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| Product | Description | |
|---|---|---|
| Native Bovine Angiotensin Converting Enzyme | Angiotensin-converting enzyme (EC 3.4.15.1), or "ACE" indirectly increases blood pressure by causing blood vessels to constrict. It does that by converting angiotensin I to angiotensin II, which constricts the vessels. For this reason, drugs known as ACE inhibitors are used to lower blood pressure. ACE, angiotensin I and angiotensin II are part of the renin-angiotensin system (RAS), which controls blood pressure by regulating the volume of fluids in the body. ACE is secreted in the lungs and kidneys by cells in the endothelium (inner layer) of blood vessels. Applications: Positive control. Group: Enzymes. Synonyms: ACE; Angiotensin Converting Enzyme; EC 3.4.15.1; dipept...te buffer-300 mM NaCl, pH 8.3 at 37°C. Storage: Maintain at -20°C in undiluted aliquots for up to 12 months. Maintain at 4°C for up to one month. A decrease in activity may occur within prolonged storage at 4°C. Source: Bovine lung. Species: Bovine. ACE; Angiotensin Converting Enzyme; EC 3.4.15.1; dipeptidyl carboxypeptidase I; peptidase P; dipeptide hydrolase, peptidyl dipeptidase; angiotensin converting enzyme; kininase II; angiotensin I-converting enzyme; carboxycathepsin; dipeptidyl carboxypeptidase; "hypertensin converting enzyme" peptidyl dipeptidase I; peptidyl-dipeptide hydrolase; peptidyldipeptide hydrolase; endothelial cell peptidyl dipeptidase; peptidyl dipept |  |
| 3- (2-Pyridyldithio) propanoic Acid | Crosslinking agent in immobilization of thrombogenesis-inhibiting enzymes on polymeric carriers. Targeted delivery of a triplex-forming oligonucleotide to hepatic stellate cells by complexes with phosphated bovine serum albumin for treatment of liver fibrosis. Group: Biochemicals. Alternative Names: 2-Carboxyethyl 2-Pyridyl Disulfide. Grades: Highly Purified. CAS No. 68617-64-1. Pack Sizes: 100mg, 250mg, 500mg, 1g. US Biological Life Sciences. |  Worldwide |
| 4-hydroxy-2-oxoglutarate aldolase | The enzymes from rat liver and bovine liver act on both enantiomers of 4-hydroxy-2-oxoglutarate. cf. EC 4.1.3.42, L-4-hydroxy-2-oxoglutarate aldolase. Group: Enzymes. Synonyms: 2-oxo-4-hydroxyglutarate aldolase; hydroxyketoglutaric aldolase; 4-hydroxy-2-ketoglutaric aldolase; 2-keto-4-hydroxyglutaric aldolase; 4-hydroxy-2-ketoglutarate aldolase; 2-keto-4-hydroxyglutarate aldolase; 2-oxo-4-hydroxyglutaric aldolase; DL-4-hydroxy-2-ketoglutarate aldolase; hydroxyketoglutarate aldolase; 2-keto-4-hydroxybutyrate aldolase; 4-hydroxy-2-oxoglutarate glyoxylate-lyase; KHGA. Enzyme Commission Number: EC 4.1.3.16. CAS No. 9030-81-3. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4901; 4-hydroxy-2-oxoglutarate aldolase; EC 4.1.3.16; 9030-81-3; 2-oxo-4-hydroxyglutarate aldolase; hydroxyketoglutaric aldolase; 4-hydroxy-2-ketoglutaric aldolase; 2-keto-4-hydroxyglutaric aldolase; 4-hydroxy-2-ketoglutarate aldolase; 2-keto-4-hydroxyglutarate aldolase; 2-oxo-4-hydroxyglutaric aldolase; DL-4-hydroxy-2-ketoglutarate aldolase; hydroxyketoglutarate aldolase; 2-keto-4-hydroxybutyrate aldolase; 4-hydroxy-2-oxoglutarate glyoxylate-lyase; KHGA. Cat No: EXWM-4901. | |
| 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. | |
| Alkaline phosphatase, Bovine intestine | Alkaline phosphatase, Bovine intestine (Apase) is a membrane-bound glycoprotein that catalyzes the hydrolysis of phosphate monoesters at alkaline pH. Alkaline phosphatase can be used in molecular biology and enzyme-free analysis. Inhibition of tissue nonspecific alkaline phosphatase can block intracellular lipid accumulation [1] [2]. Uses: Scientific research. Group: Natural products. Alternative Names: Apase. CAS No. 9001-78-9. Pack Sizes: 5 mg; 10 mg; 25 mg; 50 mg; 100 mg. Product ID: HY-P2818. |  |
| Alkaline Phosphatase from Bovine, Recombinant | Alkaline phosphatase (ALP, ALKP, ALPase, Alk Phos) (EC 3.1.3.1) is a hydrolase enzyme responsible for removing phosphate groups from many types of molecules, including nucleotides, proteins, and alkaloids. The process of removing the phosphate group is called dephosphorylation. As the name suggests, alkaline phosphatases are most effective in an alkaline environment. It is sometimes used synonymously as basic phosphatase. Applications: Alkaline phosphatase is used for conjugation to antibodies and other proteins for elisa, western blotting, and hist ochemical detection. it is routinely used to dephosphorylate proteins and nucleic acids. it may be used for protein label...ic acid phosphatase using a fluorogenic assay. it is commonly used as a "reporter" in detection systems, in which it is conjugated to a protein (antibody, streptavidin, etc.) that specifically recognizes a target molecule. alkaline phosphatase has also been used to dephosphorylate casein. Group: Enzymes. Synonyms: Alkaline phosphatase; ALP; ALKP; ALPase; Alk Phos; EC 3.1.3.1; Alkaline phosphomonoesterase; Glycerophosphatase; Phosphomonoesterase. Enzyme Commission Number: EC 3.1.3.1. CAS No. 9001-78-9. ALP. Mole weight: apparent mol wt 160 kDa. Activity: > 4000 units/mg protein. Storage: 2-8°C. Source: Pichia pastoris. Species: Bovine. Alkaline phosphatase; ALP; ALKP; AL | |
| α-1,3-Galactosyltransferase from Bovine, Recombinant | In enzymology, a N-acetyllactosaminide 3-alpha-galactosyltransferase (EC 2.4.1.87) is an enzyme that catalyzes the chemical reaction: UDP-galactose + beta-D-galactosyl-(1->4)-beta-N-acetyl-D-glucosaminyl-R ? UDP + alpha-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-beta-N- acetylglucosaminyl-R. Thus, the two substrates of this enzyme are UDP-galactose and [[beta-D-galactosyl-(1->4)-beta-N-acetyl-D-glucosaminyl-R]], whereas its 3 products are UDP, [[alpha-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-beta-N-]], and acetylglucosaminyl-R. Group: Enzymes. Synonyms: alpha-galactosyltransferase; UDP-galactose-acetyllactosamine alpha-D-galactosyltransferase; glycopeptide alpha-1,3-D-galactosyltransfera. Enzyme Commission Number: EC 2.4.1.87. CAS No. 128449-51-4. Purity: min 95% by SDS-PAGE. Galactosyltransferase. Mole weight: 36 kDa. Source: E. coli. Species: Bovine. alpha-galactosyltransferase; UDP-galactose-acetyllactosamine alpha-D-galactosyltransferase; glycopeptide alpha-1,3-D-galactosyltransferase; glucosaminylglycopeptide alpha-1,3-galactosyltransferase; uridine diphosphogalactose-acetyllactosamine; alpha1->3-galactosyltransferase; uridine diphosphogalactose-acetyllactosamine galactosyltransferase; galactosyltransferase; beta-D-galactosyl-N-acetylglucosaminylglycopeptide; alpha-1,3-galactosyltransferase. Cat No: NATE-1480. | |
| Aprotinin, Bovine (Pancreatic trypsin inhibitor) | Aprotinin is a competitive serine protease inhibitor that inhibits trypsin, chymotrypsin, kallikrein and plasmin. Aprotinin forms stable complexes with and blocks the active sites of enzymes. Binding is reversible with most aprotinin-protease complexes, dissociating at pH >10 or <3. Effective concentration is equimolar with protease. Group: Biochemicals. Alternative Names: Antikrein; Antilysin; Antilysine; Aprostat; Aprotinin; BPTI; BPTI Trypsin Inhibitor; Basic Pancreatic Trypsin Inhibitor; Bayer A 128; Bovine Basic Pancreatic Trypsin Inhibitor; Bovine Pancreatic Trypsin Inhibitor; Bovine Trypsin Inhibitor; Fosten; Kallikrein-trypsin Inactivator; Kiker 52G; Kir Richter; Kunitz Pancreatic Trypsin Inhibitor; Kunitz Protease Inhibitor; Kunitz Trypsin Inhibitor; Kunitz-type Inhibitor; Kunitz-type Proteinase Inhibitor; Kunitz-type Trypsin Inhibitor; Onquinin; Pancreatic Basic Trypsin Inhibitor; Pancreatic Trypsin Inhibitor; Pancreatic Trypsin Inhibitor (Kunitz); Protease Inhibitor, Kunitz Type; RP 9921; Repulson; Trasuylol; Trasylol; Trazinin; Triazinin; Trypsin Inhibitor, Trasylol; Trypsin-kallikrein Inhibitor (Kunitz); Zymofren. Grades: Highly Purified. CAS No. 9087-70-1. Pack Sizes: 100mg, 250mg, 500mg, 1g. Molecular Formula: C???H???N??O??S?, Molecular Weight: 6511.45. US Biological Life Sciences. | Worldwide |
| β(1-3,4)-Galactosidase from Bovine, Recombinant | β-galactosidase is a hydrolase enzyme that catalyzes the hydrolysis of β-galactosides into monosaccharides. Substrates of different β-galactosidases include ganglioside GM1, lactosylceramides, lactose, and various glycoproteins. Group: Enzymes. Synonyms: β-galactosidase; beta-gal; β-gal; EC 3.2.1.23; lactase; β-lactosidase; maxilact; hydrolact; β-D-lactosidase; S 2107; lactozym; trilactase; β-D-galactanase; oryzatym; sumiklat; β-D-galactoside galactohydrolase. Enzyme Commission Number: EC 3.2.1.23. CAS No. 9031-11-2. β-gal. Mole weight: 71 kDa. Storage: 4°C. Form: Liquid. Source: Pichia pastoris. Species: Bovine testis. β-galactosidase; beta-gal; β-gal; EC 3.2.1.23; lactase; β-lactosidase; maxilact; hydrolact; β-D-lactosidase; S 2107; lactozym; trilactase; β-D-galactanase; oryzatym; sumiklat; β-D-galactoside galactohydrolase; β1-3,4 Galactosidase; β(1-3,4)-Galactosidase. Cat No: NATE-1627. | |
| Bovine Catalase-polyethylene glycol | PEG labeled catalase is one of PEGylated catalase conjugates. Catalase is a common enzyme found in nearly all living organisms exposed to oxygen. It catalyzes the decomposition of hydrogen peroxide to water and oxygen. Catalase is an important enzyme in protecting the cell from oxidative damage by reactive oxygen species. PEG modified catalase shows better stability with good reactivity. We provide a variety of chemically functionalized and bio-conjugated catalase with different functionality. These functionalized catalase conjugates were purified by size exclusion chromatography to ensure adequate applications both in-vitro and in-vivo. Group: Enzymes. Synonyms: PEG-Catalase; Catalase-polyethylene glycol; CAT-PEG. CAS No. 9001-5-2. CAT. Mole weight: ~250 KDa. Activity: 2000-5000 units/mg before conjugation; 20~50 PEG5000 on each catalase molecule. Storage: Store at -20°C. Form: Lyophilized powder. Source: Bovine liver. Species: Bovine. PEG-Catalase; Catalase-polyethylene glycol; CAT-PEG. Pack: Package size based on protein content. Cat No: NATE-0111. | |
| Bovine Superoxide dismutase-polyethylene glycol | Superoxide dismutases (SOD) are enzymes that alternately catalyze the dismutation (or partitioning) of the superoxide (O2-) radical into either ordinary molecular oxygen (O2) or hydrogen peroxide (H2O2). Superoxide is produced as a by-product of oxygen metabolism and, if not regulated, causes many types of cell damage. Hydrogen peroxide is also damaging, but less so, and is degraded by other enzymes such as catalase. Thus, SOD is an important antioxidant defense in nearly all living cells exposed to oxygen. One exception is Lactobacillus plantarum and related lactobacilli, which use a different mechanism to prevent damage from reactive (O2-). Group: Enzymes. Synonyms: PEG-SOD; Superoxide dismutase-polyethylene glycol; SOD-PEG. SOD. Activity: 11,000 units/mg SOD before conjugation; SOD/PEG ratio: 10-20 PEG with each SOD enzyme. Appearance: Off-white. Storage: Store at -20°C. Form: Lyophilized powder. Source: Bovine Kidney. Species: Bovine. PEG-SOD; Superoxide dismutase-polyethylene glycol; SOD-PEG. Cat No: NATE-0682. | |
| Carbonic Anhydrase II from Bovine, Recombinant | The carbonic anhydrases (or carbonate dehydratases) form a family of enzymes that catalyze the rapid interconversion of carbon dioxide and water to bicarbonate and protons (or vice versa), a reversible reaction that occurs relatively slowly in the absence of a catalyst. The active site of most carbonic anhydrases contains a zinc ion; they are therefore classified as metalloenzymes. Carbonic anhydrase is a zinc-containing enzyme that catalyzes the reversible conversion of carbon dioxide to bicarbonate. one of its main physiological roles is to maintain the acid-base balance in blood and other tissues. lack of carbonic anhydrase results in carbonic anhydrase type ii defi...ns: Carbonic anhydrase is used to create carbon dioxide capture systems and to research various purification techniques. carbonic anhydrase is also used to study acid-base regulation in fish and carbonic anhydrase type ii deficiency syndrome. bovine carbonic anhydrase ii (ca II), has been widely used as a model protein in the investigation of the protein folding process. Group: Enzymes. Synonyms: carbonic anhydrases; carbonate dehydratases; EC 4.2.1.1; anhydrase; carbonate anhydrase; carbonic acid anhydrase; carboxyanhydrase; carbonic anhydrase A; carbonate hydro-lyase. Enzyme Commission Number: EC 4.2.1.1. CAS No. 9001-03-0. Purity: >90% by SDS-PAGE. Carbonic Anhydras | |
| CATALASE | CATALASE. Synonyms: equilase;Catalase-Agarose;H2O2 oxidoreductase;Catalase from A. niger, lyophil.;Catalase from bovine liver, lyophil.;Catalase-peroxidase;CATALASE FROM BOVINE LIVERCA.65000 U/MG PROTEIN SUSPENSION;CATALASE FROM ASPERGILLUSNIGER CA.2000 U/MG LYOPH.SALT-FREE. CAS No. 9001-5-2. Pack Sizes: 1 kg. Product ID: CDF4-0037. Molecular formula: C9H10O3. Category: Enzyme Preparations. Product Keywords: Food Ingredients; Enzyme Preparations; CATALASE; CDF4-0037; 9001-05-2; C9H10O3; 232-577-1; 9001-05-2. Purity: 0.99. Color: Deep Brown. EC Number: 232-577-1. Physical State: Suspension. Storage: -20°C. Product Description: CAT (catalase) is an endogenous antioxidant enzyme, thus conferring protection to cells against damage by ROS (reactive oxygen species). In humans, this gene is localized to chromosome 11p13, which is composed of 12 introns and 13 exons. |  |
| Catalase from bovine liver | Catalase from bovine liver. Synonyms: H2O2:H2O2 oxidoreductase. CAS No. 9001-5-2. Product ID: CDC10-0039. Category: Antioxidant Cosmetic Chemicals. Product Keywords: Cosmetic Ingredients; Antioxidant Cosmetic Chemicals; Catalase from bovine liver; CDC10-0039; 9001-05-2; H2O2:H2O2 oxidoreductase; MFCD00081483; 9001-05-2. Physical State: aqueous suspension. Quality Level: 200. Storage: 2-8°C. Application: Catalase from bovine liver has been used for measuring the hydrogen peroxide conetent in cancer tissue homogenates. It has also been used to test the effect of organophosphate insecticide chlorpyrifos-ethyl (CE) [0,0-diethyl 0 (3,5,6-trichloro-2-pyridyl) phosphorothioate] on its enzyme activity. Density: 1.06 g/mL at 20 °C. Product Description: Catalase from bovine liver contains 506 residues. It is a tetramer and each monomer corresponds to a molecular weight of 61 kDa. The active site in each momomer comprises nicotinamide adenine dinucleotide phosphate (NADPH) and iron binding region. | |
| Chymotrypsin | Chymotrypsin is a proteolytic enzyme. It can priority hydrolyze tyrosine containing l-isomer, phenylalanine and the peptide bond of tryptophan, the best effective condition is pH 8.0. Its activity can be restrained by heavy metal or natural trypsin inhibitor in some degrees. Applications: Practically used to heal cicatrisation caused by injuries, inflammation and it is also used for avoiding part dropsy, blood-gathering, haematoma caused by wrick, breast dropsy after operation, tympanitis and rhinitis brief introduction of production: the high purity chymotrypsin is extracted from bovine or porcine pancreas and purified by affinity chromatography in order to avoid being polluted by other protease. Group: Enzymes. Synonyms: Chymotrypsin; Alpha-chymotrypsin; Chymotrypsin A; Chymotrypsin B. CAS No. 9004-7-3. Chymotrypsin. Appearance: inquire. Chymotrypsin; Alpha-chymotrypsin; Chymotrypsin A; Chymotrypsin B. Pack: inquire. Cat No: BIO-1012. | |
| dihydroorotate dehydrogenase (quinone) | This Class 2 dihydroorotate dehydrogenase enzyme contains FMN. The enzyme is found in eukaryotes in the mitochondrial membrane, in cyanobacteria, and in some Gram-negative and Gram-positive bacteria associated with the cytoplasmic membrane. The reaction is the only redox reaction in the de-novo biosynthesis of pyrimidine nucleotides. The best quinone electron acceptors for the enzyme from bovine liver are ubiquinone-6 and ubiquinone-7, although simple quinones, such as benzoquinone, can also act as acceptor at lower rates. Methyl-, ethyl-, tert-butyl and benzyl (S)-dihydroorotates are also substrates, but methyl esters of (S)-1-methyl and (S)-3-methyl and (S)-1,3-dimethyldihydroorotates are not. Class 1 dihydroorotate dehydrogenases use either fumarate (EC 1.3.98.1), NAD+ (EC 1.3.1.14) or NADP+ (EC 1.3.1.15) as electron acceptor. Group: Enzymes. Synonyms: dihydroorot. Enzyme Commission Number: EC 1.3.5.2. CAS No. 59088-23-2. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-1386; dihydroorotate dehydrogenase (quinone); EC 1.3.5.2; 59088-23-2; dihydroorotate:ubiquinone oxidoreductase; (S)-dihydroorotate:(acceptor) oxidoreductase; (S)-dihydroorotate:acceptor oxidoreductase; DHOdehase (ambiguous); DHOD (ambiguous); DHODase (ambiguous); DHODH. Cat No: EXWM-1386. | |
| Endo-β-galactosidase from Bacteroides fragilis, Recombinant | Endo-β-Galactosidase is an enzyme that hydrolyzes internal β-galactosidic linkages of oligosaccharides in poly-N-acetyl-lactosamine structures. This enzyme resembles the Escherichia freundii enzyme due to its specificity towards bovine corneal keratan sulphate, milk oligosaccharides and the glycolipids lacto-N-neotetraosylceramide and lacto-N-tetraosylceramide. Group: Enzymes. Synonyms: β-Galactosidase bacterial; Keratanase; Endo-β-galactosidase; keratan sulfate endogalactosidase; keratan-sulfate 1,4-β-D-galactanohydrolase; EC 3.2.1.103. Enzyme Commission Number: EC 3.2.1.103. CAS No. 55072-01-0. Endo-β-galactosidase. Mole weight: ~32 kDa. Activity: >14 U/ml; Specific Activity: >140 U/mg protein. Storage: 2-8°C. Form: Sterile-filtered in 20 mM Tris-HCl, pH 7.5. Source: E. coli. Species: Bacteroides fragilis. β-Galactosidase bacterial; Keratanase; Endo-β-galactosidase; keratan sulfate endogalactosidase; keratan-sulfate 1,4-β-D-galactanohydrolase; EC 3.2.1.103. Cat No: NATE-1413. | |
| Enterokinase from bovine intestine, Recombinant | Enteropeptidase (also called enterokinase) is an enzyme produced by cells of the duodenum and involved in human and animal digestion. It is secreted from intestinal glands (the crypts of Lieberkühn) following the entry of ingested food passing from the stomach. Enteropeptidase converts trypsinogen (a zymogen) into its active form trypsin, resulting in the subsequent activation of pancreatic digestive enzymes. Absence of enteropeptidase results in intestinal digestion impairment. Applications: Enterokinase is a member of the s1 peptidase family. in vivo, it is responsble for the proteolytic activation of trypsin from trypsinogen. enterokinase is used for site specific ...yme from creative enzymes has been used to compare the specific activity with that of purified, recombinant bovine enterokinase (light chain) overexpressed in escherichia coli. Group: Enzymes. Synonyms: enterokinase; enteropeptidase; EC 3.4.21.9; 9014-74-8. Enzyme Commission Number: EC 3.4.21.9. CAS No. 9014-74-8. Enterokinase. Mole weight: 28 kDa light chain form. Activity: Type I, > 20 units/mg protein. Storage: -20°C. Form: Type I, supplied as a solution in 20 mM Tris-HCl, 200 mM NaCl, and 50% glycerol; Type II, white powder. Source: E. coli. Species: Bovine intestine. enterokinase; enteropeptidase; EC 3.4.21.9; 9014-74-8. Pack: vial of ~0.2 unit. Cat No: NATE-0226. | |
| glycine N-phenylacetyltransferase | Not identical with EC 2.3.1.13 (glycine N-acyltransferase).This enzyme was purified from bovine liver mitochondria. L-asparagine, L-glutamine and L-arginine are alternative substrates to glycine, but have higher Km values. Group: Enzymes. Synonyms: arylacetyl-CoA N-acyltransferase; arylacetyltransferase; GAT (gene name). Enzyme Commission Number: EC 2.3.1.192. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-2135; glycine N-phenylacetyltransferase; EC 2.3.1.192; arylacetyl-CoA N-acyltransferase; arylacetyltransferase; GAT (gene name). Cat No: EXWM-2135. | |
| Immobilized bovine chymotrypsin | Immobilized bovine chymotrypsin is ideal for digestions of proteins and peptides. Chymotrypsin is a protease that cleaves peptide bonds at Trp, Tyr, Phe, Leu and Met. Chymotrypsin protease is generally specific for hydrophobic residues and is often used to provide complementary sequence coverage when compared to tryptic digested samples. Group: Enzymes. Synonyms: EC 3. 4. 21. 1; α-Chymotrypsin; chymotrypsins A and B; alpha-chymar ophth; avazyme; chymar; chymotest; enzeon; quimar; quimotrase; alpha-chymar; alpha-chymotrypsin A; alpha-chymotrypsin; Chymotrypsin. Enzyme Commission Number: EC 3. 4. 21. 1. Purity: >95% by SDS-PAGE analysis. Mole weight: 25000. Stability: 12 months from delivery. Storage: 4°C. Form: Resin. Source: Bovine pancreas. Species: Bovine. EC 3. 4. 21. 1; α-Chymotrypsin; chymotrypsins A and B; alpha-chymar ophth; avazyme; chymar; chymotest; enzeon; quimar; quimotrase; alpha-chymar; alpha-chymotrypsin A; alpha-chymotrypsin; Chymotrypsin; Immobilized chymotrypsin. Cat No: NATE-1754. | |
| Immobilized bovine trypsin | Immobilized bovine trypsin is ideal for digestions of proteins and peptides. Trypsin is a protease that cleaves peptide bonds at Arg and Lys. Trypsin protease is TPCK treated to remove chymotryptic activity before immobilization. Trypsin can be used to provide complementary sequence coverage when compared to chymotryptic digested samples. Group: Enzymes. Synonyms: α-trypsin; β-trypsin; cocoonase; parenzyme; parenzymol; tryptar; trypure; pseudotrypsin; tryptase; tripcellim; sperm receptor hydrolase; Alpha-trypsin; Beta-trypsin; EC 3. 4. 21. 4; Trypsin. Enzyme Commission Number: EC 3. 4. 21. 4. Purity: >95% by SDS-PAGE analysis. Mole weight: 23300. Stability: 12 months from delivery. Storage: 4°C. Form: Resin. Source: Bovine pancreas. Species: Bovine. α-trypsin; β-trypsin; cocoonase; parenzyme; parenzymol; tryptar; trypure; pseudotrypsin; tryptase; tripcellim; sperm receptor hydrolase; Alpha-trypsin; Beta-trypsin; EC 3. 4. 21. 4; Trypsin; Immobilized trypsin. Cat No: NATE-1755. | |
| Immobilized RNase A on G3m | RNase A is an endonuclease that cleaves RNA but not DNA. RNase A specifically cuts pyrimidine ribonucleotides at the 3'-adjacent phosphodiester bond Py/pN, with the intermediary formation of nucleoside-2',3'-cyclophosphate. G3m: 25 ug (2. 5 Kunitz units) RNase A per CR-column immobilized on dextranThis G3m-column digests at least 200 ug RNA per application. Nr. 5 Storage buffer: 50 mM Tris/HCl, pH 7. 5Nr. 5 Reaction buffer: 50 mM Tris/HCl, pH 7. 5 (also active with 1% SDS)Nr. 6 Washing buffer: 50 mM Tris/HCl, 1 M NaCl, pH 7. 5The columns are provided in storage buffer. Group: Enzymes. Synonyms: Pancreatic ribonucleases; EC 3. 1. 27. 5; RNase; RNase I; RNase A; pancreatic RNase; ...lease; SLSG glycoproteins; gene S locus-specific glycoproteins; S-genotype-asssocd. glycoproteins; ribonucleate 3'-pyrimidino-oligonucleotidohydrolase; 9001-99-4. Enzyme Commission Number: EC 3. 1. 27. 5. Storage: 4 °C. Source: Bovine pancreas. Pancreatic ribonucleases; EC 3. 1. 27. 5; RNase; RNase I; RNase A; pancreatic RNase; ribonuclease I; endoribonuclease I; ribonucleic phosphatase; alkaline ribonuclease; ribonuclease; gene S glycoproteins; Ceratitis capitata alkaline ribonuclease; SLSG glycoproteins; gene S locus-specific glycoproteins; S-genotype-asssocd. glycoproteins; ribonucleate 3'-pyrimidino-oligonucleotidohydrolase; 9001-99-4; Immobilized RNase A. Cat No: NATE-1773. | |
| Immobilized TLCK-Chymotrypsin on F7m | α-chymotrypsin hydrolyzes peptides, amides, and esters preferentially at the carboxyl groups of hydrophobic amino acids (L-tyrosine, L-phenylalanine, and L-tryptophan but also bonds of leucyl, methionyl, asparaginyl, and glutamyl residues). F7m: 1. 0 mg α-chymotrypsin per CR-column immobilized on polyvinyl. 55 units immobilized per CR-columnNr. 5 Storage buffer: 50 mM Tris/HCl, pH 7. 5Nr. 5 Reaction buffer: 50 mM Tris/HCl, pH 7. 5; also active in 0.1% SDSNr. 6 Washing buffer: 50 mM Tris/HCl, 1 M NaCl, pH 7. 5. Group: Enzymes. Synonyms: EC 3. 4. 21. 1; α-Chymotrypsin; chymotrypsins A and B; alpha-chymar ophth; avazyme; chymar; chymotest; enzeon; quimar; quimotrase; alpha-chymar; alpha-chymotrypsin A; alpha-chymotrypsin; Chymotrypsin. Enzyme Commission Number: EC 3. 4. 21. 1. Storage: 4 °C. Source: Bovine pancreas. EC 3. 4. 21. 1; α-Chymotrypsin; chymotrypsins A and B; alpha-chymar ophth; avazyme; chymar; chymotest; enzeon; quimar; quimotrase; alpha-chymar; alpha-chymotrypsin A; alpha-chymotrypsin; Chymotrypsin; Immobilized TLCK-Chymotrypsin; Immobilized Chymotrypsin; TLCK-Chymotrypsin. Cat No: NATE-1769. | |
| Immobilized TLCK-Chymotrypsin on G3m | α-chymotrypsin hydrolyzes peptides, amides, and esters preferentially at the carboxyl groups of hydrophobic amino acids (L-tyrosine, L-phenylalanine, and L-tryptophan but also bonds of leucyl, methionyl, asparaginyl, and glutamyl residues). G3m: 25 ug α-chymotrypsin per CR-column immobilized on dextran. 1. 4 units immobilized per CR-column. This CR-column cuts at least 100 ug tubulin per application; it cuts 5 ug/minuteBSA without SDS, but at least 45 ug/minute BSA in the presence of 0.1% SDS. Nr. 5 Storage buffer: 50 mM Tris/HCl, pH 7. 5Nr. 5 Reaction buffer: 50 mM Tris/HCl, pH 7. 5; also active in 0.1% SDSNr. 6 Washing buffer: 50 mM Tris/HCl, 1 M NaCl, pH 7. 5. Group: Enzymes. Synonyms: EC 3. 4. 21. 1; α-Chymotrypsin; chymotrypsins A and B; alpha-chymar ophth; avazyme; chymar; chymotest; enzeon; quimar; quimotrase; alpha-chymar; alpha-chymotrypsin A; alpha-chymotrypsin; Chymotrypsin. Enzyme Commission Number: EC 3. 4. 21. 1. Storage: 4 °C. Source: Bovine pancreas. EC 3. 4. 21. 1; α-Chymotrypsin; chymotrypsins A and B; alpha-chymar ophth; avazyme; chymar; chymotest; enzeon; quimar; quimotrase; alpha-chymar; alpha-chymotrypsin A; alpha-chymotrypsin; Chymotrypsin; Immobilized TLCK-Chymotrypsin; Immobilized Chymotrypsin; TLCK-Chymotrypsin. Cat No: NATE-1770. | |
| Immobilized TPCK-Trypsin on F7m | Trypsin hydrolyzes proteins, peptides, amides and esters specifically at the carboxyl groups of the basic amino acids L-arginine or L-lysine. F7m: 1. 0 mg trypsin per CR-column, immobilized on polyvinyl10,200 ST-units immobilized per CR-column. Nr. 15 Storage buffer: 50 mM Tris/HCl at pH 8. 0 at 4°CNr. 67 Reaction buffer: 50 mM phosphate at pH 8. 0Nr. 68 Washing buffer: 50 mM phosphate at pH 8. 0, 1 M NaCl. Group: Enzymes. Synonyms: α-trypsin; β-trypsin; cocoonase; parenzyme; parenzymol; tryptar; trypure; pseudotrypsin; tryptase; tripcellim; sperm receptor hydrolase; Alpha-trypsin; Beta-trypsin; EC 3. 4. 21. 4; Trypsin. Enzyme Commission Number: EC 3. 4. 21. 4. Storage: 4 °C. Source: Bovine pancreas. α-trypsin; β-trypsin; cocoonase; parenzyme; parenzymol; tryptar; trypure; pseudotrypsin; tryptase; tripcellim; sperm receptor hydrolase; Alpha-trypsin; Beta-trypsin; EC 3. 4. 21. 4; Trypsin; Immobilized TPCK-Trypsin; Immobilized Trypsin; TPCK-Trypsin. Cat No: NATE-1771. | |
| Immobilized TPCK-Trypsin on G3m | Trypsin hydrolyzes proteins, peptides, amides and esters specifically at the carboxyl groups of the basic amino acids L-arginine or L-lysine. G3m: 25 ug trypsin per CR-column, immobilized on dextran. 260 ST-units immobilized per CR-column. This CR-column cuts at least 50 ug tubulin per application. Nr. 15 Storage buffer: 50 mM Tris/HCl at pH 8. 0Nr. 67 Reaction buffer: 50 mM phosphate at pH 8. 0 (S?rensen)Nr. 68 Washing buffer: 50 mM phosphate at pH 8. 0, 1 M NaCl. Group: Enzymes. Synonyms: α-trypsin; β-trypsin; cocoonase; parenzyme; parenzymol; tryptar; trypure; pseudotrypsin; tryptase; tripcellim; sperm receptor hydrolase; Alpha-trypsin; Beta-trypsin; EC 3. 4. 21. 4; Trypsin. Enzyme Commission Number: EC 3. 4. 21. 4. Storage: 4 °C. Source: Bovine pancreas. α-trypsin; β-trypsin; cocoonase; parenzyme; parenzymol; tryptar; trypure; pseudotrypsin; tryptase; tripcellim; sperm receptor hydrolase; Alpha-trypsin; Beta-trypsin; EC 3. 4. 21. 4; Trypsin; Immobilized TPCK-Trypsin; Immobilized Trypsin; TPCK-Trypsin. Cat No: NATE-1772. | |
| Immobilized Trypsin, TPCK Treated (Agarose Resin) | Trypsin immobilized on beaded agarose makes it possible to eliminate enzyme contamination of tryptic digests. The trypsin can be easily removed from the digest by separating the trypsin gel from the digestion solution. The Thermo Scientific Immobilized TPCK Trypsin is treated with L-1-tosylamido-2-phenylethyl chloromethyl ketone (TPCK), which is a reagent that has been reported to inhibit chymotrypsin activity without effect on trypsin. Trypsin is a 23,200 molecular weight protein with a pH optimum between 7.5 and 9.0. The isoelectric points of trypsinogen and trypsin are 10.5 and 9.3, respectively. Trypsin has a wide range of applications including amino acid analys...estimated from the number of lysine and arginine residues in the protein. Ionexchange chromatography, paper electrophoresis or peptide mapping can be used to separate digestion fragments. Group: Enzymes. Synonyms: Immobilized Trypsin. Enzyme Commission Number: EC 3.4.21.4. Trypsin. Activity: > 200 TAME units per mL of gel. Storage: Upon receipt store at 4°C. Product is shipped at ambient temperature. Form: 2mL of settled gel supplied as a 50% slurry containing glycerol and 0.05% sodium azide as a preservative. Source: Bovine pancreas. Immobilized Trypsin, TPCK Treated (Agarose Resin); Immobilized Trypsin; Trypsin; Protein Fragmentation Enzymes Kits. Cat No: NATE-1867. | |
| K 259-2 | K-259-2, a new inhibitor of Ca2+ and calmodulin-dependent cyclic nucleotide phosphodiesterase, was isolated from the cultured broth of Micromonospora olivasterospora K-259. IC50 values for the effect of K-259-2 against Ca2+ and calmodulin-stimulated activity of the enzyme preparations from bovine brain and heart were 6.6 and 2.9 microM, respectively. Synonyms: K-259-2; 1,6,8-Trihydroxy-3-[(Z)-2-ethyl-2-butenyl]-9,10-dihydro-9,10-dioxoanthracene-2-carboxylic acid. CAS No. 102819-46-5. Molecular formula: C21H18O7. Mole weight: 382.36. |  |
| Lactosyl Ceramide, Bovine | Lactosyl Ceramide neutral glycosphingolipid (GSL) that is the common precursor of the ganglio-, globo-, globoiso-, lacto-, neolacto-, and muco-series of GSL. Promotes a time- and concentration-dependent proliferation of aortic smooth muscle cells via specific activation of ERK 1 (p44 MAP kinase). Also stimulates Ras-GTP loading, MEK and Raf kinases, p44 MAP kinase, and c-fos expression in human aortic smooth muscle cells. Applications: An inducer of ras-gtp loading, mek and raf kinases, p44 map kinase, c-fos expression. Group: Coenzymes. Synonyms: Ceramide β-lactoside. CAS No. 4682-48-8. Purity: ≥98%. Mole weight: 960.4. Form: Solid. Ceramide β-lactoside; Lactosyl Ceramide, Bovine; 4682-48-8. Cat No: COEC-107. | |
| L-Lactic dehydrogenase | L-Lactic dehydrogenase. Synonyms: IUB: 1.1.1.27;LACTIC DEHYDROGENASE;LACTIC DEHYDROGENASE BOVINE HEART;LACTIC ACID DEHYDROGENASE;LACTATE DEHYDROGENASE;LACTATE DEHYDROGENASE, HUMAN MUSCLE;LACTATE DEHYDROGENASE ISOENZYME-1, HUMAN;L-LACTATE DEHYDROGENASE. CAS No. 9001-60-9. Product ID: CDF4-0043. Category: Enzyme Preparations. Product Keywords: Food Ingredients; Enzyme Preparations; L-Lactic dehydrogenase; CDF4-0043; 9001-60-9; 232-617-8; 9001-60-9. Purity: 0.99. Color: White. EC Number: 232-617-8. Physical State: Suspension. Storage: 2-8°C. | |
| low-density-lipoprotein receptor kinase | Phosphorylates the last serine residue (Ser-833) in the cytoplasmic domain of the low-density lipoprotein receptor from bovine adrenal cortex. Casein can also act as a substrate but with lower affinity. GTP can act instead of ATP. Group: Enzymes. Synonyms: ATP:low-density-lipoprotein-L-serine O-phosphotransferase; LDL receptor kinase; [low-density-lipoprotein] kinase; low-density lipoprotein kinase; low-density-lipoprotein receptor kinase (phosphorylating); STK7. Enzyme Commission Number: EC 2.7.11.29. CAS No. 107445-00-1. 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-3149; low-density-lipoprotein receptor kinase; EC 2.7.11.29; 107445-00-1; ATP:low-density-lipoprotein-L-serine O-phosphotransferase; LDL receptor kinase; [low-density-lipoprotein] kinase; low-density lipoprotein kinase; low-density-lipoprotein receptor kinase (phosphorylating); STK7. Cat No: EXWM-3149. | |
| LY83583 | LY83583 is an Msp1 inhibitor, a guanylate cyclase inhibitor and a cGMP modulator. LY83583 inhibits soluble guanylate cyclase in human platelets with an IC50 of 2 μM. LY83583 also inhibits leukotriene synthesis in guinea pig lung and rat peritoneal cells with an IC50 of 1.8 μM, and is a noncompetitive inhibitor of glutathione reductase in bovine intestinal mucosa with a Ki of 3 μM. Uses: Enzyme inhibitors. Synonyms: 6-Anilino-5,8-quinolinedione; 6-(Phenylamino)quinoline-5,8-dione; 6-(Phenylamino)-5,8-quinolinedione; 6-Anilinoquinoline-5,8-quinone; 6-(phenylamino)quinoline-5,8-dione. Grades: ≥95%. CAS No. 91300-60-6. Molecular formula: C15H10N2O2. Mole weight: 250.25. | |
| magnolysin | An endopeptidase of 58 kDa known from bovine pituitary neurosecretory granules and bovine and human corpus luteum. Inhibited by EDTA. Group: Enzymes. Synonyms: bovine neurosecretory granule protease cleaving pro-oxytocin/neurophysin; pro-oxytocin/neurophysin convertase; prooxyphysin proteinase; pro-oxytocin convertase. Enzyme Commission Number: EC 3.4.24.62. CAS No. 162875-09-4. 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-4345; magnolysin; EC 3.4.24.62; 162875-09-4; bovine neurosecretory granule protease cleaving pro-oxytocin/neurophysin; pro-oxytocin/neurophysin convertase; prooxyphysin proteinase; pro-oxytocin convertase. Cat No: EXWM-4345. | |
| N-Acetylglucosamine endo-β-galactosidase 16C from Clostridium perfringens, Recombinant | Endo-β-Galactosidase is an enzyme that hydrolyzes internal β-galactosidic linkages of oligosaccharides in poly-N-acetyl-lactosamine structures. This enzyme resembles the Escherichia freundii enzyme due to its specificity towards bovine corneal keratan sulphate, milk oligosaccharides and the glycolipids lacto-N-neotetraosylceramide and lacto-N-tetraosylceramide. Group: Enzymes. Synonyms: β-Galactosidase bacterial; Keratanase; Endo-β-galactosidase; keratan sulfate endogalactosidase; keratan-sulfate 1,4-β-D-galactanohydrolase; EC 3.2.1.103. Enzyme Commission Number: EC 3.2.1.-. Purity: >90% by SDS-PAGE. Endo-β-galactosidase. Mole weight: 33.7 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. β-Galactosidase bacterial; Keratanase; Endo-β-galactosidase; keratan sulfate endogalactosidase; keratan-sulfate 1,4-β-D-galactanohydrolase; EC 3.2.1.-; N-Acetylglucosamine endo-β-galactosidase 16C. Cat No: NATE-1412. | |
| N-acetyl neuraminyl galactosyl glucosyl ceramide β-1,4-N-acetylgalactosaminyltransferase | Requires Mn2+. Only substances containing sialic acid residues can act as acceptors; bovine fetuin is the best acceptor tested. Group: Enzymes. Synonyms: uridine diphosphoacetylgalactosamine-acetylneuraminyl(α 2?3)galactosyl(β 1?4)glucosyl β1?4-acetylgalactosaminyltransferase; UDP-N-acetyl-D-galactosamine:N-acetylneuraminyl-2,3-α-D-g. Enzyme Commission Number: EC 2.4.1.165. CAS No. 109136-50-7. 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-2390; N-acetyl neuraminyl galactosyl glucosyl ceramide β-1,4-N-acetylgalactosaminyltransferase; EC 2.4.1.165; 109136-50-7; uridine diphosphoacetylgalactosamine-acetylneuraminyl(α 2?3)galactosyl(β 1?4)glucosyl β1?4-acetylgalactosaminyltransferase; UDP-N-acetyl-D-galactosamine:N-acetylneuraminyl-2,3-α-D-galactosyl-1,4-β-D-glucosylceramide β-1,4-N-acetylgalactosaminyltransferase; UDP-N-acetyl-D-galactosamine:N-acetylneuraminyl-(2?3)-α-D-galactosyl-(1?4)-β-D-glucosyl(1<->1)ceramide 4-β-N-acetylgalactosaminyltransferase; UDP-N-acetyl-D-galactosamine:N-acetylneuraminyl-(2?3)-α-D-galactosyl-(1?4)-β-D-glucosyl-(1<->1)-ceramide 4-β-N-acetylgalactosaminyltransferase. Cat No: EXWM-2390. | |
| N-Acylmannosamine 1-Dehydrogenase from Pseudomonas sp., Recombinant | In enzymology, a N-acylmannosamine 1-dehydrogenase (EC 1.1.1.233) is an enzyme that catalyzes the chemical reaction:N-acyl-D-mannosamine + NAD+<-> N-acyl-D-mannosaminolactone + NADH + H+. Thus, the two substrates of this enzyme are N-acyl-D-mannosamine and NAD+, whereas its 3 products are N-acyl-D-mannosaminolactone, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. Group: Enzymes. Synonyms: N-acylmannosamine 1-dehydrogenase; EC 1.1.1.233; N-acylmannosamine dehydrogenase; N-acetyl-D-mannosamine dehydrogenase; N-acyl-D-mannosamine dehydrogenase; N-acylmannosamine dehydrogenase; 117698-08-5. Enzyme Commission Number: EC 1.1.1.233. CAS No. 117698-08-5. N-acylmannosamine 1-dehydrogenase. Mole weight: mol wt ~120 kDa (gel filtration). Activity: > 45 units/mg protein. Storage: -20°C. Form: lyophilized powder; Powder also contains bovine albumin and sucrose. Source: E. coli. Species: Pseudomonas sp. N-acylmannosamine 1-dehydrogenase; EC 1.1.1.233; N-acylmannosamine dehydrogenase; N-acetyl-D-mannosamine dehydrogenase; N-acyl-D-mannosamine dehydrogenase; N-acylmannosamine dehydrogenase; 117698-08-5. Cat No: NATE-0470. | |
| Native Almond α (1-3,4) Fucosidase | 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 ...buffer supplied with the enzyme, >85% of the original activity is observed after two months at 2-8°C. In the buffer solution at 37°C, the half-life is approximately 80 hours. Storage: Shipped on ice pack for next day delivery. Store at -20°C. Store lyophilized enzyme at-20°C. Enzyme reconstituted with the provided reaction buffer is stable at 2-8°C for at least two months and may be stored at-20°C for at least six months. Avoid repeated freeze/thaw cycles. Form: Lyophilized from 50 mM sodium acetate, 3 mg/ml bovine serum albumin (pH 5.0). Source: Almond meal. Species: Almond. α (1-3,4) Fucosidase; alpha-L-fucosidase; Alpha-Fucosidase; FUCA1; FUCA. Cat No: NATE-0260. | |
| Native Bovine Acid Phosphatase, Prostatic | Acid phosphatases (APase) are a family of enzymes that non-specifically catalyze the hydrolysis of monoesters and anhydrides of phosphoric acid to produce inorganic phosphate at an optimum pH of 4 to 7. Acid phosphatase from potatoes is a 111 kDa diner consisting of two subunits at 41 and 35 kDa. This phosphatase has also been shown to cleave DNA. Group: Enzymes. Synonyms: acid phosphatase; 9001-77-8; acid phosphomonoesterase; phosphomonoesterase; glycerophosphatase; acid monophosphatase; acid phosphohydrolase; acid phosphomonoester hydrolase; uteroferrin; acid nucleoside diphosphate phosphatase; orthophosphoric-monoester phosphohydrolase (acid optimum); EC 3.1.3.2; APase. Enzyme Commission Number: EC 3.1.3.2. CAS No. 9001-77-8. Apase. Activity: ~10 units/g solid. Storage: -20°C. Form: Partially purified, lyophilized powder. Source: Bovine prostate. Species: Bovine. acid phosphatase; 9001-77-8; acid phosphomonoesterase; phosphomonoesterase; glycerophosphatase; acid monophosphatase; acid phosphohydrolase; acid phosphomonoester hydrolase; uteroferrin; acid nucleoside diphosphate phosphatase; orthophosphoric-monoester phosphohydrolase (acid optimum); EC 3.1.3.2; APase. Cat No: NATE-0081. | |
| Native Bovine Alkaline Phosphatase | Alkaline phosphatase (ALP, ALKP, ALPase, Alk Phos) (EC 3.1.3.1) is a hydrolase enzyme responsible for removing phosphate groups from many types of molecules, including nucleotides, proteins, and alkaloids. The process of removing the phosphate group is called dephosphorylation. As the name suggests, alkaline phosphatases are most effective in an alkaline environment. It is sometimes used synonymously as basic phosphatase. Bovine intestinal alkaline phosphatase is a dimeric, membrane-derived glycoprotein. at least three isoforms exist, which typically possess two n-linked and one or more o-linked glycans per monomer.2 the enzyme requires zinc, and magnesium or calcium divalen...r proteins for elisa, western blotting, and hist ochemical detection. it is routinely used to dephosphorylate proteins and nucleic acids. it may be used for protein labeling when high sensitivity is required. alkaline phosphatase may be also be used to dephosphorylate the 5?-termini of dna or rna to prevent self-ligation. dna or rna can also be tagged with radiolabeled phosphate (via t4 polynucleotide kinase) after dephosphorylation with alkaline phosphatase. this product has been used to study the mon oclonal alkaline phosphatase-anti-alkaline phosphatase (apaap) complex. high specific activity grade recommended for antibody and protein conjugation. Group: Enzymes. Synonyms | |
| Native Bovine α (1-2,3,4,6) Fucosidase | 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 (1-2,3,4,6) Fucosidase; alpha-L-fucosidase; Alpha-Fucosidase; FUCA1; FUCA. FUCA. Source: Bovine kidney. Species: Bovine. α (1-2,3,4,6) Fucosidase; alpha-L-fucosidase; Alpha-Fucosidase; FUCA1; FUCA. Cat No: NATE-0261. | |
| Native Bovine α-Chymotrypsinogen A | Chymotrypsinogen is a proteolytic enzyme and a precursor (zymogen) of the digestive enzyme chymotrypsin. It is a single polypetide chain consisting of 245 amino acid residues. It is synthesized in the acinar cells of the pancreas and stored inside membrane-bounded granules at the apex of the acinar cell. The cell is then stimulated by either a hormonal signal or a nerve impulse and the contents of the granules spill into a duct leading into the duodenum. Applications: The enzyme has been used in the non-invasive determination of solid-state protein conformation using near infrared (nir) spectroscopy. it has been used to study the partitioning of protein in polymer/polymer aqueous two-phase systems. the enzyme has also been used for self-interaction chromatography applications, to test the rapid measurement of protein osmotic second virial coefficients. in this technique, the protein is immobilized on chromatographic particles and its retention is measured using isocratic elution. Group: Zymogens. Synonyms: 9035-75-0; Chymotrypsinogen; α-Chymotrypsino. CAS No. 9035-75-0. Chymotrypsinogen A. Activity: > 40 units/mg solid. Storage: -20°C. Form: essentially salt-free, lyophilized powder. Source: Bovine Pancreas. Species: Bovine. 9035-75-0; Chymotrypsinogen; α-Chymotrypsinogen A; Chymotrypsinogen A; Chymotrypsin. Cat No: NATE-0748. | |
| Native Bovine α-L-Fucosidase | In enzymology, an alpha-L-fucosidase (EC 3.2.1.51) is an enzyme that catalyzes the chemical reaction:an alpha-L-fucoside + H2O<-> L-fucose + an alcohol. Thus, the two substrates of this enzyme are alpha-L-fucoside and H2O, whereas its two products are L-fucose and alcohol. This enzyme belongs to the family of hydrolases, specifically those glycosidases that hydrolyse O-and S-glycosyl compounds. This enzyme participates in n-glycan degradation and glycan structures-degradation. Group: Enzymes. Synonyms: α-L-Fucosidase; EC 3.2.1.51; α-fucosidase. Enzyme Commission Number: EC 3.2.1.51. CAS No. 9037-65-4. FUCA. Activity: > 2.0 units/mg protein (biuret). Storage: 2-8°C. Form: ammonium sulfate suspension. Suspension in 3.2 M (NH4)2SO4, 10 mM NaH2PO4 10 mM Citrate, pH 6.0. Source: Bovine kidney. Species: Bovine. α-L-Fucosidase; EC 3.2.1.51; α-fucosidase. Cat No: NATE-0266. | |
| Native Bovine Auto-Activated Protein Kinase | Auto-Activated Protein Kinase phosphorylates and inactivates protein phosphatase 2A. The funtion appears to be related to the catalytic domain of p21-activated p65 (PAK) protein kinase which is produced in apoptotic cells. AK is also involved in cytoskeleton organization and other signal transduction processes. Group: Enzymes. Synonyms: AK; Auto-Activated Protein Kinase. AK. Activity: ~17,000 units/mg protein. Stability: -70°C. Form: aqueous solution. Source: bovine kidney. Species: Bovine. AK; Auto-Activated Protein Kinase. Cat No: NATE-0042. | |
| Native Bovine β(1-3,4)-Galactosidase | Hydrolyzes non-reducing terminal galactose β(1-3) and β(1-4) linkages. Can be used in conjunction with other β-galactosidases for exoglycosidase sequencing. Applications: The enzyme has applications in the analysis of a wide variety of glycoconjugates. it is particularly useful for ensuring the complete removal of β(1-3) and β(1-4)-linked non-reducing terminal galactose residues of oligosaccharides. gal β(1-6) glcnac is hydrolyzed more slowly, however this linkage is not normally encountered in native complex glycans. this activity towards β(1-3) and β(1-4)-linked galactose contrasts with that of our other β-galactosidases whi...tose residues. Group: Enzymes. Synonyms: β-galactosidase; beta-gal; β-gal; lactase; β-lactosidase; maxilact; hydrolact; β-D-lactosidase; lactozym; trilactase; β-D-galactanase; oryzatym; sumiklat; β-D-galactoside galactohydrolase. β-gal. Mole weight: ~68 kD. Form: 20 mM sodium Citrate phosphate, 150 mM NaCl (pH 4.0). Source: Bovine testis. Species: Bovine. β(1-3,4)-Galactosidase; β-galactosidase; beta-gal; β-gal; EC 3.2.1.23; lactase; β-lactosidase; maxilact; hydrolact; β-D-lactosidase; S 2107; lactozym; trilactase; β-D-galactanase; oryzatym; sumiklat; β-D-galactoside galactohydrolase. Cat No: NATE-0973. | |
| Native Bovine β-1,4-Galactosyl Transferase | β-1,4-Galactosyl Transferase catalyzes the transfer of galactose from UDP-galactose to the terminal N-acetylglucosamine residues on elongating oligosaccharide chains. It is also considered to be a biosynthetic enzyme of the Golgi apparatus. β-1,4-Galactosyl Transferase can also be found on the cell surface functioning as a cell-adhesion molecule during various cellular interactions by binding to N-acetylglucosamine containing oligosaccharide substrates or ligands in the extracellular matrix. Group: Enzymes. Synonyms: lactose synthase; UDP-α-D-galactose-glucose galactosyltransferase; N-acetyllactosamine synthase; uridine diphosphogalactose-glucose galactosyltransferase; lactose synthetase; UDP-galactose:D-glucose 4-β-D-galactotransferase; UDP-galactose:D-glucose 4-β-D-galactosyltransferase; EC . Enzyme Commission Number: EC 2.4.1.22. CAS No. 9030-11-9. Galactosyltransferase. Mole weight: Mr ~44000. Activity: > 0.6 units/mg. Storage: -20°C. Source: Bovine milk. Species: Bovine. lactose synthase; UDP-α-D-galactose-glucose galactosyltransferase; N-acetyllactosamine synthase; uridine diphosphogalactose-glucose galactosyltransferase; lactose synthetase; UDP-galactose:D-glucose 4-β-D-galactotransferase; UDP-galactose:D-glucose 4-β-D-galactosyltransferase; EC 2.4.1.22; 9030-11-9. Cat No: NATE-0760. | |
| Native Bovine β-Galactosidase | β-galactosidase, also called beta-gal or β-gal, is a hydrolase enzyme that catalyzes the hydrolysis of β-galactosides into monosaccharides. Substrates of different β-galactosidases include ganglioside GM1, lactosylceramides, lactose, and various glycoproteins. Applications: Β-galactosidase was used in the production of a stabilized, single reagent for alcohol analysis. Group: Enzymes. Synonyms: β-Galactosidase; beta-gal; β-gal; GLB; 9031-11-2; EC 3.2.1.23; lactase; β-lactosidase; maxilact; hydrolact; β-D-lactosidase; S 2107; lactozym; trilactase; β-D-galactanase; oryzatym; sumiklat. Enzyme Commission Number: EC 3.2.1.23. CAS No. 9031-11-2. β-gal. Activity: > 0.15 units/mg protein. Storage: -20°C. Form: lyophilized powder. Source: Bovine liver. Species: Bovine. β-Galactosidase; beta-gal; β-gal; GLB; 9031-11-2; EC 3.2.1.23; lactase; β-lactosidase; maxilact; hydrolact; β-D-lactosidase; S 2107; lactozym; trilactase; β-D-galactanase; oryzatym; sumiklat. Cat No: NATE-0294. | |
| Native Bovine β-Glucuronidase | β-glucuronidase catalyzes the breakdown of complex carbohydrates. In humans it converts conjugated bilirubin into the unconjugated form, making bilirubin suitable for reabsorption. Applications: Β-glucuronidase is used as a reporter gene in gus assays to monitor gene expression. 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. Activity: Type B-10, ~10,000 units/mg solid; Type B-1, > 1,000,000 units/g solid; Type B-3, > 2,000,000 units/g solid. Source: Bovine liver. Species: Bovine. 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-0329. | |
| Native Bovine β-N-Acetylglucosaminidase | This enzyme, sometimes called β-N-acetylhexosaminidase, is reported to liberate terminal β-linked N-acetylglucosamine and N-acetylgalactosamine from a variety of substrates. The activity of β-N-actylglucosaminidase may be determined with the chromogenic substrate p-nitrophenyl-N-acetyl-β-D-glucosaminide. β-N-actylglucosaminidase hydrolyzes the terminal nonreducing N-acetyl-D-hexosamine residues. This enzyme contains two predominant isozymes, Hex A, a heterodimer, and Hex B, a homodimer. N-acetylglucosamine, acetamide, N-2-acetamido-2-deoyglucosylamine, N-acetylnojirimycin, and N-acetyldeoxynojirmycin are known inhibitors. Applications: Bovine ki...idase A; N-acetylhexosaminidase; β-D-hexosaminidase; 9012-33-3; EC 3.2.1.52. Enzyme Commission Number: EC 3.2.1.52. CAS No. 9012-33-3. β-N-Acetylhexosaminidase. Activity: 10-50 units/mg protein. Storage: 2-8°C. Form: ammonium sulfate suspension. Suspension in 3.2 M (NH4)2SO4, pH approx. 6.0. Source: Bovine kidney. Species: Bovine. hexosaminidase; β-acetylaminodeoxyhexosidase; N-acetyl-β-D-hexosaminidase; N-acetyl-beta-hexosaminidase; β-hexosaminidase; β-acetylhexosaminidinase; β-D-N-acetylhexosaminidase; β-N-acetyl-D-hexosaminidase; β-N-acetylglucosaminidase; hexosaminidase A; N-acetylhexosaminidase; β-D-hexosaminidase; | |
| Native Bovine Carbonic Anhydrase | The carbonic anhydrases (or carbonate dehydratases) form a family of enzymes that catalyze the rapid interconversion of carbon dioxide and water to bicarbonate and protons (or vice versa), a reversible reaction that occurs relatively slowly in the absence of a catalyst. The active site of most carbonic anhydrases contains a zinc ion; they are therefore classified as metalloenzymes. It was from bovine erythrocytes. a dialyzed, lyophilized powder. Applications: Co2 determination in blood; elimination of co2 in reagents for acidity testing; carboxy group transfers; reduction reactions. Group: Enzymes. Synonyms: carbonic anhydrases; carbonate dehydratases; EC 4.2.1.1; anhydrase; carbonate anhydrase; carbonic acid anhydrase; carboxyanhydrase; carbonic anhydrase A; carbonate hydro-lyase. Enzyme Commission Number: EC 4.2.1.1. CAS No. 9001-03-0. Carbonic Anhydrase. Mole weight: 29.0 kDa (Theoretical) 30 kDa (Lindskog et al. 1971). Activity: > 3,000 units per mg dry weight. Storage: 2-8°C. Form: lyophilized powder. Source: Bovine Erythrocytes. Species: Bovine. carbonic anhydrases; carbonate dehydratases; EC 4.2.1.1; anhydrase; carbonate anhydrase; carbonic acid anhydrase; carboxyanhydrase; carbonic anhydrase A; carbonate hydro-lyase. Cat No: NATE-0101. | |
| Native Bovine Carboxypeptidase A | Carboxypeptidase as isolated from Bovine pancreas glands is a metalloenzyme that contains 1 g atom of zinc per mole of protein. It catalyzes the hydrolysis of the carboxyl-terminal peptide bond in peptides and proteins. It is primarily specific to aromatic and hydrophobic side chains such as phenylalanine, tryptophan or leucine. The enzyme also exhibits esterase activity. It is inhibited by beta-phenylpropionate and indole acetate. Protein determined by e1%/278. Applications: Carboxypeptidase a from bovine pancreas has been used in a study to investigate the expression of a soluble and activatable form of bovine procarboxypeptidase a in escherichia coli. carboxypeptidase a fr...dase A1; pancreatic procarboxypeptidase A; 11075-17-5; Carboxypolypeptidase; Peptidyl-L-amino-acid hydrolase; carboxypeptidase A; carboxypolypeptidase; pancreatic carboxypeptidase A; tissue carboxypeptidase A. Enzyme Commission Number: EC 3.4.17.1. CAS No. 11075-17-5. CPA1. Mole weight: mol wt ~35 kDa. Activity: > 50 units/mg protein. Storage: 2-8°C. Form: aqueous suspension. Source: Bovine pancreas. Species: Bovine. EC 3.4.17.1; CPA1; CPA; carboxypeptidase A1; pancreatic procarboxypeptidase A; 11075-17-5; Carboxypolypeptidase; Peptidyl-L-amino-acid hydrolase; carboxypeptidase A; carboxypolypeptidase; pancreatic carboxypeptidase A; tissue carboxypeptidase A. Cat No: NATE-0150 | |
| Native Bovine Catalase | Catalase activates the decomposition of hydrogen peroxide, a reactive oxygen species, into water and oxygen. It functions as a natural antioxidant, protecting cells against oxidative damage to proteins, lipids and nucleic acids. Catalase has also been used to study the role reactive oxygen species play in gene expression and apoptosis. Group: Enzymes. Synonyms: EC 1.11.1.6; Catalase; catalase; equilase; caperase; optidase; catalase-peroxidase; CAT; H2O2:H2O2 oxidoreductase; 9001-05-2. Enzyme Commission Number: EC 1.11.1.6. CAS No. 9001-5-2. CAT. Activity: Type 1 (Suspension) > 20,000 units per mg; Type 2 (Filtered) > 40,000 units per mg; Type 3 (Lyophilized) > 3,000 units per mg. Storage: All preparations are stable for 12 months at 2-8°C. Lyophilized preparations should be protected from moisture. Form: A partially purified, lyophilized powder. Source: Bovine Liver. Species: Bovine. EC 1.11.1.6; Catalase; catalase; equilase; caperase; optidase; catalase-peroxidase; CAT; H2O2:H2O2 oxidoreductase; 9001-05-2. Cat No: NATE-0105. | |
| Native Bovine Cathepsin B | Cathepsin B has been found to cleave procaspase 1 and procaspase 11 and to induce apoptosis in digitonin-permeabilized cells. Translocation of cathepsin B from the cytoplasm to the nucleus contributes to bile salt induced apoptosis of Rat hepatocytes. Levels of cathepsin B in PC12 cells significantly decrease 12 to 24 hours after apoptosis is induced. Group: Enzymes. Synonyms: CTSB; cathepsin B; 9047-22-7; APPS; CPSB; cathepsin B1 (obsolete); cathepsin II. CAS No. 9047-22-7. Cathepsin B. Activity: > 10 units/mg protein. Form: Lyophilized powder containing sodium phosphate, sodium chloride and ~6% EDTA as stabilizer. Source: Bovine spleen. Species: Bovine. CTSB; cathepsin B; 9047-22-7; APPS; CPSB; cathepsin B1 (obsolete); cathepsin II. Cat No: NATE-0167. | |
| Native Bovine Cathepsin C | Cathespin C is a dipeptidyl aminopeptidase that can sequentially remove dipeptides from a peptide chain with an unsubstituted N-terminus. The enzyme exhibits a preference for glycine and proline as N-terminal aminoacids. Substrates that have an N-terminal lysyl or arginyl residue, or a penultimate proryl residue are not targeted by this enzyme. The endopeptidase activity requires the presence of halide ions and sulfydryl activators. Applications: Cathepsin c has been used in a study that demonstrated the potential of a proteomics approach to identify novel proteins expressed by extravillous trophoblast and to uncover the mechanisms leading to disease states in pregnancy. catheps...s. Synonyms: CTSC; cathepsin C; 9032-68-2; EC 3.4.14.1; dipeptidyl aminopeptidase I; dipeptidyl transferase; dipeptidyl transferase; dipeptide arylamidase I; DAP I; dipeptidyl-peptidase I; DPP-I; CPPI; DPP1; DPPI; HMS; JP; JPD; PALS; PDON1; PLS. Enzyme Commission Number: EC 3.4.14.1. CAS No. 9032-68-2. CTSC. Activity: > 5 units/mg protein. Form: Lyophilized from a 1 M sodium chloride solution. Source: Bovine spleen. Species: Bovine. CTSC; cathepsin C; 9032-68-2; EC 3.4.14.1; dipeptidyl aminopeptidase I; dipeptidyl transferase; dipeptidyl transferase; dipeptide arylamidase I; DAP I; dipeptidyl-peptidase I; DPP-I; CPPI; DPP1; DPPI; HMS; JP; JPD; PALS; PDON1; PLS. Cat No: NATE-0170. | |
| Native Bovine Cathepsin D | Cathepsin D is an endosomal-lysosomal aspartic protease implicated in breast cancer metastasis and Alzheimers disease. Lysosomal release of cathepsin D has been found to precede cytochrome c release and loss of membrane potential in apoptotic Human foreskin fibroblasts. Cathepsin D levels in PC12 cells increase 12 to 24 hours after apoptosis is induced. Group: Enzymes. Synonyms: CTSD; cathepsin D; 9025-26-7; EC 3.4.23.5; CLN10; CPSD; HEL-S-130P. Enzyme Commission Number: EC 3.4.23.5. CAS No. 9025-26-7. CTSD. Mole weight: 45 kDa. Activity: > 2.0 units/mg protein. Form: Lyophilized powder containing Citrate buffer salts. Source: Bovine spleen. Species: Bovine. CTSD; cathepsin D; 9025-26-7; EC 3.4.23.5; CLN10; CPSD; HEL-S-130P. Cat No: NATE-0171. | |
| Native Bovine Cholesterol Esterase | Cholesterol esterase (CE) is a reversible enzyme that can hydrolyze or synthesize fatty acid esters of cholesterol and other sterols. Hydrolysis of water insoluble long chain fatty acid esters requires bile salt activation. Hydrolysis of water soluble esters of short chain fatty acids and lysophospholipids does not require activation by bile salts. It also hydrolyzes tri-, di-, and mono-acylglycerols, phospholipids, lysophospholipids, and ceramide. This monomeric glycoprotein may have multiple functions in lipid and lipoprotein metabolism, as well as in atherosclerosis. Protein determined by biuret. Applications: Cholesterol esterase bound to membrane-associated heparin on b...terase; cholesteryl ester hydrolase; sterol ester hydrolase; cholesterol ester hydrolase; cholesterase; acylcholesterol lipase; EC 3.1.1.13; 9026-00-0; sterol esterase; CE. Enzyme Commission Number: EC 3.1.1.13. CAS No. 9026-00-0. Cholesterol Esterase. Activity: > 200 units/g protein. Storage: -20°C. Form: Lyophilized powder. This product is partially purified from bovine pancreas and is supplied as an off-white to tan lyophilized powder containing 30-65% protein (biuret), potassium phosphate. Source: Bovine pancreas. Species: Bovine. cholesterol esterase; cholesteryl ester synthase; triterpenol esterase; cholesteryl esterase; cholesteryl ester hydrolase; sterol ester hydrol | |
| Native Bovine Chymotrypsinogen A | Chymotrypsinogen is a proteolytic enzyme and a precursor (zymogen) of the digestive enzyme chymotrypsin. It is a single polypetide chain consisting of 245 amino acid residues. It is synthesized in the acinar cells of the pancreas and stored inside membrane-bounded granules at the apex of the acinar cell. The cell is then stimulated by either a hormonal signal or a nerve impulse and the contents of the granules spill into a duct leading into the duodenum. Group: Zymogens. Synonyms: chymotrypsinogen A; Chymotrypsinogen; Chymotrypsin. CAS No. 9035-75-0. Purity: Purified, Five times crystallized, electrophoretically homogeneous. Chymotrypsinogen A. Activity: Activates to at least 45 units per mg protein. Stability: The enzyme is stable for days in solution at pH 3.0 and for years as a dry powder when stored refrigerated. Storage: Store at 2-8°C. Form: lyophilized powder. Source: Bovine Pancreas. Species: Bovine. chymotrypsinogen A; Chymotrypsinogen; Chymotrypsin. Cat No: NATE-0134. | |
| Native Bovine Creatine Phosphokinase | Creatine kinase plays a key role in the energy metabolism of cells with intermittently high and fluctuating energy requirements. Examples of such cells include cardiac or skeletal muscle cells and neural tissues of brain and retina. The enzyme catalyzes the reversible transfer of the phosphoryl group from phosphorylcreatine to ADP, in order to generate ATP.1 The molecular mass of the protein is found to be approximately 80 kDa Da. It is made up of 2 subunits, each having a molecular weight of 40 kDa ± 2000. The lighter subunit is present in larger amounts. Protein determined by biuret. Applications: Creatine phosphokinase from bovine heart has been used to investigate wheth...osphotransferase; CK; CPK; MM-CK; MB-CK; BB-CK; creatine phosphokinase; creatine phosphotransferase; phosphocreatine kinase; adenosine triphosphate-creatine transphosphorylase; Mi-CK; CK-BB; CK-MM; CK-MB; CKMiMi; MiMi-CK; 9001-15-4. Enzyme Commission Number: EC 2.7.3.2. CAS No. 9001-15-4. Activity: > 100 U/mg. Storage: -20°C. Form: salt-free, lyophilized powder. Source: Bovine heart. Species: Bovine. EC 2.7.3.2; ATP:creatine phosphotransferase; CK; CPK; MM-CK; MB-CK; BB-CK; creatine phosphokinase; creatine phosphotransferase; phosphocreatine kinase; adenosine triphosphate-creatine transphosphorylase; Mi-CK; CK-BB; CK-MM; CK-MB; CKMiMi; MiMi-CK; 9001-15-4. Cat No: NATE-0136. | |
| Native Bovine Deoxyribonuclease I | Deoxyribonuclease I (usually called DNase I), is an endonuclease coded by the human gene DNASE1. DNase I is a nuclease that cleaves DNA preferentially at phosphodiester linkages adjacent to a pyrimidine nucleotide, yielding 5'-phosphate-terminated polynucleotides with a free hydroxyl group on position 3', on average producing tetranucleotides. It acts on single-stranded DNA, double-stranded DNA, and chromatin. In addition to its role as a waste-management endonuclease, it has been suggested to be one of the deoxyribonucleases responsible for DNA fragmentation during apoptosis. Protein determined by biuret. Applications: Used for the removal of dna from protein samples. dnase...rom bovine pancreas has also been used in a study to investigate the effects of minor and major groove-binding drugs and intercalators on the dna association of minor groove-binding proteins reca and deoxyribonuclease i. Group: Enzymes. Synonyms: DNASE1; deoxyribonuclease I; deoxyribonuclease-1; DNase I; 9003-98-9; EC 3.1.21.1; pancreatic DNase; DNase; thymonuclease, dornase; dornava; dornavac; pancreatic deoxyribonuclease; pancreatic dornase; deoxyribonuclease (pancreatic); pancreatic DNase; DNAase; deoxyribonucleic phosphatase; alkaline deoxyribonuclease; alkaline DNase; endodeoxyribonuclease I; DNA depolymerase; Escherichia coli endonuclease I; deoxyribonuclease A; DNA end | |
| Native Bovine Deoxyribonuclease II | Deoxyribonuclease II, also called as acid DNAse, hydrolyzes deoxyribonucleotide linkages in native and denatured DNA yielding products with 3'-phosphates. In vitro, its optimum pH range is 4.5-5.0. It also acts upon p-nitrophenyl-phosphodiesters at pH 5.6-5.9. The molecular weight is approximately 38 kDa Da. Applications: Dnase ii from creative enzymes has been used in the dissociation medium during the preparation of embryonic cardiac myocytes from rat heart. deoxyribonuclease ii from bovine spleen has been used in a study that conducted a partial purification of deoxyribonucleases from eggs and liver of xenopus laevis. deoxyribonuclease ii from bovine spleen has also been used in a study to investigate nucleic acid and protein synthesis of splenic lymphocytes. Group: Enzymes. Synonyms: DNASE2; deoxyribonuclease II; EC 3.1.22.1; 9025-64-3; DNase II; pancreatic DNase II; deoxyribonucleate 3'-nucleotidohydrolase; DNase II; pancreati. Enzyme Commission Number: EC 3.1.22.1. CAS No. 9025-64-3. DNASE2. Activity: > 1,000 units/mg protein. Storage: -20°C. Form: essentially salt-free, lyophilized powder. Source: Bovine spleen. Species: Bovine. DNASE2; deoxyribonuclease II; EC 3.1.22.1; 9025-64-3; DNase II; pancreatic DNase II; deoxyribonucleate 3'-nucleotidohydrolase; DNase II; pancreatic DNase II; acid deoxyribonuclease; acid Dnase. Cat No: NATE-0201. | |
| Native Bovine Enterokinase | Enteropeptidase (also called enterokinase) is an enzyme produced by cells of the duodenum and involved in human and animal digestion. It is secreted from intestinal glands (the crypts of Lieberkühn) following the entry of ingested food passing from the stomach. Enteropeptidase converts trypsinogen (a zymogen) into its active form trypsin, resulting in the subsequent activation of pancreatic digestive enzymes. Absence of enteropeptidase results in intestinal digestion impairment. Enterokinase is a highly specific serine protease that is used for the removal of the flag peptide from n-terminal and met-n-terminal fusion proteins. it does not remove the c-terminal flag. Applications...ytic activation of trypsin from trypsinogen. enterokinase is used for site specific cleavage of recombinant fusion proteins containing an accessible enterokinase recognition site for removal of affinity tags. removes flag peptide from n-terminal and met-n-terminal fusion proteins. Group: Enzymes. Synonyms: enterokinase; enteropeptidase; EC 3.4.21.9; 9014-74-8. Enzyme Commission Number: EC 3.4.21.9. CAS No. 9014-74-8. Enterokinase. Mole weight: 150 kDa (consisting of 115kDa and 35kDa subunits.). Activity: Type I, > 20 units/mg protein. Storage: -20°C. Form: powder. Source: Bovine intestine. Species: Bovine. enterokinase; enteropeptidase; EC 3.4.21.9; 9014-74-8. Cat No: NATE-0224. | |
| Native Bovine Factor IXa β | Prepared from Bovine Factor IX by activation with Bovine Factor Xla, this Bovine Factor Xla is removed after activation. Complete activation is observed by SDS-PAGE. The Factor Xla activates FIX in a two-step reaction. In the first step, an internal Arg-Ala bond is cleaved, and in the second step, an Arg-Val bond is cleaved. The second cleavage leads to the liberation of an activation peptide from the NH2-terminal portion of the heavy chain to produce factor IXa&beta. Group: Enzymes. Synonyms: Bovine Factor IXa Beta; Factor IXa Beta; Factor Ixa. Factor IXa Beta. Mole weight: 43.9 kDa. Activity: 3096.00 PEU/mg. Storage: < -60°C. Source: Bovine. Species: Bovine. Bovine Factor IXa Beta; Factor IXa Beta; Factor Ixa. Cat No: NATE-0867. | |
| Native Bovine Factor Xa | Bovine Factor Xa is prepared from Bovine Factor X by activation with Russell's Viper Venom. This RVV-X is removed after activation. Complete activation is observed by SDS-PAGE. Factor Xa, as part of the prothrombinase complex along with the cofactor Va, phospholipids and calcium ions, catalyzes the rapid conversion of prothrombin to thrombin. Group: Enzymes. Synonyms: Bovine Factor Xa; Factor Xa. Factor Xa. Mole weight: 45.3 kDa. Activity: 210.00 IU/mg. Storage: < -60°C. Source: Bovine. Species: Bovine. Bovine Factor Xa; Factor Xa. Cat No: NATE-0868. | |
| Native Bovine Factor X Activated (Xa) | Factor Xa catalyzes the hydrolysis of the Arg-Thr and then Arg-Ile bonds in prothrombin to yield active thrombin. The fairly strict recognition sequence is Ile-Glu (or Asp)-Gly-Arg-↓-X. It may sometimes cleave at other basic residues, depending on the conformation of the target protein. Factor Xa will not cleave if a proline residue follows the arginine of the recognition sequence. Factor xa is a serine endoproteinase and a member of the s1 peptidase family. factor xa plays a critical role in the coagulation cascade by catalyzing the proteolytic conversion of prothrombin to active thrombin. factor xa?s prothrombin conversion activity is greatly enhanced in vivo when c...d with 10 μg of factor xa for 2.5 hours at 37 oc. Group: Enzymes. Synonyms: EC 3.4.21.6; 9002-05-5; thrombokinase; prothrombase; prothrombinase; activated blood-coagulation factor X; autoprothrombin C; thromboplastin; plasma thromboplastin; factor Xa; activated Stuart-Prower factor; activated factor X; coagulation factor Xa. Enzyme Commission Number: EC 3.4.21.6. CAS No. 9002-5-5. Factor Xa. Storage: -20°C. Form: aqueous glycerol solution. Source: Bovine plasma. Species: Bovine. EC 3.4.21.6; 9002-05-5; thrombokinase; prothrombase; prothrombinase; activated blood-coagulation factor X; autoprothrombin C; thromboplastin; plasma thromboplastin; factor Xa; activated Stuart-Pr | |
| Native Bovine Factor XIa | Bovine Factor Xla is purified from freshly collected Bovine Plasma using a combination of salt precipitations and activation on a negative surface. This Factor Xla is a potent activator of both Human and Bovine Factor IX. Bovine Factor XIa purity is determined by SDS-PAGE and shows complete reduction upon incubation with 2-mercaptoethanol. Group: Enzymes. Synonyms: Bovine Factor XIa; Factor XIa. Factor XIa. Storage: < -60°C. Source: Bovine. Species: Bovine. Bovine Factor XIa; Factor XIa. Cat No: NATE-0869. | |
| Native Bovine Galactosyltransferase | Galactosyltransferase catalyzes the transfer of galactosyl molecules in the synthesis of oligosaccharides. Applications: Galactosyltransferase is the catalytic component of the lactose synthetase system; it synthesizes lactose slowly in the absence of the regulatory protein α-lactalbumin. galactosyltransferase will also transfer galactose from udp-galactose to n-acetylglucosamine. this preparation is useful in the determination of α-lactalbumin, udp-galactose, and n-acetylglucosamine. Group: Enzymes. Synonyms: EC 2.4.1.22; UDP-α-D-galactose-glucose galactosyltransferase; N-acetyllactosamine synthase; uridine diphosphogalactose-glucose galactosyltransferase; lactose synthetase; UDP-galactose:D-glucose 4-β-D-galactotransferase; UDP-galactose:D-glucose 4-β-D-galactosyltransferase; 9031-68-9. Enzyme Commission Number: EC 2.4.1.22. CAS No. 9031-68-9. Galactosyltransferase. Storage: -20°C. Form: Lyophilized powder containing Tris, EDTA, and (NH4)2SO4. Source: Bovine milk. Species: Bovine. EC 2.4.1.22; UDP-α-D-galactose-glucose galactosyltransferase; N-acetyllactosamine synthase; uridine diphosphogalactose-glucose galactosyltransferase; lactose synthetase; UDP-galactose:D-glucose 4-β-D-galactotransferase; UDP-galactose:D-glucose 4-β-D-galactosyltransferase; 9031-68-9. Cat No: NATE-0274. | |
| Native Bovine Gamma-Glutamyl Transferase | γ-glutamyl transferase is an enzyme that transfers gamma-glutamyl functional groups. It is found in many tissues, the most notable one being the liver, and has significance in medicine as a diagnostic marker. GGT catalyzes the transfer of the gamma-glutamyl moiety of glutathione to an acceptor that may be an amino acid, a peptide or water (forming glutamate). GGT plays a key role in the gamma-glutamyl cycle, a pathway for the synthesis and degradation of glutathione and drug and xenobiotic detoxification. Other lines of evidence indicate that GGT can also exert a prooxidant role, with regulatory effects at various levels in cellular signal transduction and cellular ...transferase; 9046-27-9; GGTP. Enzyme Commission Number: EC 2.3.2.2. CAS No. 9046-27-9. Purity: Purified. γ-GT. Activity: > 30 U/mg (Dimension Clinical Chemistry System). Appearance: Tan Powder. Storage: -20°C. Form: Lyophilized. Source: Bovine Kidney. Species: Bovine. EC 2.3.2.2; glutamyl transpeptidase; α-glutamyl transpeptidase; γ-glutamyl peptidyltransferase; γ-glutamyl transpeptidase (ambiguous); γ-GPT; γ-GT; γ-GTP; L-γ-glutamyl transpeptidase; L-γ-glutamyltransferase; L-glutamyltransferase; GGT (ambiguous); γ-glutamyltranspeptidase (ambiguous); γ-glutamyltransferase; 9046-27-9; GGTP. Cat No: NATE-0790. | |
| Native Bovine Glutamate Dehydrogenase | Glutamate dehydrogenase (GLDH) is an enzyme, present in most microbes and the mitochondria of eukaryotes, as are some of the other enzymes required for urea synthesis, that converts glutamate to α-ketoglutarate, and vice versa. In animals, the produced ammonia is usually used as a substrate in the urea cycle. Typically, the α-ketoglutarate to glutamate reaction does not occur in mammals, as glutamate dehydrogenase equilibrium favours the production of ammonia and α-ketoglutarate. Group: Enzymes. Synonyms: glutamate dehydrogenase [NAD(P)+]; EC 1.4.1.3; GLDH; glutamic dehydrogenase; glutamate dehydrogenase [NAD(P)]; L-glutamate: NAD(P)+ oxidoreductase (deaminating); L-GLDH; Glutamate Dehydrogenase from bovine liver; L-Glutamic Dehydrogenase; glutamate dehydrogenase. Enzyme Commission Number: EC 1.4.1.3. CAS No. 9001-46-1. GLDH. Mole weight: 260 kDa (gel). Activity: > 500U /mg protein. Appearance: White/off white powder. Storage: -20°C. Form: Freeze dried powder. Source: Bovine liver. Species: Bovine. glutamate dehydrogenase [NAD(P)+]; EC 1.4.1.3; GLDH; glutamic dehydrogenase; glutamate dehydrogenase [NAD(P)]; L-glutamate: NAD(P)+ oxidoreductase (deaminating); L-GLDH; Glutamate Dehydrogenase from bovine liver; L-Glutamic Dehydrogenase; glutamate dehydrogenase. Cat No: DIA-146. | |
| Native Bovine Glutathione Peroxidase | Glutathione peroxidase is an enzyme which reduced lipid hydroperoxides into their corresponding alcohols. It also reduces free hydrogen peroxide in to water. In vivo it is responsible for protecting hemoglobin from oxidative breakdown. Applications: Glutathione peroxidase from bovine erythr ocytes was used as a positive control in cloning and characterization of full-length cdnas encoding two glutathione peroxidases (gpxs) from globodera rost ochiensis. it was used for the determination of glutathione peroxidase activity in human milk. Group: Enzymes. Synonyms: EC 1.11.1.9; GSH peroxidase; selenium-glutathione peroxidase; reduced glutathione peroxidase; 9013-66-5; GSH-Px, Glutathione:hydrogen-peroxide oxido-reductase; Glutathione Peroxidase. Enzyme Commission Number: EC 1.11.1.9. CAS No. 9013-66-5. Mole weight: mol wt 84.5 kDa. Activity: > 300 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing 25% sucrose and 2.5% dithiothreitol with sodium phosphate buffer salts. Source: Bovine erythr ocytes. Species: Bovine. EC 1.11.1.9; GSH peroxidase; selenium-glutathione peroxidase; reduced glutathione peroxidase; 9013-66-5; GSH-Px, Glutathione:hydrogen-peroxide oxido-reductase; Glutathione Peroxidase. Cat No: NATE-0322. | |
| Native Bovine Guanylate Kinase | In enzymology, a guanylate kinase (EC 2.7.4.8) is an enzyme that catalyzes the chemical reaction:ATP + GMP<-> ADP + GDP. Thus, the two substrates of this enzyme are ATP and GMP, whereas its two products are ADP and GDP. This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a phosphate group as acceptor. This enzyme participates in purine metabolism. Group: Enzymes. Synonyms: guanylate kinase; deoxyguanylate kinase; 5'-GMP kinase; GMP kinase; guanosine monophosphate kinase; ATP:GMP phosphotransferase; EC 2.7.4.8; 9026-59-9. Enzyme Commission Number: EC 2.7.4.8. CAS No. 9026-59-9. GMP kinase. Activity: 10-40 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing potassium phosphate buffer salts. Source: Bovine brain. Species: Bovine. guanylate kinase; deoxyguanylate kinase; 5'-GMP kinase; GMP kinase; guanosine monophosphate kinase; ATP:GMP phosphotransferase; EC 2.7.4.8; 9026-59-9. Cat No: NATE-0309. | |
| Native Bovine Hyaluronidase | Hyaluronidase degrades hyaluronan and has been found to be inappropriately regulated during cancer progression. These enzymes randomly cleave β-N-acetylhexosamine-[1?4] glycosidic bonds in hyaluronic acid, chondroitin, and chondroitin sulfates. Group: Enzymes. Synonyms: hyaluronoglucosaminidase; hyaluronidase; hyaluronoglucosidase; chondroitinase; chondroitinase I; hyaluronate 4-glycanohydrolase; EC 3.2.1.35; 37326-33-3. Enzyme Commission Number: EC 3.2.1.35. CAS No. 37326-33-3. Hyaluronidase. Mole weight: mol wt ~55 kDa (four subunits of 14 kDa each). Activity: Type I, 750-3000 units/mg solid; Type II, 300-1,000 units/mg; Type III, 3,000-15,000 units/mg solid; Type IV, 400-1000 units/mg solid. Storage: -20°C. Form: lyophilized powder. Source: Bovine testes. Species: Bovine. hyaluronoglucosaminidase; hyaluronidase; hyaluronoglucosidase; chondroitinase; chondroitinase I; hyaluronate 4-glycanohydrolase; EC 3.2.1.35; 37326-33-3. Cat No: NATE-0347. | |
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