary function in Humans is the development and maintenance of the immune system. Protein determined by biuret. Applications: Adenosine deaminase is useful in various molecular biology assays, such as glycerol release assays. adenosine deaminase is a potential target for treatments of combined immunodeficiency disease. Group: Enzymes. Synonyms: ADA; adenosine deaminase; adenosine aminohydrolase; 9026-93-1; EC 3.5.4.4. Enzyme Commission Number: EC 3.5.4.4. CAS No. 9026-93-1. ADA. Mole weight: 32.5-33 kDa. Activity: 60-130 units/mg protein; > 130 units/mg protein; 150-200 units/mg protein. Storage: 2-8°C. Form: ammonium sulfate suspension. Suspension in 3.2 M (NH4)2SO4, 0.01 M potassium phosphate, pH 6.0. Source: E. coli. Species: Bovine. ADA; adenosine deaminase; adenosine aminohydrolase; 9026-93-1; EC 3.5.4.4. Cat No: NATE-0032. | |
| Adenosine deaminase from Human, Recombinant | Adenosine deaminase is an enzyme (EC 3.5.4.4) involved in purine metabolism. It is needed for the breakdown of adenosine from food and for the turnover of nucleic acids in tissues. Present in virtually all mammalian cells, its primary function in Humans is the development and maintenance of the immune system. Applications: Adenosine deaminase (ada) is a key enzyme in purine metabolism and is essential for normal immune function. it is important in the study of immune system diseases such as rheumatoid arthritis. Group: Enzymes. Synonyms: ADA; adenosine deaminase; adenosine aminohydrolase; 9026-93-1; EC 3.5.4.4. Enzyme Commission Number: EC 3.5.4.4. CAS No. 9026-93-1. ADA. Activity: >1 U/mL. Storage: Store at -20°C. Source: E. coli. Species: Human. ADA; adenosine deaminase; adenosine aminohydrolase; 9026-93-1; EC 3.5.4.4. Cat No: NATE-1583. | |
| Adenosine deaminase, Recombinant | Adenosine deaminase is an enzyme (EC 3.5.4.4) involved in purine metabolism. It is needed for the breakdown of adenosine from food and for the turnover of nucleic acids in tissues. Present in virtually all mammalian cells, its primary function in Humans is the development and maintenance of the immune system. Group: Enzymes. Synonyms: ADA; adenosine deaminase; adenosine aminohydrolase; 9026-93-1; EC 3.5.4.4. Enzyme Commission Number: EC 3.5.4.4. CAS No. 9026-93-1. Purity: > 90 %. ADA. Mole weight: About 53kDa (SDS-PAGE). Activity: 200U/mg protein. Appearance: White powder, lyophilized. Storage: Redissolved in 20% glycerol, 4°C, store at -20°C for long-term preservation, Avoid multiple freeze-thaw cycles. Source: E. coli. ADA; adenosine deaminase; adenosine aminohydrolase; 9026-93-1; EC 3.5.4.4. Cat No: NATE-1009. | |
| α(2-3,6,8) Neuraminidase from Clostridium perfringens, Recombinant | Neuraminidase enzymes are glycoside hydrolase enzymes (EC 3.2.1.18) that cleave the glycosidic linkages of neuraminic acids. Neuraminidase enzymes are a large family, found in a range of organisms. The best-known neuraminidase is the viral neuraminidase, a drug target for the prevention of the spread of influenza infection. The viral neuraminidases are frequently used as antigenic determinants found on the surface of the Influenza virus. Some variants of the influenza neuraminidase confer more virulence to the virus than others. Other homologs are found in mammalian cells, which have a range of functions. Neuraminidase is the common name for acetyl-neuraminyl hydrolase (sialidase). this neuraminidase catalyzes the hydrolysis of α2-3, α2-6, and α2-8 linked n-acetyl-neuraminic acid residues from glycoproteins and oligosaccharides. Group: Enzymes. Synonyms: neuraminidase; sialidase; α-ne. Purity: > 95% determined by SDS-PAGE. Neuraminidase. Mole weight: 43 kDa. Activity: ~225,000 units/mg. Storage: at -20°C. Form: 50 mM NaCl, 20 mM Tris-HCl (pH 7.5 25°C) and 5 mM Na2EDTA. Source: E. coli. Species: Clostridium perfringens. neuraminidase; sialidase; α-neuraminidase; acetylneuraminidase; exo-α-sialidase; EC 3.2.1.18; 9001-67-6; α(2-3,6,8) Neuraminidase. Cat No: NATE-1277. | |
| α(2-3) Neuraminidase from Salmonella typhimurium LT2, Recombinant | Neuraminidase enzymes are glycoside hydrolase enzymes (EC 3.2.1.18) that cleave the glycosidic linkages of neuraminic acids. Neuraminidase enzymes are a large family, found in a range of organisms. The best-known neuraminidase is the viral neuraminidase, a drug target for the prevention of the spread of influenza infection. The viral neuraminidases are frequently used as antigenic determinants found on the surface of the Influenza virus. Some variants of the influenza neuraminidase confer more virulence to the virus than others. Other homologs are found in mammalian cells, which have a range of functions. Α2-3 neuraminidase is a highly specific exogl... sialyl linkages and shows only trace activity against α2-8 sialyl linkages. Group: Enzymes. Synonyms: neuraminidase; sialidase; α-neuraminidase; acetylneuraminidase; exo-α-sialidase; EC 3.2.1.18; 9001-67-6. Neuraminidase. Mole weight: 41 kDa. Activity: ~11,300,000 units/mg. Storage: Store at 4°C or in small aliquots at -20°C. Avoid repeated freeze/thaw cycles. Form: 50 mM NaCl, 20 mM Tris-HCl (pH 7.5 25°C), and 5 mM Na2EDTA. Source: E. coli. Species: Salmonella typhimurium LT2. neuraminidase; sialidase; α-neuraminidase; acetylneuraminidase; exo-α-sialidase; EC 3.2.1.18; 9001-67-6; α(2-3) Neuraminidase. Cat No: NATE-1276. | |
| α(2-3) Neuraminidase S from Streptococcus pneumoniae, Recombinant | Neuraminidase enzymes are glycoside hydrolase enzymes (EC 3.2.1.18) that cleave the glycosidic linkages of neuraminic acids. Neuraminidase enzymes are a large family, found in a range of organisms. The best-known neuraminidase is the viral neuraminidase, a drug target for the prevention of the spread of influenza infection. The viral neuraminidases are frequently used as antigenic determinants found on the surface of the Influenza virus. Some variants of the influenza neuraminidase confer more virulence to the virus than others. Other homologs are found in mammalian cells, which have a range of functions. Neuraminidase is the common name for acetyl-neurami...;2-3 linked n-acetyl-neuraminic acid residues from glycoproteins and oligosaccharides. Group: Enzymes. Synonyms: neuraminidase; sialidase; α-neuraminidase; acetylneuraminidase; exo-α-sialidase; EC 3.2.1.18; 9001-67-6. Purity: > 95% determined by SDS-PAGE. Neuraminidase. Mole weight: 74000 daltons. Activity: 160,000 units/mg. Storage: at -20°C. Form: 50 mM NaCl, 20 mM Tris-HCl (pH 7.5 25°C) and 1 mM EDTA. Source: E. coli. Species: Streptococcus pneumoniae. neuraminidase; sialidase; α-neuraminidase; acetylneuraminidase; exo-α-sialidase; EC 3.2.1.18; 9001-67-6; α(2-3) Neuraminidase S; α(2-3) Neuraminidase. Cat No: NATE-1275. | |
| α-Amylase from Bacillus subtilis, Recombinant | α-Amylase is a protein enzyme EC 3.2.1.1 that hydrolyses alpha bonds of large, alpha-linked polysaccharides, such as starch and glycogen, yielding glucose and maltose. It is the major form of amylase found in Humans and other mammals. It is also present in seeds containing starch as a food reserve, and is secreted by many fungi. Group: Enzymes. Synonyms: glycogenase; αamylase, α-amylase; 1,4-α-D-glucan glucanohydrolase; EC 3.2.1.1; 9001-19-8; endoamylase; Taka-amylase A. Enzyme Commission Number: EC 3.2.1.1. CAS No. 9000-90-2. Purity: > 95 % as judged by SDS-PAGE. α-Amylase. Mole weight: 72550.6 Da. Activity: 4449.51 U/mg. Storage: Store at 4°C (shipped at room temperature). Form: Supplied in 3.2 M ammonium sulphate. Source: Bacillus subtilis subsp. subtilis str. 168. glycogenase; αamylase, α-amylase; 1,4-α-D-glucan glucanohydrolase; EC 3.2.1.1; 9001-19-8; endoamylase; Taka-amylase A. Cat No: NATE-1172. | |
| α-Amylase from Bacteroides fragilis, Recombinant | α-Amylase is a protein enzyme EC 3.2.1.1 that hydrolyses alpha bonds of large, alpha-linked polysaccharides, such as starch and glycogen, yielding glucose and maltose. It is the major form of amylase found in Humans and other mammals. It is also present in seeds containing starch as a food reserve, and is secreted by many fungi. Group: Enzymes. Synonyms: glycogenase; αamylase, α-amylase; 1,4-α-D-glucan glucanohydrolase; EC 3.2.1.1; 9001-19-8; endoamylase; Taka-amylase A. Enzyme Commission Number: EC 3.2.1.1. CAS No. 9000-90-2. Purity: > 95 % as judged by SDS-PAGE. α-Amylase. Mole weight: 59099.7 Da. Activity: 36.25 U/mg. Storage: Store at 4°C (shipped at room temperature). Form: Supplied in 3.2 M ammonium sulphate. Source: Bacteroides fragilis NCTC 9343. glycogenase; αamylase, α-amylase; 1,4-α-D-glucan glucanohydrolase; EC 3.2.1.1; 9001-19-8; endoamylase; Taka-amylase A. Cat No: NATE-1173. | |
| α-Amylase from Escherichia coli, Recombinant | α-Amylase is a protein enzyme EC 3.2.1.1 that hydrolyses alpha bonds of large, alpha-linked polysaccharides, such as starch and glycogen, yielding glucose and maltose. It is the major form of amylase found in Humans and other mammals. It is also present in seeds containing starch as a food reserve, and is secreted by many fungi. Group: Enzymes. Synonyms: glycogenase; αamylase, α-amylase; 1,4-α-D-glucan glucanohydrolase; EC 3.2.1.1; 9001-19-8; endoamylase; Taka-amylase A. Enzyme Commission Number: EC 3.2.1.1. CAS No. 9000-90-2. Purity: > 95 % as judged by SDS-PAGE. α-Amylase. Mole weight: 60459.5 Da. Activity: 23.61 U/mg. Storage: Store at 4°C (shipped at room temperature). Form: Supplied in 3.2 M ammonium sulphate. Source: Escherichia coli str. K-12 substr. W3110. glycogenase; αamylase, α-amylase; 1,4-α-D-glucan glucanohydrolase; EC 3.2.1.1; 9001-19-8; endoamylase; Taka-amylase A. Cat No: NATE-1174. | |
| α-Lactose hydrate | α-Lactose (hydrate) (α-D-Lactose (hydrate)) is the principal carbohydrate in the milk of most mammals. α-Lactose (hydrate) consists of glucose and galactose and exists in the form of two anomers, α and &beta. α-Lactose (hydrate) has many uses in the food and pharmaceutical industries, such as a free-flowing or agglomerating agent, a diluent for pigments, flavors, or enzymes [1] [2] [3]. Uses: Scientific research. Group: Natural products. Alternative Names: α-D-Lactose hydrate. CAS No. 5989-81-1. Pack Sizes: 10 mM * 1 mL; 500 g. Product ID: HY-W087904. | |
| α-tubulin N-acetyltransferase | The enzyme from Chlamydomonas flagella also acetylates mammalian brain α-tubulin. Group: Enzymes. Synonyms: α-tubulin acetylase; TAT; α-tubulin acetyltransferase; tubulin N-acetyltransferase; acetyl-CoA:α-tubulin-L-lysine N-acetyltransferase; acetyl-CoA:[α-tubulin]-L-lysine 6-N-acetyltransferase. Enzyme Commission Number: EC 2.3.1.108. CAS No. 99889-90-4. 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-2046; α-tubulin N-acetyltransferase; EC 2.3.1.108; 99889-90-4; α-tubulin acetylase; TAT; α-tubulin acetyltransferase; tubulin N-acetyltransferase; acetyl-CoA:α-tubulin-L-lysine N-acetyltransferase; acetyl-CoA:[α-tubulin]-L-lysine 6-N-acetyltransferase. Cat No: EXWM-2046. | |
| aminopeptidase B | Cytosolic or membrane-associated enzyme from mammalian tissues, activated by chloride ions and low concentrations of thiol compounds. This is one of the activities of the bifunctional enzyme EC 3.3.2.6 (membrane alanyl aminopeptidase family). Group: Enzymes. Synonyms: arylamidase II; arginine aminopeptidase; arginyl aminopeptidase; Cl--activated arginine aminopeptidase; cytosol aminopeptidase IV; L-arginine aminopeptidase. Enzyme Commission Number: EC 3.4.11.6. CAS No. 9073-92-1. 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-4027; aminopeptidase B; EC 3.4.11.6; 9073-92-1; arylamidase II; arginine aminopeptidase; arginyl aminopeptidase; Cl--activated arginine aminopeptidase; cytosol aminopeptidase IV; L-arginine aminopeptidase. Cat No: EXWM-4027. | |
| AMPK Signaling Agonist, F17 (4-hydroxy-1-isobutyl-N-(5-methylthiazol-2-yl)-2-oxo-1,2-dihydroquinoline-3-carboxamide) | A cell-permeable 4-hydroxy-2-oxo quinoline carboxamide that acts as an agonist of AMPK signaling. It is shown to reduce fat storage in C. elegans (EC50 ~0.1uM) and reduce the expression level of fat-7 (a C. elegans ortholog of mammalian stearoyl-CoA desaturase-1), through aak-1 (an ortholog for the AMPK-a1 catalytic subunit) and K08F8.2 (a transcription factor) dependent mechanisms. In addition, it markedly reduces the number of lipid droplets in HepG2 human hepatocarcinoma cells at 25uM, and elicits the phosphorylation and inactivation of acetyl coenzyme A carboxylase (ACC, the enzyme that catalyzes the rate-limiting step in de novo fatty acid synthesis). F17-induced ACC phosphorylation can be abrogated by simultaneous treatment with an AMPK inhibitor compound C. Group: Biochemicals. Grades: Highly Purified. CAS No. 280112-24-5. Pack Sizes: 5mg. US Biological Life Sciences. | Worldwide |
| Amylase 126A from Clostridium perfringens, Recombinant | α-Amylase is a protein enzyme EC 3.2.1.1 that hydrolyses alpha bonds of large, alpha-linked polysaccharides, such as starch and glycogen, yielding glucose and maltose. It is the major form of amylase found in Humans and other mammals. It is also present in seeds containing starch as a food reserve, and is secreted by many fungi. Group: Enzymes. Synonyms: glycogenase; αamylase, α-amylase; 1,4-α-D-glucan glucanohydrolase; EC 3.2.1.1; 9001-19-8; endoamylase; Taka-amylase A. Enzyme Commission Number: EC 3.2.1.1. CAS No. 9000-90-2. Purity: >90% by SDS-PAGE. α-Amylase. Mole weight: 40.4 kDa. Storage: This enzyme is shipped at room temperature but should be stored at -20 °C. Form: 35 mM NaHepes buffer, pH 7.5, 750 mM NaCl, 200 mM imidazol, 3.5 mM CaCl2, 0.02% sodium azide and 25% (v/v) glycerol. Source: E. coli. Species: Clostridium perfringens. glycogenase; αamylase, α-amylase; 1,4-α-D-glucan glucanohydrolase; EC 3.2.1.1; 9001-19-8; endoamylase; Taka-amylase A; Amylase 126A. Cat No: NATE-1302. | |
| Amylase 13A from Bacillus licheniformis, Recombinant | α-Amylase is a protein enzyme EC 3.2.1.1 that hydrolyses alpha bonds of large, alpha-linked polysaccharides, such as starch and glycogen, yielding glucose and maltose. It is the major form of amylase found in Humans and other mammals. It is also present in seeds containing starch as a food reserve, and is secreted by many fungi. Group: Enzymes. Synonyms: glycogenase; αamylase, α-amylase; 1,4-α-D-glucan glucanohydrolase; EC 3.2.1.1; 9001-19-8; endoamylase; Taka-amylase A. Enzyme Commission Number: EC 3.2.1.1. CAS No. 9000-90-2. Purity: >90% by SDS-PAGE. α-Amylase. Mole weight: 57.4 kDa. Storage: This enzyme is shipped at room temperature but should be stored at -20 °C. Form: 35 mM NaHepes buffer, pH 7.5, 750 mM NaCl, 200 mM imidazol, 3.5 mM CaCl2, 0.02% sodium azide and 25% (v/v) glycerol. Source: E. coli. Species: Bacillus licheniformis. glycogenase; αamylase, α-amylase; 1,4-α-D-glucan glucanohydrolase; EC 3.2.1.1; 9001-19-8; endoamylase; Taka-amylase A; Amylase 13A. Cat No: NATE-1300. | |
| Amylase 13A from Escherichia coli, Recombinant | α-Amylase is a protein enzyme EC 3.2.1.1 that hydrolyses alpha bonds of large, alpha-linked polysaccharides, such as starch and glycogen, yielding glucose and maltose. It is the major form of amylase found in Humans and other mammals. It is also present in seeds containing starch as a food reserve, and is secreted by many fungi. Group: Enzymes. Synonyms: glycogenase; αamylase, α-amylase; 1,4-α-D-glucan glucanohydrolase; EC 3.2.1.1; 9001-19-8; endoamylase; Taka-amylase A. Enzyme Commission Number: EC 3.2.1.1. CAS No. 9000-90-2. Purity: >90% by SDS-PAGE. α-Amylase. Mole weight: 58.6 kDa. Storage: This enzyme is shipped at room temperature but should be stored at -20 °C. Form: 35 mM NaHepes buffer, pH 7.5, 750 mM NaCl, 200 mM imidazol, 3.5 mM CaCl2, 0.02% sodium azide and 25% (v/v) glycerol. Source: E. coli. Species: Escherichia coli. glycogenase; αamylase, α-amylase; 1,4-α-D-glucan glucanohydrolase; EC 3.2.1.1; 9001-19-8; endoamylase; Taka-amylase A; Amylase 13A. Cat No: NATE-1304. | |
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