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| Product | Description | |
|---|---|---|
| 2,6-Dichlorobenzonitrile | 2,6-Dichlorobenzonitrile (DCBN or dichlobenil) is a herbicide and is slightly toxic for humans. It is metabolized in the liver by the enzyme CYP2A6. Group: Biochemicals. Grades: Highly Purified. CAS No. 1194-65-6. Pack Sizes: 50g, 100g. Molecular Formula: C7H3Cl2N, Molecular Weight: 172.01. US Biological Life Sciences. |  Worldwide |
| 2,6-Dichlorobenzonitrile-13C6 | 2,6-Dichlorobenzonitrile-13C6 is the isotope labelled analog of 2,6-Dichlorobenzonitrile (D431945); a herbicide that is slightly toxic for humans and is metabolized in the liver by the enzyme CYP2A6. Group: Biochemicals. Grades: Highly Purified. Pack Sizes: 1mg, 10mg. Molecular Formula: C13C6H3Cl2N, Molecular Weight: 177.97. US Biological Life Sciences. | Worldwide |
| 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. |  |
| (3aR,4R,12R,12aR)-3a,4,12,12a-Tetrahydro-2,2-dimethyl-4,12-epoxy-5H,8H-1,3-dioxolo[4,5-e]pyrimido[2,1-b][1,3]oxazocin-8-one | (3aR,4R,12R,12aR)-3a,4,12,12a-Tetrahydro-2,2-dimethyl-4,12-epoxy-5H,8H-1,3-dioxolo[4,5-e]pyrimido[2,1-b][1,3]oxazocin-8-one is a potential drug being studied in biomedicine to treat various types of cancer. It has been found to inhibit the enzyme MELK, which is overexpressed in certain cancer cells. Studies have shown promising results in inhibiting the growth of tumors in preclinical models and further research is being conducted to determine its safety and efficacy in humans. Synonyms: 2',3'-O-isopropylidene-5',6-anhydrouridine. CAS No. 3868-21-1. Molecular formula: C12H14N2O5. Mole weight: 266.25. |  |
| 3-dehydrosphinganine reductase | 3-dehydrosphinganine reductase (EC 1.1.1.102) also known as 3-ketodihydrosphingosine reductase (KDSR) or follicular variant translocation protein 1 (FVT1) is an enzyme that in humans is encoded by the KDSR gene. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. This enzyme participates in sphingolipid metabolism. Group: Enzymes. Synonyms: D-3-dehydrosphinganine reductase; D-3-oxosphinganine reductase; DSR; 3-oxosphinganine reductase; 3-oxosphinganine:NADPH oxidoreductase; D-3-oxosphinganine:B-NADPH oxidoreductase. Enzyme Commission Number: EC 1.1.1.102. CAS No. 37250-36-5. 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-0005; 3-dehydrosphinganine reductase; EC 1.1.1.102; 37250-36-5; D-3-dehydrosphinganine reductase; D-3-oxosphinganine reductase; DSR; 3-oxosphinganine reductase; 3-oxosphinganine:NADPH oxidoreductase; D-3-oxosphinganine:B-NADPH oxidoreductase. Cat No: EXWM-0005. | |
| 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. | |
| 5-Lipoxygenase from human, Recombinant | Arachidonate 5-lipoxygenase, also known as ALOX5, 5-lipoxygenase, 5-LOX, or 5-LO, is an enzyme that in humans is encoded by the ALOX5 gene. Arachidonate 5-lipoxygenase is a member of the lipoxygenase family of enzymes. It transforms EFAs into leukotrienes and is a current target for pharmaceutical intervention in a number of diseases. Group: Enzymes. Synonyms: Arachidonate 5-lipoxygenase; ALOX5; 5-lipoxygenase; 5-LOX; 5-LO; 5LPG; LOG5. Enzyme Commission Number: EC 1.13.11.34. CAS No. 80619-02-9. Lipoxygenase. Mole weight: 78 kDa. Activity: 1,259.96 U/ml. Stability: As supplied, 6 months from the QC date provided on the Certificate of Analysis, when stored properly. Storage: at -80°C. Form: A solution in 100 mM Tris-HCl, pH 8.0, containing 5 mM EGTA, 1mM CaCl2, and 30% glycerol. Source: S9 insect cells. Species: Human. Arachidonate 5-lipoxygenase; ALOX5; 5-lipoxygenase; 5-LOX; 5-LO; 5LPG; LOG5. Cat No: NATE-1249. | |
| 7,8-Dihydro-D-Neopterin | 7,8-Dihydro-D-Neopterin is an intermediate in the biosynthesis of Biopterin (sc-204781). 7,8-Dihydro-D-Neopterin, also known as Dihydroneopterin, is closely related to tetrahydrobiopterin, an important cofactor in humans. Applications: An intermediate in the biosynthesis of tetrahydrobiopterin. Group: Coenzymes. Synonyms: 7,8-Dihydroneopterin; Dihydroneopterin. CAS No. 1218-98-0. Mole weight: 255.2. Appearance: Powder. Form: Solid. 7,8-Dihydroneopterin; Dihydroneopterin; 7,8-Dihydro-D-Neopterin; 1218-98-0. Cat No: COEC-063. | |
| 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. | |
| 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. | |
| 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. | |
| Alanine Racemase (Crude Enzyme) | This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on amino acids and derivatives. This enzyme participates in alanine and aspartatemetabolism and D-alanine metabolism. It employs one cofactor, pyridoxal phosphate. At least two compounds, 3-Fluoro-D-alanine and D-Cycloserine are known to inhibit this enzyme. The D-alanine produced by alanine racemase is used for peptidoglycan biosynthesis. Peptidoglycan is found in the cell walls of all bacteria, including many which are harmful to humans. The enzyme is absent in higher eukaryotes but found everywhere in prokaryotes, making alanine racemase a great target for antimicrobial drug...udies have shown that without the alr gene being expressed, the bacteria would need an external source of D-alanine in order to survive. Therefore, the alr gene is a feasible target for antimicrobial drugs. This product with the indicated enzyme activity was briefly purified from engineered E. coli. Applications: Drug development; pharmacology; medicine; pharmacology. Group: Enzymes. Synonyms: L-alanine racemase. Enzyme Commission Number: EC 5.1.1.1. CAS No. 9024-06-0. Alanine Racemase. Activity: Undetermined. Appearance: Clear to translucent yellow solution. Storage: at -20 °C or lower, for at least 1 month. Source: E. coli. L-alanine racemase. Pack: 100ml. Cat No: NATE-1854. | |
| Alanine-Valine transaminase (Crude Enzyme) | Branched chain aminotransferase is an aminotransferase enzyme which acts upon branched-chain amino acids. It uses largely α-ketoglutarate in forming branched chain α-keto acids and glutamate. The biological function of branched chain aminotransferases (BCAT) is to catalyse the synthesis or degradation of the branched chain amino acids leucine, isoleucine, and valine. In humans, branched chain amino acids are essential and are degraded by BCATs. This product with the indicated enzyme activity was briefly purified from engineered E. coli. Applications: Nutrition. Group: Enzymes. Synonyms: Transaminase B; branched-chain amino acid aminotransferase; branched-chain amino acid-glutamate Transaminase; branched-chain aminotransferase; L-branched chain amino acid aminotransferase; glutamate-branched-chain amino acid Transaminase. Enzyme Commission Number: EC 2.6.1.42. CAS No. 9054-65-3. Activity: Undetermined. Appearance: Clear to translucent yellow solution. Storage: at -20 °C or lower, for at least 1 month. Source: E. coli. Transaminase B; branched-chain amino acid aminotransferase; branched-chain amino acid-glutamate Transaminase; branched-chain aminotransferase; L-branched chain amino acid aminotransferase; glutamate-branched-chain amino acid Transaminase. Pack: 100ml. Cat No: NATE-1821. | |
| 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. | |
| Alcohol dehydrogenase from Human, 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-alcohol dehydrogenase; NADH-aldehyde dehydrogenase; primary alcoh. Enzyme Commission Number: EC 1.1.1.2. Alcohol dehydrogenase. Mole weight: 36573.0 Da. Source: Human. 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 1.1.1.2. Cat No: NATE-1197. | |
| Alcohol Dehydrogenase (NADP+ dependent) from E. coli, Recombinant | Alcohol dehydrogenase [NADP+] also known as aldehyde reductase or aldo-keto reductase family 1 member A1 is an enzyme that in humans is encoded by the AKR1A1 gene. This gene encodes a member of the aldo/keto reductase superfamily, which consists of more than 40 known enzymes and proteins. This member, also known as aldehyde reductase, is involved in the reduction of biogenic and xenobiotic aldehydes and is present in virtually every tissue. Alternative splicing of this gene results in two transcript variants encoding the same protein. Group: Enzymes. Synonyms: EC 1.1.1.2; Aromatic Alcohol Dehydrogenase; Alcohol:NADP+ oxidoreductase; AKR1A1; ALDR1; ALR; . Enzyme Commission Number: EC 1.1.1.2. CAS No. 9028-12-0. ALR. Activity: >500 U/ml. Form: Liquid. Source: E. coli. Species: E. coli. EC 1.1.1.2; Aromatic Alcohol Dehydrogenase; Alcohol:NADP+ oxidoreductase; AKR1A1; ALDR1; ALR; ARM; DD3; HEL-S-6; aldehyde reductase; aldo-keto reductase family 1 member A1; alcohol dehydrogenase (NADP+); aldehyde reductase (NADPH2); NADP-alcohol dehydrogenase; NADP+-aldehyde reductase; NADP+-dependent aldehyde reductase; NADPH-aldehyde reductase; NADPH-dependent aldehyde reductase; nonspecific succinic semialdehyde reductase; ALR 1; low-Km aldehyde reductase; high-Km aldehyde reductase; alcohol dehydrogenase (NADP). Cat No: NATE-1589. | |
| α-1,4-Galactosyltransferase from Neisseria meningitides, Recombinant | Lactosylceramide 4-alpha-galactosyltransferase is an enzyme that in humans is encoded by the A4GALT gene. The protein encoded by this gene catalyzes the transfer of galactose to lactosylceramide to form globotriaosylceramide, which has been identified as the P(k) antigen of the P blood group system. The encoded protein, which is a type II membrane protein found in the Golgi, is also required for the synthesis of the bacterial verotoxins receptor. Group: Enzymes. Synonyms: lactosylceramide 4-alpha-galactosyltransferase; Galbeta1-4Glcbeta1-Cer alpha1,4-galactosyltransferase; globotriaosylceramide/CD77 synthase; histo-blood group Pk UDP-ga. Enzyme Commission Number: EC 2.4.1.228. CAS No. 52725-57-2. Purity: min 95% by SDS-PAGE. Galactosyltransferase. Mole weight: 34 kDa. Source: E. coli. Species: Neisseria meningitides. lactosylceramide 4-alpha-galactosyltransferase; Galbeta1-4Glcbeta1-Cer alpha1,4-galactosyltransferase; globotriaosylceramide/CD77 synthase; histo-blood group Pk UDP-galactose; UDP-galactose:lactosylceramide 4II-alpha-D-galactosyltransferase; UDP-galactose:beta-D-galactosyl-(1->4)-D-glucosyl(1<->1)ceramide 4II-alpha-D-galactosyltransferase; UDP-galactose:beta-D-galactosyl-(1->4)-D-glucosyl-(1<->1)-ceramide 4II-alpha-D-galactosyltransferase; α-1,4-Galactosyltransferase. Cat No: NATE-1479. | |
| α-1,6-Fucosidase solution from Elizabethkingia miricola, Recombinant | Tissue alpha-L-fucosidase is an enzyme that in humans is encoded by the FUCA1 gene. Alpha-Fucosidase is an enzyme that breaks down fucose. Fucosidosis is an autosomal recessive lysosomal storage disease caused by defective alpha-L-fucosidase with accumulation of fucose in the tissues. Different phenotypes include clinical features such as neurologic deterioration, growth retardation, visceromegaly, and seizures in a severe early form; coarse facial features, angiokeratoma corporis diffusum, spasticity and delayed psychomotor development in a longer surviving form; and an unusual spondylometaphyseoepiphyseal dysplasia in yet another form. Group: Enzymes. Synonyms: α-1,6-Fucosidase; alpha-L-fucosidase; Alpha-Fucosidase; FUCA1; FUCA; 9037-65-4. Enzyme Commission Number: EC 3.2.1.51. CAS No. 9037-65-4. FUCA. Activity: > 1.8 units/mg protein. Storage: 2-8°C. Form: buffered aqueous solution, Solution in 20 mM Tris-HCl, pH 7.5, 25 mM NaCl. Source: E. coli. Species: Elizabethkingia miricola. α-1,6-Fucosidase; alpha-L-fucosidase; Alpha-Fucosidase; FUCA1; FUCA; 9037-65-4. Pack: 0.04 unit in glass bottle. Cat No: NATE-0264. | |
| 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. | |
| amidophosphoribosyltransferase | Amidophosphoribosyltransferase (ATase), also known as glutamine phosphoribosylpyrophosphate amidotransferase (GPAT), is an enzyme responsible for catalyzing the conversion of 5-phosphoribosyl-1-pyrophosphate (PRPP) into 5-phosphoribosyl-1-amine (PRA), using the ammonia group from a glutamine side-chain. This is the committing step in de novo purine synthesis. In humans it is encoded by the PPAT (phosphoribosyl pyrophosphate amidotransferase) gene. ATase is a member of the purine/pyrimidine phosphoribosyltransferase family. Group: Enzymes. Synonyms: phosphoribosyldiphosphate 5-amidotransfer. Enzyme Commission Number: EC 2.4.2.14. CAS No. 9031-82-7. 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-2641; amidophosphoribosyltransferase; EC 2.4.2.14; 9031-82-7; phosphoribosyldiphosphate 5-amidotransferase; glutamine phosphoribosyldiphosphate amidotransferase; α-5-phosphoribosyl-1-pyrophosphate amidotransferase; 5'-phosphoribosylpyrophosphate amidotransferase; 5-phosphoribosyl-1-pyrophosphate amidotransferase; 5-phosphororibosyl-1-pyrophosphate amidotransferase; glutamine 5-phosphoribosylpyrophosphate amidotransferase; glutamine ribosylpyrophosphate 5-phosphate amidotransferase; phosphoribose pyrophosphate amidotransferase; phosphoribosyl pyrophosphate amidotransfe | |
| Aminopeptidase N Inhibitor | Membrane alanyl aminopeptidase is also known as alanyl aminopeptidase (AAP) or aminopeptidase N (AP-N), which is an enzyme that in humans is encoded by the ANPEP gene. Aminopeptidase N (AP-N) inhibitor is a reversible inhibitor of AP-N/CD13 (IC50 = 25 μM). It is selective for AP-N/CD13 over matrix metalloproteinase-9 (MMP-9), angiotensin converting enzyme (ACE), neutral endopeptidase (NEP), γ-glutamyl transpeptidase, and the serine proteases dipeptidyl peptidase 4 (DPP-4) and cathepsin G at a concentration of 1 mM. AP-N inhibitor is non-cytotoxic to U937 cells at a concentration of 100 μM. Human aminopeptidase N is a receptor for one strain of human coronavirus that is an important cause of upper respiratory tract infections. Defects in this gene appear to be a cause of various types of leukemia or lymphoma. Synonyms: AP-N Inhibitor. Grades: ≥95%. CAS No. 596108-59-7. Molecular formula: C17H10N2O8. Mole weight: 370.27. | |
| 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. | |
| Amylase 13A from Streptococcus mutans, 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: 58.4 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: Streptococcus mutans. 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-1301. | |
| Amylase 57C from Thermotoga maritima, 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: 48.0 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: Thermotoga maritima. glycogenase; αamylase, α-amylase; 1,4-α-D-glucan glucanohydrolase; EC 3.2.1.1; 9001-19-8; endoamylase; Taka-amylase A; Amylase 57C. Cat No: NATE-1303. | |
| arachidonate 5-lipoxygenase | Arachidonate 5-lipoxygenase, also known as ALOX5, 5-lipoxygenase, 5-LOX, or 5-LO, is a non-heme iron-containing enzyme (EC 1.13.11.34) that in humans is encoded by the ALOX5 gene. Arachidonate 5-lipoxygenase is a member of the lipoxygenase family of enzymes. It transforms EFA substrates into leukotrienes as well as a wide range of other biologically active products. ALOX5 is a current target for pharmaceutical intervention in a number of diseases. Group: Enzymes. Synonyms: leukotriene-A4 synthase; Δ5-lipoxygenase; 5Δ-lipoxygenase; arachidonic 5-lipoxygenase; arachidonic acid 5-lipoxygenase; C-5-lipoxygenase; LTA synthase; leukotriene A4 synthase. Enzyme Commission Number: EC 1.13.11.34. CAS No. 80619-02-9. Lipoxygenase. 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-0553; arachidonate 5-lipoxygenase; EC 1.13.11.34; 80619-02-9; leukotriene-A4 synthase; Δ5-lipoxygenase; 5Δ-lipoxygenase; arachidonic 5-lipoxygenase; arachidonic acid 5-lipoxygenase; C-5-lipoxygenase; LTA synthase; leukotriene A4 synthase. Cat No: EXWM-0553. | |
| Aurora Kinase A active human, Recombinant | Aurora A kinase also known as serine/threonine-protein kinase 6 is an enzyme that in humans is encoded by the AURKA gene. Aurora A is a member of a family of mitotic serine/threonine kinases. It is implicated with important processes during mitosis and meiosis whose proper function is integral for healthy cell proliferation. Aurora A is activated by one or more phosphorylations and its activity peaks during the G2 phase to M phase transition in the cell cycle. Human aurora kinase a (genbank accession no. nm_003600), amino acids 2-403 with n-terminal his6-tag, mw=50 kda, expressed in a baculovirus infected sf9 cell expression system. Applications: Useful for the study of enzyme kinetics, screening inhibitors, and selectivity profiling. Group: Enzymes. Synonyms: Aurora Kinase A; Aurora A kinase; serine/threonine-protein kinase 6; AURKA; AIK; ARK1; AURA; AURORA2; BTAK; PPP1R47; STK15; STK6; STK7. Purity: > 90% (SDS-PAGE). ARK1. Mole weight: mol wt 50 kDa. Activity: ~17,000 units/mg protein. Form: aqueous solution. Source: baculovirus infected Sf9 cells. Species: Human. Aurora Kinase A; Aurora A kinase; serine/threonine-protein kinase 6; AURKA; AIK; ARK1; AURA; AURORA2; BTAK; PPP1R47; STK15; STK6; STK7. Pack: Minimum 50 ng protein/vial by Bradford. Cat No: NATE-0087. | |
| Benzyl 2-O-[2-(Acetylamino)-2-deoxy-β-D-glucopyranosyl]-α-D-mannopyranoside | A product formed from Benzyl α-D-mannopyranoside by α-3-D-mannoside by the enzyme UDP-GlcNAc:α-3-D-mannoside β1,2-N-acetylglucosaminyltransferase I.2 in humans. Synonyms: GlcNAc(β1-2)Man(α1-)O-benzyl; Phenylmethyl 2-O-[2-(Acetylamino)-2-deoxy-D-glucopyranosyl]-α-D-mannopyranoside. CAS No. 436853-00-8. Molecular formula: C21H31NO11. Mole weight: 473.37. | |
| β-Ala-His dipeptidase | Present in the serum of humans and higher primates, but not in the serum of other mammals. Activated by Cd2+ and citrate. Belongs in peptidase family M20. Group: Enzymes. Synonyms: serum carnosinase. Enzyme Commission Number: EC 3.4.13.20. CAS No. 525589-43-9. 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-4034; β-Ala-His dipeptidase; EC 3.4.13.20; 525589-43-9; serum carnosinase. Cat No: EXWM-4034. | |
| β-D-Glucuronidase from Bacteria, Recombinant | β-glucuronidase catalyzes the breakdown of complex carbohydrates. In humans it converts conjugated bilirubin into the unconjugated form, making bilirubin suitable for reabsorption. Group: Enzymes. Synonyms: β-glucuronide glucuronohydrolase glucuronidase; exo-β-D-glucuronidase; ketodase; EC 3.2.1.31; 9001-45-0; β-D-glucuronoside glucuronosohydrolase; GUSB. Enzyme Commission Number: EC 3.2.1.31. CAS No. 9001-45-0. GUSB. Mole weight: 68 kD (SDS-PAGE). Activity: > 170 U/mg protein. Storage: Below -20°C. Form: Glycerol Solution. Source: E. coli. Species: Bacteria. β-glucuronide glucuronohydrolase glucuronidase; exo-β-D-glucuronidase; ketodase; EC 3.2.1.31; 9001-45-0; β-D-glucuronoside glucuronosohydrolase; GUSB. Cat No: NATE-1036. | |
| Bifidobacterium longum | A probiotic used in dietary supplements for humans and animals. Applications: Dietary supplements. Group: Enzymes. Synonyms: Bifidobacterium longum. Probiotic. Appearance: powder or liquid. Source: Bifidobacterium longum. Bifidobacterium longum. Pack: 25kg/paper barrel (powder form), 30kg/polyster barrel (liquid form). Cat No: DIS-1015. | |
| Bifunctional Chimeras of Glutamylcysteine Synthetase and Glutathione Synthetase (Crude Enzyme) | GSH, and by extension GCL, is critical to cell survival. Nearly every eukaryotic cell, from plants to yeast to humans, expresses a form of the GCL protein for the purpose of synthesizing GSH. To further highlight the critical nature of this enzyme, genetic knockdown of GCL results in embryonic lethality. Furthermore, dysregulation of GCL enzymatic function and activity is known to be involved in the vast majority of human diseases, such as diabetes, Parkinson's disease, Alzheimers disease, COPD, HIV/AIDS, and cancer. This typically involves impaired function leading to decreased GSH biosynthesis, reduced cellular antioxidant capacity, and the in...se forming carbon-nitrogen bonds as acid-D-amino-acid ligases (peptide synthases). This product with the indicated enzyme activity was briefly purified from engineered E. coli. Applications: Agriculture; medicine; synthesis; biotechnology; pharmacology. Group: Enzymes. Enzyme Commission Number: EC 6.3.2.2/ 6.3.2.3. CAS No. 9023-64-7/9023-62-5. Activity: Undetermined. Appearance: Clear to translucent yellow solution. Storage: at -20 °C or lower, for at least 1 month. Source: E. coli. Bifunctional Chimeras of Glutamylcysteine Synthetase and Glutathione Synthetase; Glutamylcysteine Synthetase; Glutathione Synthetase. Pack: 100ml. Cat No: NATE-1859. | |
| BTK inhibitor 2 | Bruton's tyrosine kinase (BTK), also known as tyrosine-protein kinase BTK, is an enzyme that in humans is encoded by the BTK gene. BTK is a kinase that plays a crucial role in B-cell development. Btk inhibitor 2 is a BTK inhibitor. Grades: ≥98%. CAS No. 1558036-85-3. Molecular formula: C24H25N5O3. Mole weight: 431.49. | |
| caspase-1 | From mammalian monocytes. This enzyme is part of the family of inflammatory caspases, which also includes caspase-4 (EC 3.4.22.57) and caspase-5 (EC 3.4.22.58) in humans and caspase-11 (EC 3.4.22.64), caspase-12, caspase-13 and caspase-14 in mice. Contains a caspase-recruitment domain (CARD) in its N-terminal prodomain, which plays a role in procaspase activation. Cleaves pro-interleukin-1β (pro-IL-1β) to form mature IL-1β, a potent mediator of inflammation. Also activates the proinflammatory cytokine, IL-18, which is also known as interferon-γ-inducing factor. Inhibited by Ac-Tyr-Val-Ala-Asp-CHO. Caspase-11 plays a critical role in the activation of caspase-1 in mi...proteinase; ICE. Enzyme Commission Number: EC 3.4.22.36. CAS No. 122191-40-6. 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-4211; caspase-1; EC 3.4.22.36; 122191-40-6; interleukin 1β-converting enzyme; protease VII; protease A; interleukin 1β precursor proteinase; interleukin 1 converting enzyme; interleukin 1β-converting endopeptidase; interleukin-1β convertase; interleukin-1β converting enzyme; interleukin-1β precursor proteinase; prointerleukin 1β protease; precursor interleukin-1β converting enzyme; pro-interleukin 1β proteinase; ICE. Cat No: EXWM-4211. | |
| caspase-11 | This murine enzyme is part of the family of inflammatory caspases, which also includes caspase-1 (EC 3.4.22.36), caspase-4 (EC 3.4.22.57) and caspase-5 (EC 3.4.22.58) in humans and caspase-12, caspase-13 and caspase-14 in mice. Contains a caspase-recruitment domain (CARD) in its N-terminal prodomain, which plays a role in procaspase activation. Like caspase-5, but unlike caspase-4, this enzyme can be induced by lipopolysaccharide. This enzyme not only activates caspase-1, which is required for the maturation of proinflammatory cytokines such as interleukin-1β (IL-1β) and IL-18, but it also activates caspase-3 (EC 3.4.22.56), which leads to cellular apoptosis under pathological conditions. Belongs in peptidase family C14. Group: Enzymes. Synonyms: CASP-11. Enzyme Commission Number: EC 3.4.22.64. 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-4240; caspase-11; EC 3.4.22.64; CASP-11. Cat No: EXWM-4240. | |
| caspase-4 | This enzyme is part of the family of inflammatory caspases, which also includes caspase-1 (EC 3.4.22.36) and caspase-5 (EC 3.4.22.58) in humans and caspase-11 (EC 3.4.22.64), caspase-12, caspase-13 and caspase-14 in mice. Contains a caspase-recruitment domain (CARD) in its N-terminal prodomain, which plays a role in procaspase activation. The enzyme is able to cleave itself and the p30 caspase-1 precursor, but, unlike caspase-1, it is very inefficient at generating mature interleukin-1β (IL-1β) from pro-IL-1&beta. Both this enzyme and caspase-5 can cleave pro-caspase-3 to release the small subunit (p12) but not the large subunit (p17). The caspase-1 inhibitor Ac-Tyr-Val-Ala-Asp-CHO can also inhibit this enzyme, but more slowly. Belongs in peptidase family C14. Group: Enzymes. Synonyms: ICErelII; ICErel-II; Ich-2; transcript X; TX; TX protease; caspase 4; CASP-4. Enzyme Commission Number: EC 3.4.22.57. CAS No. 182762-08-9. 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-4232; caspase-4; EC 3.4.22.57; 182762-08-9; ICErelII; ICErel-II; Ich-2; transcript X; TX; TX protease; caspase 4; CASP-4. Cat No: EXWM-4232. | |
| caspase-5 | This enzyme is part of the family of inflammatory caspases, which also includes caspase-1 (EC 3.4.22.36) and caspase-4 (EC 3.4.22.57) in humans and caspase-11 (EC 3.4.22.64), caspase-12, caspase-13 and caspase-14 in mice. Contains a caspase-recruitment domain (CARD) in its N-terminal prodomain, which plays a role in procaspase activation. The enzyme is able to cleave itself and the p30 caspase-1 precursor, but is very inefficient at generating mature interleukin-1β (IL-1β) from pro-IL-1&beta. Both this enzyme and caspase-4 can cleave pro-caspase-3 to release the small subunit (p12) but not the large subunit (p17). Unlike caspase-4, this enzyme can be induced by lipopolysaccharide. Belongs in peptidase family C14. Group: Enzymes. Synonyms: ICErel-III; Ich-3; ICH-3 protease; transcript Y; TY; CASP-5. Enzyme Commission Number: EC 3.4.22.58. CAS No. 192465-11-5. 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-4233; caspase-5; EC 3.4.22.58; 192465-11-5; ICErel-III; Ich-3; ICH-3 protease; transcript Y; TY; CASP-5. Cat No: EXWM-4233. | |
| Caspase-6 (Active) from Human, Recombinant | Caspase-6 is an enzyme that in humans is encoded by the CASP6 gene. This gene encodes a protein that is a member of the cysteine-aspartic acid protease (caspase) family. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes that undergo proteolytic processing at conserved aspartic residues to produce two subunits, large and small, that dimerize to form the active enzyme. This protein is processed by caspases 7, 8 and 10, and is thought to function as a downstream enzyme in the caspase activation cascade. Caspase 6 can also undergo self-processing without other members of the caspase family. Alternative splicing of this gene results in two transcript variants that encode different isoforms. Group: Enzymes. Synonyms: CASP6; MCH2; Caspase-6 (Active); Caspase-6. Caspase 6. Appearance: Liquid. Storage: -80°C. Form: Liquid. 5μg in 25μl of 50mM TRIS (pH 8.0) containing 100mM sodium chloride and 50mM imidazole. Source: E. coli. Species: Human. CASP6; MCH2; Caspase-6 (Active); Caspase-6. Cat No: NATE-0814. | |
| CATALASE | CATALASE. Synonyms: equilase;Catalase-Agarose;H2O2 oxidoreductase;Catalase from A. niger, lyophil.;Catalase from bovine liver, lyophil.;Catalase-peroxidase;CATALASE FROM BOVINE LIVERCA.65000 U/MG PROTEIN SUSPENSION;CATALASE FROM ASPERGILLUSNIGER CA.2000 U/MG LYOPH.SALT-FREE. CAS No. 9001-5-2. Pack Sizes: 1 kg. Product ID: CDF4-0037. Molecular formula: C9H10O3. Category: Enzyme Preparations. Product Keywords: Food Ingredients; Enzyme Preparations; CATALASE; CDF4-0037; 9001-05-2; C9H10O3; 232-577-1; 9001-05-2. Purity: 0.99. Color: Deep Brown. EC Number: 232-577-1. Physical State: Suspension. Storage: -20°C. Product Description: CAT (catalase) is an endogenous antioxidant enzyme, thus conferring protection to cells against damage by ROS (reactive oxygen species). In humans, this gene is localized to chromosome 11p13, which is composed of 12 introns and 13 exons. |  |
| CAY10485 | Acetyl-CoA acetyltransferase, mitochondrial, also known as acetoacetyl-CoA thiolase, is an enzyme that in humans is encoded by the ACAT (Acetyl-Coenzyme A acetyltransferase) gene. Both ACAT-1 and ACAT-2 are acetyl-CoA C-acetyltransferase enzyme. CAY10485 inhibits human ACAT-1 and ACAT-2 with an IC50 of 95 and 81 μM, respectively. It also inhibits copper-mediated oxidation of low density lipoproteins. Synonyms: 3,4-dihydroxy Hydrocinnamic acid (L-Aspartic acid dibenzyl ester) amide. Grades: ≥98%. CAS No. 615264-62-5. Molecular formula: C27H27NO7. Mole weight: 477.5. | |
| CAY10486 | Acetyl-CoA acetyltransferase, mitochondrial, also known as acetoacetyl-CoA thiolase, is an enzyme that in humans is encoded by the ACAT (Acetyl-Coenzyme A acetyltransferase) gene. Both ACAT-1 and ACAT-2 are acetyl-CoA C-acetyltransferase enzyme. CAY10486 inhibits human ACAT-1 and ACAT-2 equally with an IC50 value of 60 μM. It also inhibits copper-mediated oxidation of low density lipoproteins. Synonyms: 4-Hydroxycinnamic acid (L-phenylalanine methyl ester) amide. Grades: ≥98%. CAS No. 615264-52-3. Molecular formula: C19H19NO4. Mole weight: 325.4. | |
| CAY10606 | Arachidonate 5-lipoxygenase, also known as ALOX5, 5-lipoxygenase, 5-LOX, or 5-LO, is a non-heme iron-containing enzyme that in humans is encoded by the ALOX5 gene. 5-LO initiates the synthesis of leukotrienes (LTs) from arachidonic acid, primarily in certain leukocyte populations. CAY10606 is a potent, reversible inhibitor of 5-LO, both in cell-free assays (IC50 = 86 nM) and in intact neutrophils (IC50 = 230 nM). It prevents the production of LTs in whole blood, whether 5-LO is activated with the calcium ionophore A23187 with IC50 of 1.6 μM. Synonyms: CAY 10606; CAY-10606. Grades: ≥98%. CAS No. 1159576-98-3. Molecular formula: C22H18ClNO3. Mole weight: 379.8. | |
| CAY10640 | Soluble epoxide hydrolase (sEH) is a bifunctional enzyme that in humans is encoded by the EPHX2 gene. sEH is a member of the epoxide hydrolase family. CAY10640 is a 1-aryl-3-(1-acylpiperidin-4-yl)urea analog that inhibits recombinant human and mouse sEH with IC50 values both equal to 0.4 nM. Synonyms: sEHi; Soluble Epoxide Hydrolase Inhibitor; CAY 10640; CAY-10640. Grades: ≥98%. CAS No. 1208549-68-1. Molecular formula: C17H20F3N3O3. Mole weight: 371.4. | |
| CAY10649 | Arachidonate 5-lipoxygenase, also known as ALOX5, 5-lipoxygenase, 5-LOX, or 5-LO, is a non-heme iron-containing enzyme that in humans is encoded by the ALOX5 gene. 5-LO initiates the synthesis of (LTs) from arachidonic acid, primarily in certain leukocyte populations. CAY10649 is a thiazolinone compound that demonstrates direct inhibition of 5-lipoxygenase (5-LO) product formation in intact polymorphonuclear leukocytes (PMNL) with IC50 of 0.28 μM. Synonyms: CAY 10649; CAY-10649. Grades: ≥98%. CAS No. 1272519-89-7. Molecular formula: C17H12ClNO2S. Mole weight: 329.8. | |
| CAY10678 | Microsomal prostaglandin E synthase-1 (mPGES-1) or Prostaglandin E synthase is an enzyme that in humans is encoded by the PTGES gene. The protein encoded by this gene is a glutathione-dependent prostaglandin E synthase. The IC50s of mPGES-1 inhibitor are 900 nM for human and 90 nM for rat. CAY10678 is a selective microsomal prostaglandin E synthase 1 (mPGES-1) inhibitor. Synonyms: mPGES-1 Inhibitor III; CAY 10678; CAY-10678. Grades: ≥98%. CAS No. 1268709-57-4. Molecular formula: C23H34N4O. Mole weight: 382.5. | |
| CAY10700 | Microsomal prostaglandin E synthase-1 (mPGES-1) or Prostaglandin E synthase is an enzyme that in humans is encoded by the PTGES gene. The protein encoded by this gene is a glutathione-dependent prostaglandin E synthase. CAY10700 is a novel selective and orally bioavailable inhibitor of mPGES-1 with IC50 of 0.24 μM for human whole blood assay. Uses: Enzyme inhibitors. Synonyms: mPGES-1 Inhibitor-1; CAY 10700; CAY-10700. Grades: ≥98%. CAS No. 1381846-21-4. Molecular formula: C16H19ClN4O2. Mole weight: 334.8. | |
| Chlorpyrifos-d10 | Chlorpyrifos-d 10 is the deuterium labeled Chlorpyrifos. Chlorpyrifos is an organophosphate insecticide that is classified as a phosphorothionate. The oxon metabolite of Chlorpyrifos is an inhibitor of acetylcholinesterase (AChE), affecting neurological function in insects, humans, and other animals. The Chlorpyrifos oxon (CPO) metabolite is hydrolyzed by the plasma enzyme paraoxonase 1 (PON1), and susceptibility to neurotoxicity associated with CPO exposure is mitigated by PON1 overexpression. Uses: Scientific research. Group: Isotope-labeled compounds. CAS No. 285138-81-0. Pack Sizes: 1 mg; 5 mg; 10 mg. Product ID: HY-B0815S. |  |
| Coenzyme A, free acid | Coenzyme A (CoA, CoASH, or HSCoA) is a coenzyme, notable for its role in the synthesis and oxidation of fatty acids, and the oxidation of pyruvate in the citric acid cycle. All genomes sequenced to date encode enzymes that use coenzyme A as a substrate, and around 4% of cellular enzymes use it (or a thioester, such as acetyl-CoA) as a substrate. In humans, CoA biosynthesis requires cysteine, pantothenate, and adenosine triphosphate (ATP). Group: Coenzymes. Synonyms: Coenzyme A; CoA; Coenzyme A, free acid; 85-61-0; CoASH; HSCoA. CAS No. 85-61-0. Purity: > 75% when determined by enzymatic analysis with phosphotransacetylase at pH 7.5. CoA. Mole weight: 767.53 (as anhydrous free acid) 803.56 (CoA.2H2O). Storage: Keep tightly stoppered in the dark below 5°C. For Prolonged storage, keep below-20°C. Coenzyme A; CoA; Coenzyme A, free acid; 85-61-0; CoASH; HSCoA. Cat No: NATE-0145. | |
| Creatine Kinase BB Fraction Human, Recombinant | Brain-type creatine kinase also known as CK-BB is a creatine kinase that in humans is encoded by the CKB gene. The protein encoded by this gene, CK-BB, consists of a homodimer of two identical brain-type CK-B subunits. BB-CK is a cytoplasmic enzyme involved in cellular energy homeostasis, with certain fractions of the enzyme being bound to cell membranes, ATPases, and a variety of ATP-requiring enzymes in the cell. > 90% (sds-page), liquid, recombinant, expressed in pichia pastoris. Applications: Human creatine kinase bb fraction has been used to investigate the survival benefit of the late percutaneous coronary intervention in patients after acute myocardial infarction. human creatine kinase bb fraction has also been used in a study to analyze protein oxidations and resultant loss of function. Group: Enzymes. Synonyms: CKB; creatine kinase, brain; CKBB; creatine kinase B-type; creatine kinase-B; creatine kinase B chain; B-CK; Brain-type creatine kinase; Creatine Kinase BB; CK-BB; BB-CK. Purity: > 90% (SDS-PAGE). CK. Stability: -70°C. Form: liquid. Source: Pichia pastoris. Species: Human. CKB; creatine kinase, brain; CKBB; creatine kinase B-type; creatine kinase-B; creatine kinase B chain; B-CK; Brain-type creatine kinase; Creatine Kinase BB; CK-BB; BB-CK. Cat No: NATE-0139. | |
| Cystathionine β Synthase from Human, recombinant | Cystathionine-β-synthase, also known as CBS, is an enzyme (EC 4.2.1.22) that in humans is encoded by the CBS gene. CBS uses the cofactor pyridoxal-phosphate (PLP) and can be allosterically regulated by effectors such as the ubiquitous cofactor S-adenosyl-L-methionine (adoMet). This enzyme belongs to the family of lyases, to be specific, the hydro-lyases, which cleave carbon-oxygen bonds. CBS is a multidomain enzyme composed of an N-terminal enzymatic domain and two CBS domains. The CBS gene is the most common locus for mutations associated with homocystinuria. Group: Enzymes. Synonyms: Cystathionine-β-synthase; CBS; EC 4.2.1.22; 9023-99-8; Cystathionine β-synthase; Beta-thionase; methylcysteine synthase; serine sulfhydrase. Enzyme Commission Number: EC 4.2.1.22. Purity: > 90% by SDS-PAGE. CBS. Mole weight: 61.9 kDa (1-551 aa, NT His Tag). Activity: 100 U/mg. Stability: Stable for at least 1 year as supplied. Avoid repeated freeze and thaw cycles. Storage: Store at -20°C. Form: Liquid. Source: E. coli. Species: Human. Cystathionine-β-synthase; CBS; EC 4.2.1.22; 9023-99-8; Cystathionine β-synthase; Cystathionine β synthase; Beta-thionase; methylcysteine synthase; serine sulfhydrase. Cat No: NATE-1667. | |
| Cystathionine-β-synthase, Recombinant | Cystathionine-β-synthase, also known as CBS, is an enzyme (EC 4.2.1.22) that in humans is encoded by the CBS gene. CBS uses the cofactor pyridoxal-phosphate (PLP) and can be allosterically regulated by effectors such as the ubiquitous cofactor S-adenosyl-L-methionine (adoMet). This enzyme belongs to the family of lyases, to be specific, the hydro-lyases, which cleave carbon-oxygen bonds. CBS is a multidomain enzyme composed of an N-terminal enzymatic domain and two CBS domains. The CBS gene is the most common locus for mutations associated with homocystinuria. Applications: This protein can be used for producing hcy in vitro diagnosis kit. Group: Enzymes. Synonyms: Cystathionine-β-synthase; CBS; EC 4.2.1.22; 9023-99-8. Enzyme Commission Number: EC 4.2.1.22. CAS No. 9023-99-8. Purity: >90% (by SDS-PAGE). CBS. Mole weight: 56 KD. Appearance: Lyophilized powder. Storage: The lyophilized powder should be stored at -20°C where it is stable for up to several years. The solution could be stored at 4°C where it is stable for up to 1 year. Repeated freezing and thawing cycles of the reconstituted solution is not recommended. Cystathionine-β-synthase; CBS; EC 4.2.1.22; 9023-99-8. Cat No: DIA-293. | |
| Cystathionine gamma-lyase, Recombinant | Cystathionine gamma-lyase (CGL),or cystathionase (CSE, EC 4.4.1.1) , the enzyme participating in the synthesis of cysteine, catalyzes cystathionine deamination action, and form cysteine, alpha ketone butyric acid and NH3. In some bacteria and mammals, including humans, this enzyme takes part in generating hydrogen sulfide. Hydrogen sulfide is one of a few gases that was recently discovered to have arole in cell signaling in the body. As a new gaseous signal molecular, h2s has the similar but different mechanisms with carbon monoxide (co), nitric oxide (no) in diastolic function forblood vessels, which has several function such as the proliferation of vascular smooth muscle...e; CGL; cystathionase; CSE; EC 4.4.1.1; homoserine deaminase; homoserine dehydratase; cystine desulfhydrase; cysteine desulfhydrase; γ-cystathionase; cystathionase; homoserine deaminase-cystathionase; γ-CTL; cystalysin; cysteine lyase; L-cystathionine cysteine-lyase (deaminating); cystathionine γ-lyase. Enzyme Commission Number: EC 4.4.1.1. Purity: >90% (SDS-PAGE test). Mole weight: About 44kDa (SDS-PAGE detection). Activity: 11.25 KU/mg protein. Appearance: Yellowish liquid (or lyophilized powder). Storage: 4°C, store at -20°C for long-term preservation. Form: Freeze dried powder. Cystathionine gamma-lyase; CGL; cystathionase; CSE; EC 4.4.1.1; homoserine | |
| Daglutril | Daglutril is a dual endothelin converting enzyme (ECE)/neutral endopeptidase (NEP) inhibitor used for the treatment of hypertension and heart failure andpulmonary. It reduces proteinuria and urinary albumin excretion in diabetic rats, and inhibits systemic conversion of big endothelin-1 in humans. Synonyms: SLV-306; SLV306; SLV 306; 2- [ (3S) -3- [ [1- [ (2R) -2-ethoxycarbonyl-4-phenylbutyl] cyclopentanecarbonyl] amino] -2-oxo-4, 5-dihydro-3H-1-benzazepin-1-yl] acetic acid. Grades: 99%. CAS No. 182821-27-8. Molecular formula: C31H38N2O6. Mole weight: 534.64. | |
| Dihydrofolate Reductase from human, Recombinant | Dihydrofolate reductase, or DHFR, is an enzyme that reduces dihydrofolic acid to tetrahydrofolic acid, using NADPH as electron donor, which can be converted to the kinds of tetrahydrofolate cofactors used in 1-carbon transfer chemistry. In humans, the DHFR enzyme is encoded by the DHFR gene. It is found in the q11?q22 region of chromosome 5. Bacterial species possesses distinct DHFR enzymes (based on their pattern of binding diaminoheterocyclic molecules), but mammalian DHFRs are highly similar. Human dhfr is an 186 amino acid protein with an apparent molecular weight of 25 kda. it is 30% homologous to the e. coli protein and up to 70% homologous to vertebrate protein... from mycobacterium smegmatis. human dihydrofolate reductase has been used in a study to investigate the stable expression of green fluorescent protein and the targeted disruption of thioredoxin peroxidase-1 gene in babesia bovis. human dihydrofolate reductase has also been used in a study to investigate the structural analysis of human dihydrofolate reductase as a binary complex. Group: Enzymes. Synonyms: DHFR; dihydrofolate reductase; DYR; DHFRP1; Tetrahydrofolate NADP+ oxidoreductase; EC 1.5.1.3; tetrahydrofolate dehydrogenase; pteridine reductase:dihydrofolate reductase; dihydrofolate reductase:thymidylate synthase; thymidylate synthetase-dihydrofolate reductase; f | |
| dolichol kinase | This enzyme belongs to the family of transferases, to be specific, those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is CTP:dolichol O-phosphotransferase. This enzyme is also called dolichol phosphokinase. This enzyme participates in N-glycan biosynthesis. In humans dolichol kinase is encoded by the DOLK gene. Group: Enzymes. Synonyms: dolichol phosphokinase. Enzyme Commission Number: EC 2.7.1.108. CAS No. 71768-07-5. 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-2954; dolichol kinase; EC 2.7.1.108; 71768-07-5; dolichol phosphokinase. Cat No: EXWM-2954. | |
| 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 |  |
| fatty-acyl-CoA-transporting ATPase | ABC-type (ATP-binding cassette-type) ATPase, characterized by the presence of two similar ATP-binding domains. Does not undergo phosphorylation during the transport process. An animal and yeast enzyme that transports fatty acyl CoA into and out of peroxisomes. In humans, it is associated with Zellwegers syndrome. Group: Enzymes. Enzyme Commission Number: EC 7.6.2.4 (Formerly EC 3.6.3.47). 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-4685; fatty-acyl-CoA-transporting ATPase; EC 3.6.3.47. Cat No: EXWM-4685. | |
| ferroxidase | The enzyme in blood plasma (ceruloplasmin) belongs to the family of multicopper oxidases. In humans it accounts for 95% of plasma copper. It oxidizes Fe(II) to Fe(III), which allows the subsequent incorporation of the latter into proteins such as apotransferrin and lactoferrin. An enzyme from iron oxidizing bacterium strain TI-1 contains heme a. Group: Enzymes. Synonyms: ceruloplasmin; caeruloplasmin; ferroxidase I; iron oxidase; iron(II):oxygen oxidoreductase; ferro:O2 oxidoreductase; iron II:oxygen oxidoreductase; hephaestin; HEPH. Enzyme Commission Number: EC 1.16.3.1. CAS No. 9031-37-2, 104404-69-5. 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-1075; ferroxidase; EC 1.16.3.1; 9031-37-2, 104404-69-5; ceruloplasmin; caeruloplasmin; ferroxidase I; iron oxidase; iron(II):oxygen oxidoreductase; ferro:O2 oxidoreductase; iron II:oxygen oxidoreductase; hephaestin; HEPH. Cat No: EXWM-1075. | |
| fragilysin | Thought to be a cause of diarrhoea in animals and humans. Hydrolyses extracellular matrix proteins, and disrupts tight junctions of intestinal epithelial cells. Also degrades intracellular, cytoskeletal proteins actin, myosin and others. In peptidase family M10 (interstitial collagenase family). Group: Enzymes. Synonyms: Bacteroides fragilis (entero)toxin. Enzyme Commission Number: EC 3.4.24.74. CAS No. 188596-63-6. 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-4358; fragilysin; EC 3.4.24.74; 188596-63-6; Bacteroides fragilis (entero)toxin. Cat No: EXWM-4358. | |
| Gliotoxin | Gliotoxin is a sulfur-containing mycotoxin produced by species of fungi and pathogens of humans. Gliotoxin exhibits inhibitory activities against histone H3K9 methyltransferase, a key enzyme in the regulation of transcriptional activity by writing epigenetic marks. Gliotoxin also exhibits immunosuppressive properties by causing apoptosis of cells of the immune system. In addition, various studies suggests Gliotoxin may also be a potential anti-inflammatory, antibiotic, antifungal and antiviral agent. Group: Biochemicals. Alternative Names: (3R,5aS,6S,10aR)-2,3,5a,6-Tetrahydro-6-hydroxy-3-(hydroxymethyl)-2-methyl-10H-3,10a-epidithiopyrazino[1,2-a]indole-1,4-dione. Grades: Highly Purified. CAS No. 67-99-2. Pack Sizes: 1mg. US Biological Life Sciences. | Worldwide |
| Glucokinase from Escherichia coli, Recombinant | Glucokinase (EC 2.7.1.2) is an enzyme that facilitates phosphorylation of glucose to glucose-6-phosphate. Glucokinase occurs in cells in the liver, pancreas, gut, and brain of humans and most other vertebrates. In each of these organs it plays an important role in the regulation of carbohydrate metabolism by acting as a glucose sensor, triggering shifts in metabolism or cell function in response to rising or falling levels of glucose, such as occur after a meal or when fasting. Mutations of the gene for this enzyme can cause unusual forms of diabetes or hypoglycemia. Group: Enzymes. Synonyms: EC 2.7.1.2; glucokinase; glucokinase (phosphorylating); 9001-36-9; GCK; FGQTL3; GK; GLK; HHF3; HK4; HKIV; HXKP; LGLK; MODY2. Enzyme Commission Number: EC 2.7.1.2. CAS No. 9001-36-9. Purity: >95% as judged by SDS-PAGE. GCK. Mole weight: 35 kDa. Activity: 5.8 U/mg protein, 98.6 U/ml. Storage: Glucokinase should be stored at 4 °C, remaining stable up to 3 years under these storage conditions. Form: 3.2 M ammonium sulphate. Source: E. coli. Species: Escherichia coli. EC 2.7.1.2; glucokinase; glucokinase (phosphorylating); 9001-36-9; GCK; FGQTL3; GK; GLK; HHF3; HK4; HKIV; HXKP; LGLK; MODY2. Cat No: NATE-1571. | |
| glycoprotein-mannosyl O6-kinase | In humans this phosphorylated trisaccharide is attached to an L-threonine residue of α-dystroglycan, an extracellular peripheral glycoprotein that acts as a receptor for extracellular matrix proteins containing laminin-G domains, and is important for its activity. Group: Enzymes. Synonyms: SGK196; protein O-mannose kinase. Enzyme Commission Number: EC 2.7.1.183. 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-3015; glycoprotein-mannosyl O6-kinase; EC 2.7.1.183; SGK196; protein O-mannose kinase. Cat No: EXWM-3015. | |
| Granzyme K from Human, Recombinant | Granzyme K is a protein that in humans is encoded by the GZMK gene. This gene product is a member of a group of related serine proteases from the cytoplasmic granules of cytotoxic lymphocytes. Cytolytic T lymphocytes (CTL) and natural killer (NK) cells share the remarkable ability to recognize, bind, and lyse specific target cells. They are thought to protect their host by lysing cells bearing on their surface 'nonself' antigens, usually peptides or proteins resulting from infection by intracellular pathogens. The protein described here lacks consensus sequences for N-glycosylation present in other granzymes. Group: Enzymes. Synonyms: Granzyme K; GZMK; GZMK. Enzyme Commission Number: EC 3.4.21.-. Purity: >98% (SDS-PAGE). Alkalophilic proteinase. Activity: ~29 U/ug protein. Stability: Stable for at least 6 months when stored at -80°C. Dilute solutions (e. g. 1-1000ng/ml) should be used within 24 hours. Storage: at -80°C. Form: Liquid. In PBS containing 10% sucrose and ~0.5M sodium chloride. Contains no preservatives. Source: E. coli. Species: Human. Granzyme K; GZMK; GZMK. Cat No: NATE-1936. | |
| histamine N-methyltransferase | Histamine N-methyltransferase (HMT, HNMT) is an enzyme that in humans is encoded by the HNMT gene. Histamine N-methyltransferase is one of two enzymes involved in the metabolism of histamine, the other being diamine oxidase. Histamine N-methyltransferase catalyzes the methylation of histamine in the presence of S-adenosylmethionine (SAM) forming N-methylhistamine. Group: Enzymes. Synonyms: histamine 1-methyltransferase; histamine methyltransferase; histamine-methylating enzyme; imidazolemethyltransferase; S-adenosylmethionine-histamine N-methyltransferase. Enzyme Commission Number: EC 2.1.1.8. CAS No. 9029-80-5. HNMT. 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-1981; histamine N-methyltransferase; EC 2.1.1.8; 9029-80-5; histamine 1-methyltransferase; histamine methyltransferase; histamine-methylating enzyme; imidazolemethyltransferase; S-adenosylmethionine-histamine N-methyltransferase. Cat No: EXWM-1981. | |
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