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| Product | Description | |
|---|---|---|
| Native Glycine max (soybean) Lipoxidase | Catalyzes the hydroperoxidation of lipids containing a cis,cis-1,4-pentadiene structure. Applications: The soybean enzyme will use arachidonic acid as a substrate, with ~ 15% of the activity indicated using linoleic acid as the substrate; the product of arachidonic acid oxidation is 12-or 15-hydroperoxyarachidonic acid (12-hpete or 15-hpete). Group: Enzymes. Synonyms: Lipoxygenases; EC 1.13.11.12; 9029-60-1; 13-lipoxidase; carotene oxidase; 13-lipoperoxidase; fat oxidase; 13-lipoxydase; lionoleate:O2 13-oxidoreductase; linoleate 13S-lipoxygenase. Enzyme Commission Number: EC 1.13.11.12. CAS No. 9029-60-1. Lipoxygenase. Mole weight: mol wt 108 kDa (two 54 kDa subunits). Activity: Type I, 500,000-1,000,000 units/mg protein; Type II, > 50,000 units/mg solid. Storage: 2-8°C. Form: Type I, ammonium sulfate suspension, Suspension in 2.3 M (NH4)2SO4 solution, pH approx. 6.0; Type II, lyophilized powder, Contains stabilizer and NaCl. Source: Glycine max (soybean). Lipoxygenases; EC 1.13.11.12; 9029-60-1; 13-lipoxidase; carotene oxidase; 13-lipoperoxidase; fat oxidase; 13-lipoxydase; lionoleate:O2 13-oxidoreductase; linoleate 13S-lipoxygenase. Cat No: NATE-0407. |  |
| Native Green coffee beans α-Galactosidase | Alpha-galactosidase is a glycoside hydrolase enzyme that hydrolyses the terminal alpha-galactosyl moieties from glycolipids and glycoproteins. It is encoded by the GLA gene. Two recombinant forms of alpha-galactosidase are called agalsidase alfa (INN) and agalsidase beta (INN). Group: Enzymes. Synonyms: Alpha-Galactosidase; Galactosidase; EC 3.2.1.22; GLA; GALA; melibiase; α-D-galactosidase; α-galactosidase A; α-galactoside galactohydrolase. Enzyme Commission Number: EC 3.2.1.22. CAS No. 9025-35-8. GLA. Activity: > 9 units/mg protein. Storage: 2-8°C. Form: ammonium sulfate suspension. Suspension in 3.2 M (NH4)2SO4 solution, pH 6.0, containing BSA. Source: Green coffee beans. Alpha-Galactosidase; Galactosidase; EC 3.2.1.22; GLA; GALA; melibiase; α-D-galactosidase; α-galactosidase A; α-galactoside galactohydrolase. Cat No: NATE-0292. | |
| Native Guinea pig Transglutaminase | Transglutaminase from guinea pig liver consists of a single polypeptide chain of 691 amino acid residues. It has six potential glycosylation sites (Asn-X-Ser or Asn-X-Thr), but it is not glycosylated. The molecular mass is approximately 76.6 kDa. It is calcium dependent and has several calcium binding sites. The enzyme is inhibited by iodoacetamide and N-ethylmaleimide in the presence of calcium. It catalyzes the incorporation of small molecular weight amines into γ-glutamine sites of proteins. In the absence of small molecular weight amines, it catalyzes the cross linking of proteins that results in the formation of γ-glutamyl-ε-lysine side chain peptide...h as huntington?s disease and alzheimer?s disease.transglutaminase has also been used in a study to develop a nonradioactive dot blot assay for transglutaminase activity. Group: Enzymes. Synonyms: transglutaminase; EC 2.3.2.13; 80146-85-6; transglutaminase; Factor XIIIa; fibrinoligase; fibrin stabilizing factor; glutaminylpeptide γ-glutamyltransferase; polyamine transglutaminase; tissue transglutaminase; R-glutaminyl-peptide:amine γ-glutamyl transferase; protein-glutamine γ-glutamyltransferase. Enzyme Commission Number: EC 2.3.2.13. CAS No. 80146-85-6. Transglutaminase. Activity: > 1.5 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing Tr | |
| Native Gymnema Extract | United States Pharmacopeia (USP) Reference Standard. Group: Pharmacopeia & metrological institutes standards. |  |
| Native Hansenula sp. Alcohol Oxidase | In enzymology, an alcohol oxidase (EC 1.1.3.13) is an enzyme that catalyzes the chemical reaction:a primary alcohol + O2? an aldehyde + H2O2. Thus, the two substrates of this enzyme are primary alcohol and O2, whereas its two products are aldehyde and H2O2. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with oxygen as acceptor. It employs one cofactor, FAD. Applications: Alcohol oxidase is used to catalyze the oxidation of short-chain, primary, aliphatic alcohols to their respective aldehydes. it may be used to study methanol metabolism is yeasts, such as candida, pichia, and hansenula. it is useful to study protein translocation into peroxisomes. Group: Enzymes. Synonyms: EC 1.1.3.13; 9073-63-6; alcohol oxidase; ethanol oxidase; Alcohol:oxygen oxidoreductase. Enzyme Commission Number: EC 1.1.3.13. CAS No. 9073-63-6. Mole weight: ~600 kDa. Activity: > 0.6 units/mg solid. Form: vacuum-dried powder. Source: Hansenula sp. EC 1.1.3.13; 9073-63-6; alcohol oxidase; ethanol oxidase; Alcohol:oxygen oxidoreductase. Cat No: NATE-0046. | |
| Native Helix pomatia β-(1?3)-D-Glucanase | Glucan endo-1,3-beta-D-glucosidase is an enzyme with system name 3-beta-D-glucan glucanohydrolase. This enzyme catalyses the following chemical reaction:Hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans. This enzyme is marginally active on mixed-link (1->3,1->4)-beta-D-glucans. Applications: Β-(1?3)-d-glucanase from is used to digest β-1,3-glucan, which is a major component of cell walls. β-(1?3)-d-glucanase from helix pomatia has been used fto digest the cell walls of c. albicans. Group: Enzymes. Synonyms: endo-1,3-β-glucanase; laminarinase; laminaranase; oligo-1,3-glucosidase; endo-1,3-β-glucanase; callase; β-1,3-glucanase; kitalase; 1,3-β-D-glucan 3-glucanohydrolase; endo-(1,3)-β-D-glucanase; (1?3)-β-glucan 3-glucanohydrolase; endo-1,3-β-. Enzyme Commission Number: EC 3.2.1.39. CAS No. 9044-93-3. Glucanase. Activity: > 0.2 units/mg. Storage: -20°C. Source: Helix pomatia. endo-1,3-β-glucanase; laminarinase; laminaranase; oligo-1,3-glucosidase; endo-1,3-β-glucanase; callase; β-1,3-glucanase; kitalase; 1,3-β-D-glucan 3-glucanohydrolase; endo-(1,3)-β-D-glucanase; (1?3)-β-glucan 3-glucanohydrolase; endo-1,3-β-D-glucanase; endo-1,3-β-glucosidase; 1,3-β-D-glucan glucanohydrolase; EC 3.2.1.39; 9044-93-3. Cat No: NATE-0303. | |
| Native Helix pomatia 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. Type h-1, partially purified powder, > 300 kda units/g solid; type h-5, lyophilized powder, > 400 kda units/g solid; type h-3, aqueous solution, > 90 kda units/ml; type h-3af, aqueous solution, > 60 kda units/ml; type h-2, aqueous solution, > 85 kda units/ml; type hp-2, aqueous solution, > 100 kda units/ml. Applications: Clinical testing diagnostic assay manufacturing. 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. Storage: Store at -20°C. Form: partially purified powder or Aqueous solution in ~1.0 M ammonium sulfate with 3 mM sodium azide as preservative. Source: Helix pomatia. 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-0331. | |
| Native Helix pomatia β-Mannosidase | Beta-mannosidase is an enzyme with system name beta-D-mannoside mannohydrolase. This enzyme catalyses the following chemical reaction:Hydrolysis of terminal, non-reducing beta-D-mannose residues in beta-D-mannosides. This gene encodes a member of the glycosyl hydrolase 2 family. The encoded protein localizes to the lysosome where it is the final exoglycosidase in the pathway for N-linked glycoprotein oligosaccharide catabolism. Mutations in this gene are associated with beta-mannosidosis, a lysosomal storage disease that has a wide spectrum of neurological involvement. Group: Enzymes. Synonyms: β-mannosidase; mannanase; mannase; β-D-mannosidase; β-mannoside mannohydrolase; exo-β-D-mannanase; EC 3.2.1.25; 9025-43-8. Enzyme Commission Number: EC 3.2.1.25. CAS No. 9025-43-8. β-Mannosidase. Activity: 5-30 units/mL. Storage: 2-8°C. Form: ammonium sulfate suspension. Suspension in 3.0 M (NH4)2SO4 containing 10 mM sodium acetate, pH approx. 4.0. Source: Helix pomatia. β-mannosidase; mannanase; mannase; β-D-mannosidase; β-mannoside mannohydrolase; exo-β-D-mannanase; EC 3.2.1.25; 9025-43-8. Cat No: NATE-0778. | |
| Native Helix pomatia Sulfatase | Sulfatases EC 3.1.6.1 are enzymes of the esterase class that catalyze the hydrolysis of sulfate esters. These may be found on a range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. In the latter case the resultant N-sulfates can also be termed sulfamates. Sulfatases play important roles in the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodelling sulfated glycosaminoglycans in the extracellular space. Together with sulfotransferases, sulfatases form the major catalytic machinery for the synthesis and breakage of su...n. Group: Enzymes. Synonyms: EC 3.1.6.1; 9016-17-5; sulfatase; nitrocatechol sulfatase; phenolsulfatase; phenylsulfatase; p-nitrophenyl sulfatase; arylsulfohydrolase; 4-methylumbelliferyl sulfatase; estrogen sulfatase; arylsulfatase. Enzyme Commission Number: EC 3.1.6.1. CAS No. 9016-17-5. Sulfatases. Activity: Type I, > 10 ,000 units/g solid; Type II, > 2 ,000 units/mL. Storage: -20°C. Form: Type I, powder; Type II, aqueous solution. Source: Helix pomatia. EC 3.1.6.1; 9016-17-5; sulfatase; nitrocatechol sulfatase; phenolsulfatase; phenylsulfatase; p-nitrophenyl sulfatase; arylsulfohydrolase; 4-methylumbelliferyl sulfatase; estrogen sulfatase; arylsulfatase. Cat No: NATE-0687. | |
| Native Hexokinase (ADP-Dependent) from Pyrococcus furiosus | In enzymology, a ADP-Dependent Hexokinase (EC 2.7.1.147) is an enzyme that catalyzes the chemical reaction: D-Glucose + ADP ? D-Glucose-6-phosphate + AMP. Applications: Useful for the enzymatic determination of adp. Group: Enzymes. Synonyms: ADP-dependent glucokinase; ADP-specific glucokinase; ADP:D-glucose 6-phosphotransferase; EC 2.7.1.147. Enzyme Commission Number: EC 2.7.1.147. CAS No. 173585-07-4. Hexokinase (ADP-Dependent). Mole weight: 100 kDa (gel filtration) 51 kDa (SDS-PAGE). Activity: More than 30 U/mg solid. Appearance: White amorphous powder, lyophilized. Storage: Storage at ?20°C in the presence of a desiccant is recommended. Source: Pyrococcus furiosus. ADP-dependent glucokinase; ADP-specific glucokinase; ADP:D-glucose 6-phosphotransferase; EC 2.7.1.147. Cat No: NATE-1135. | |
| Native Hexokinase (ADP-Dependent) from Thermococcus litoralis | In enzymology, a ADP-Dependent Hexokinase (EC 2.7.1.147) is an enzyme that catalyzes the chemical reaction: D-Glucose + ADP ? D-Glucose-6-phosphate + AMP. Applications: Useful for the enzymatic determination of 1,5 anhydroglucitol. Group: Enzymes. Synonyms: ADP-dependent glucokinase; ADP-specific glucokinase; ADP:D-glucose 6-phosphotransferase; EC 2.7.1.147. Enzyme Commission Number: EC 2.7.1.147. CAS No. 173585-07-4. Hexokinase (ADP-Dependent). Mole weight: 50 kDa (gel filtration) 50 kDa (SDS-PAGE). Activity: More than 25 U/mg solid. Appearance: White amorphous powder, lyophilized. Storage: Storage at ?20°C in the presence of a desiccant is recommended. Source: Thermococcus litoralis. ADP-dependent glucokinase; ADP-specific glucokinase; ADP:D-glucose 6-phosphotransferase; EC 2.7.1.147. Cat No: NATE-1136. | |
| Native Honey bee venom (Apis mellifera) Phospholipase A2 | Phospholipase A2 (PLA2) hydrolyzes the β-ester bond of zwitterionic glycerophospholipids. Preferred substrates are phosphatidylcholine, phosphatidylethanolamine, and their plasmalogen analogues. Phosphatidylinositol and phosphatidylserine are also hydrolyzed. It aggressively attacks phospholipids in membranes of intact cells. PLA2 specifically recognizes the sn-2 acyl bond of phospholipids and catalytically hydrolyzes the bond releasing arachidonic acid and lysophospholipids. Group: Enzymes. Synonyms: Phospholipases A2; EC 3.1.1.4; 9001-84-7; lecithinase A; phosphatidase; phosphatidolipase; phospholipase A; PLA2; Phosphatidylcholine 2-acylhydrolase; PLA2s. Enzyme Commission Number: EC 3.1.1.4. CAS No. 9001-84-7. PLA2. Activity: 600-2400 units/mg protein. Storage: -20°C. Form: salt-free, lyophilized powder. Source: Honey bee venom (Apis mellifera). Phospholipases A2; EC 3.1.1.4; 9001-84-7; lecithinase A; phosphatidase; phosphatidolipase; phospholipase A; PLA2; Phosphatidylcholine 2-acylhydrolase; PLA2s. Cat No: NATE-0585. | |
| Native Horse Esterase | An esterase is a hydrolase that splits esters into acids and alcohols. Group: Enzymes. Synonyms: EC 3.1.1.1; ali-esterase; B-esterase; monobutyrase; cocaine esterase; procaine esterase; methylbutyrase; vitamin A esterase; butyryl esterase; carboxyesterase; carboxylate esterase; carboxylic esterase; methylbutyRate esterase; triacetin esterase; carboxyl ester hydrolase; butyRate esterase; methylbutyrase; α-carboxylesterase; propionyl esterase; nonspecific carboxylesterase; esterase D; esterase B; esterase A; serine esterase; carboxylic acid esterase; cocaine esterase; 9016-18-6. Enzyme Commission Number: EC 3.1.1.1. CAS No. 9016-18-6. Esterase. Mole weight: Mr ~70 kDa. Activity: 0.5-1.0 units/mg. Storage: -20°C. Form: lyophilized powder; brown. Source: Horse liver. Species: Horse. EC 3.1.1.1; ali-esterase; B-esterase; monobutyrase; cocaine esterase; procaine esterase; methylbutyrase; vitamin A esterase; butyryl esterase; carboxyesterase; carboxylate esterase; carboxylic esterase; methylbutyRate esterase; triacetin esterase; carboxyl ester hydrolase; butyRate esterase; methylbutyrase; α-carboxylesterase; propionyl esterase; nonspecific carboxylesterase; esterase D; esterase B; esterase A; serine esterase; carboxylic acid esterase; cocaine esterase; 9016-18-6. Cat No: NATE-0236. | |
| Native Horseradish Apoperoxidase | Native Horseradish Apoperoxidase. Group: Enzymes. Synonyms: Apoperoxidase. Apoperoxidase. Stability: Store at -20°C (-4°F). Form: Freeze-dried powder. Source: Horseradish. Species: Horseradish. Apoperoxidase. Cat No: NATE-0880. | |
| Native Horseradish Peroxidase | The enzyme horseradish peroxidase (HRP), found in horseradish, is used extensively in molecular biology applications primarily for its ability to amplify a weak signal and increase detectability of a target molecule. HRP is often used in conjugates (molecules that have been joined genetically or chemically) to determine the presence of a molecular target. For example, an antibody conjugated to HRP may be used to detect a small amount of a specific protein in a western blot. Here, the antibody provides the specificity to locate the protein of interest and the HRP enzyme, in the presence of a substrate, produces a detectable signal. Horseradish peroxidase is also commonly used i...plant peroxidase; Japanese radish peroxidase; horseradish peroxidase (HRP); soybean peroxidase (SBP); extensin peroxidase; heme peroxidase; oxyperoxidase; protoheme peroxidase; pyrocatechol peroxidase; scopoletin peroxidase; Coprinus cinereus peroxidase; Arthromyces ramosus peroxidase. Enzyme Commission Number: EC 1.11.1.7. CAS No. 9003-99-0. Activity: > 150 units/mg. Storage: 2-8°C. Form: Freeze dried powder. Source: Horseradish. EC 1.11.1.7; HRP; peroxidase; Horseradish Peroxidase; lactoperoxidase; guaiacol peroxidase; plant peroxidase; Japanese radish peroxidase; horseradish peroxidase (HRP); soybean peroxidase (SBP); extensin peroxidase; heme peroxidase; oxyperoxidase; prot | |
| Native Horseradish Poly Peroxidase | Native Horseradish Poly Peroxidase. Part of marker enzyme portfolio. poly peroxidase is lyophilized in 10 mmol/l potassium phosphate, 50 mmol/l nacl, 1 mmol/l edta, ph 6.1and saccharose as stabilizer. enhance elisa sensitivity by using polymeric peroxidase (poly pod). Applications: Poly peroxidase (poly pod) is a marker enzyme enabling peroxidation of reduced dyes in the indicator reaction producing a color, fluorimetric or luminescent derivative of the labeled molecule for further detection and quantification. Group: Enzymes. Synonyms: Poly Peroxidase. Peroxidase. Mole weight: 800 ± 200 kDa. Activity: >600 U/mg. Stability: At -60 to -90°C within specification range for 48 months. Appearance: Red-brown lyophilizate. Source: Horseradish. Species: Horseradish. Poly Peroxidase. Cat No: NATE-0881. | |
| Native Horseradish Superoxide Dismutase | 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-). Applications: Superoxide dism...mutase and glutathione reductase, and environmental and xenobiotic stress tolerance in maize inbreds. superoxide dismutase from horseradish has also been used in a study to investigate chemiluminometric enzyme sensors for flow-injection analysis. Group: Enzymes. Synonyms: EC 1.15.1.1; 9054-89-1; SOD; Superoxide:superoxide oxidoreductase; Superoxide Dismutase. Enzyme Commission Number: EC 1.15.1.1. CAS No. 9054-89-1. SOD. Activity: 1,000-4,000 units/mg protein. Stability: -20°C. Form: Lyophilized powder containing potassium phosphate buffer salts. Source: Horseradish. EC 1.15.1.1; 9054-89-1; SOD; Superoxide:superoxide oxidoreductase; Superoxide Dismutase. Cat No: NATE-0679. | |
| Native H. pylori Urease | Ureases (EC 3.5.1.5), functionally, belong to the superfamily of amidohydrolases and phosphotriesterases. It is an enzyme that catalyzes the hydrolysis of urea into carbon dioxide and ammonia. The reaction occurs as follows: (NH2)2CO + H2O ? CO2 + 2NH3. Applications: Specific methodologies have not been tested using this product. Group: Enzymes. Synonyms: EC 3.5.1.5; Urease. Enzyme Commission Number: EC 3.5.1.5. CAS No. 9002-13-5. Purity: Sephadex G200 Purified. SDS-PAGE analysis with 30KD and 66KD. Urease. Form: Antigen Grade, Liquid. Source: H. pylori. EC 3.5.1.5; Urease. Cat No: PHAM-179. | |
| Native Human Alanine Aminotransferase | Alanine transaminase (ALT) is a transaminase enzyme (EC 2.6.1.2). It is also called alanine aminotransferase (ALAT) and was formerly called serum glutamate-pyruvate transaminase (SGPT) or serum glutamic-pyruvic transaminase (SGPT). ALT is found in plasma and in various body tissues, but is most common in the liver. It catalyzes the two parts of the alanine cycle. Serum ALT level, serum AST (aspartate transaminase) level, and their ratio (AST/ALT ratio) are commonly measured clinically as biomarkers for liver health. The tests are part of blood panels. Alanine transaminase, also commonly known as serum glutamate pyruvate transaminase is an enzyme involved in the synthesis o...oup: Enzymes. Synonyms: Alanine transaminase; ALT; EC 2.6.1.2; alanine aminotransferase; ALAT; glutamic-pyruvic transaminase; glutamic-alanine transaminase; GPT; β-alanine aminotransferase; alanine-α-ketoglutarate aminotransferase; alanine-pyruvate aminotransferase; glutamic acid-pyruvic acid transaminase; glutamic-pyruvic aminotransferase; L-alanine aminotransferase; L-alanine transaminase; L-alanine-α-ketoglutarate aminotransferase; pyruvate transaminase; pyruvate-alanine aminotransferase; pyruvate-glutamate transaminase. Enzyme Commission Number: EC 2.6.1.2. CAS No. 9000-86-6. ALT. Activity: >5 U /mg. Storage: -20°C. Source: Human Liver. Species: Human. | |
| Native Human 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. 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 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. Group: Enzymes. Synonyms: Alkaline phosphatase; ALP; ALKP; ALPase; Alk . Enzyme Commission Number: EC 3.1.3.1. CAS No. 9001-78-9. Activity: > 10 units/mg solid. Storage: -20°C. Form: Freeze dried powder. Source: Human placenta. Species: Human. Alkaline phosphatase; ALP; ALKP; ALPase; Alk Phos; EC 3.1.3.1; Alkaline phosphomonoesterase; Glycerophosphatase; Phosphomonoesterase. Cat No: NATE-0057. | |
| Native Human α-1-Antitrypsin | Alpha-1 Antitrypsin or α1-antitrypsin (A1AT) is a protease inhibitor belonging to the serpin superfamily. It is generally known as serum trypsin inhibitor. Alpha 1-antitrypsin is also referred to as alpha-1 proteinase inhibitor (A1PI) because it inhibits a wide variety of proteases. It protects tissues from enzymes of inflammatory cells, especially neutrophil elastase, and has a reference range in blood of 1.5-3.5 gram/liter (in US the reference range is generally expressed as mg/dL or micromoles), but the concentration can rise manyfold upon acute inflammation. In its absence, neutrophil elastase is free to break down elastin, which contributes to the elasticity of the lungs, resulting in respiratory complications such as emphysema, or COPD (chronic obstructive pulmonary disease) in adults and cirrhosis in adults or children. Group: Enzymes. Synonyms: Alpha-1-Antitrypsin; A1AT; α1-antitrypsin; SERPINA1; A1A; A1AT; AAT; PI; PI1; PRO2275; alpha1AT. CAS No. 9041-92-3. Purity: > 95% (SDS-PAGE). A1AT. Mole weight: 54kDa. Storage: 2-8°C. Form: Lyophilized. Source: Human Plasma. Species: Human. Alpha-1-Antitrypsin; A1AT; α1-antitrypsin; SERPINA1; A1A; A1AT; AAT; PI; PI1; PRO2275; alpha1AT. Cat No: NATE-0010. | |
| Native Human α-2 Antiplasmin | Alpha 2-antiplasmin (or α2-antiplasmin or plasmin inhibitor) is a serine protease inhibitor (serpin) responsible for inactivating plasmin, an important enzyme that participates in fibrinolysis and degradation of various other proteins. This protein is encoded by the SERPINF2 gene. Group: Enzymes. Synonyms: Alpha-2 Antiplasmin; α2-antiplasmin; plasmin inhibitor; SERPINF2; A2AP; AAP; ALPHA-2-PI; API; PLI. Purity: > 95% (SDS-PAGE). A2AP. Mole weight: 63-70 kDa. Storage: -20°C. Form: Lyophilized. Source: Human Plasma. Species: Human. Alpha-2 Antiplasmin; α2-antiplasmin; plasmin inhibitor; SERPINF2; A2AP; AAP; ALPHA-2-PI; API; PLI. Cat No: NATE-0011. | |
| Native Human α-Amylase | α-Amylase is a protein enzyme EC 3.2.1.1 that hydrolyses alpha bonds of large, alpha-linked polysaccharides, such as starch and glycogen, yielding glucose and maltose. It is the major form of amylase found in Humans and other mammals. It is also present in seeds containing starch as a food reserve, and is secreted by many fungi. Applications: Α-amylase is used to hydrolyze α bonds of α-linked polysaccharides, such as starch and glycogen. α-amylase has been used in various plant studies, such as metabolism studies in arabidopsis. α-amylase from human saliva has been used to study the development of nutraceuticals, which may aid the treatment of diabetes and obesity. Group: Enzymes. Synonyms: glycogenase; αamylase, α-amylase; 1,4-α-D-glucan glucanohydrolase; EC 3.2.1.1; 9001-19-8; endoamylase; Taka-amylase A. Enzyme Commission Number: EC 3.2.1.1. CAS No. 9001-19-8. α-Amylase. Activity: 1,000-3,000 units/mg protein; 300-1,500 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing (NH4)2SO4 and sodium Citrate. Source: Human saliva. Species: Human. glycogenase; αamylase, α-amylase; 1,4-α-D-glucan glucanohydrolase; EC 3.2.1.1; 9001-19-8; endoamylase; Taka-amylase A. Cat No: NATE-0743. | |
| Native Human α-Chymotrypsin | Chymotrypsin is a digestive enzyme component of pancreatic juice acting in the duodenum where it performs proteolysis, the breakdown of proteins and polypeptides. Chymotrypsin preferentially cleaves peptide amide bonds where the carboxyl side of the amide bond (the P1 position) is a large hydrophobic amino acid (tyrosine, tryptophan, and phenylalanine). These amino acids contain an aromatic ring in their sidechain that fits into a 'hydrophobic pocket' (the S1 position) of the enzyme. It is activated in the presence of trypsin. Applications: Human α-chymotrypsin has been used in a study to assess the quantitative structure-activity relationships for organophosphates binding to trypsin and chymotrypsin. human α-chymotrypsin has also been used in a study to investigate the direct detection of native proteins in biological matrices using extractive electrospray ionization mass spectrometry. Group: Enzymes. Synonyms: EC 3.4.21.1; α-Chy. Enzyme Commission Number: EC 3.4.21.1. CAS No. 9004-7-3. Chymotrypsin. Mole weight: mol wt 25 kDa. Storage: -20°C. Form: lyophilized powder. Source: Human pancreas. Species: Human. 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. Cat No: NATE-0747. | |
| Native Human Annexin A3 | Annexins form a family of proteins that bind phospholipids in a calcium dependent manner with repeats of 70-80 amino acid domains that are highly conserved, with the different properties being conferred by the variable N-termini. Annexin III is expressed in differentiated cells of myeloid lineage which is expressed less ubiquitously than Annexin V.Annexin III associates with cytoplasmic granules in both neutrophils and monocytes and it is suggested to be enzymatically active. It is thought to have prognostic value in a number of cancers including colorectal and upper tract urethral carcinoma. It may also play a specific role as a non-invasive marker for early detection of prostate cancer. Applications: Annexin a3 levels have been reported to be of clinical significance in prostate cancer, upper tract urethral carcinoma, colorectal cancer, breast cancer and lung adenocarcinoma. Group: Others. Synonyms: Annexin III; Annexin-3, 35-alpha calcimedin; inositol 1,2-cyclic phosphate 2-phosphohydrolase; Lipocor. Purity: >90% by SDS-polyacrylamide electrophoresis, Purified using conventional chromatography procedures. Mole weight: 36 kDa. Source: Human Neutrophils. Species: Human. Annexin III; Annexin-3, 35-alpha calcimedin; inositol 1,2-cyclic phosphate 2-phosphohydrolase; Lipocortin III; Placental anticoagulent protein III; PAP-III; Annexin A3. Cat No: NATE-1596. | |
| Native Human Antistreptolysin O | Streptolysin is a hemolysin produced by group A streptococci. In an infected individual streptolysin O acts as a protein antigen, and the patient mounts an antibody response. A rise in anti-streptolysin O level begins about 1 week after infection and peaks 2-3 weeks later. In the absence of complications or reinfection, the anti-streptolysin O ASO titer will usually fall to preinfection levels within 6-12 months. Both clinical and laboratory findings should be correlated in reaching a diagnosis. Streptococcal infections are caused by bacteria known as Streptococcus. There are several disease-causing strains of streptococci (groups A, B, C, D, and G), which are identified by t... antibody tests are useful for group A streptococci. Group A streptococci are the most virulent species for humans and are the cause of strep throat, tonsillitis, wound and skin infections, blood infections (septicemia), scarlet fever, pneumonia, rheumatic fever, Sydenham's chorea (formerly called St. Vitus' dance), and glomerulonephritis. Group: Enzymes. Synonyms: Anti-streptolysin O; ASO; ASLO. Purity: Purified. ASO. Activity: > 500 IU/mL. Stability: 2 years. Appearance: Free of hemolysis and particulates. Storage: 2-8°C. Form: Liquid; 0.2 micron filtered, 0.09% sodium azide, pH 7.0-7.2. Source: Human Plasma. Species: Human. Anti-streptolysin O; ASO; ASLO. Cat No: NATE-0948. | |
| Native Human Aspartate Aminotransferase | Aspartate Aminotransferase (AST), also known as Glutamate Oxaloacetate Transaminase (GOT), is a pyridoxal phosphate-dependant enzyme which exists in two isoenzymes; mitochondrial and cytosolic forms. The AST enzyme plays an important role in amino acid metabolism and in the urea and tricarboxylic acid cycles. In liver about 80% of the enzyme activity is mitochondrial in origin, whereas in serum the enzyme activity is largely cytosolic. In hepatic disease, serum levels are used to assess liver necrosis and for determining prognosis. In patients with acute Myocardial infarction, measurement of AST isoenzymes provides diagnostic information that differs from that obtained by determination of other marker proteins. Creative Enzymes products are not intended for use in pharmaceutical applications. Applications: Research life science elisa assay clinical chemistry. Group: Enzymes. Synonyms: EC 2.6.1.1; glutamic-oxaloacetic transaminase; glutamic-aspartic transaminase; transaminase A; AAT; AspT; 2-oxoglutaRate-glutamate aminotransferase; aspartate α-ketoglutaRate transaminase; aspartate aminotransferase; aspartate-2-oxoglutaRate transaminase; aspartic acid aminotransferas. Enzyme Commission Number: EC 2.6.1.1. CAS No. 9000-97-9. AST. Activity: >50U/ml. Storage: -20°C. Source: Human Cardiac Tissue. Species: Human. EC 2.6.1.1; glutamic-oxaloa | |
| Native Human 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: Β-n-...etylhexosaminidase; 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: 6-20 units/mg protein. Storage: 2-8°C. Form: ammonium sulfate suspension. Suspension in 2.4 M (NH4)2SO4 containing 0.15 M NaCl and 0.1 M sodium phosphate, pH 6.0. Source: Human placenta. Species: Human. 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 | |
| Native Human Butyrylcholinesterase | Butyrylcholinesterase (BChE) is a serine hydrolase that is structurally similar to acetylcholinesterase (AChE), but differs in substRate specificities and inhibitor sensitivities. BChE can, unlike AChE, efficiently hydrolyze larger esters of choline such as butyrylcholine and benzoylcholine. The enzyme is a tetrameric glycoprotein with four equal subunits (110 kDa each). The enzyme is activated by Ca2+ and Mg2+ and the activity is constant over the pH range 6.0-8.0. It is inhibited by Betaine, nicotine, organophosphates, carbamates. Applications: Butyrylcholinesterase (bche) is a serine hydrolase that shares substantial structural similarities with acetylcholinesterase (ache) but has different substrate and inhibitor specificities. bche is found in the serum, hemopoietic cells, liver, lung, heart and the central nervous system of vertebrates. Group: Enzymes. Synonyms: Butyrylcholinesterase; BCHE; BuChE; pseudocholinesterase; plasma cholinesterase; EC 3.1.1.8; 9001-08-5; Acylcholine acyl-hydrolase; Choline esterase; butyryl. Enzyme Commission Number: EC 3.1.1.8. CAS No. 9001-8-5. BCHE. Activity: > 50 U/mg protein. Source: Human serum. Species: Human. Butyrylcholinesterase; BCHE; BuChE; pseudocholinesterase; plasma cholinesterase; EC 3.1.1.8; 9001-08-5; Acylcholine acyl-hydrolase; Choline esterase; butyryl. Cat No: NATE-0093. | |
| Native Human Calpain 1 | Caplain 1 is a neutral calcium-dependent cysteine protease containing the EF-hand motif. The protease consists of two subunits; the larger subunit has four domains that are homologous with papain and calmodulin. The smaller subunit has one domain that shares homology with calmodulin. It is activated by micromolar levels of calcium and hence, it is also called as micro-calpain. Its activation leads to cellular protein degradation, neuronal cell degeneRation, and autoimmune demyelinating diseases such as multiple sclerosis. > 95% (sds-page). Applications: Human calpain 1 has been used in a study to assess how the crystal structures of human calpains 1 and 9 imply diverse mechanisms of action and auto-inhibition. human calpain 1 has also been used in a study to investigate the synthesis, biological evaluation and molecular modelling of n-heterocyclic dipeptide aldehydes as selective calpain inhibitors. Group: Enzymes. Synonyms: calpain 1, μ-calpain; calcium-activated neutral protease I; EC 3.4.22.52. Enzyme Commission Number: EC 3.4.22.52. CAS No. 78990-62-2. Calpain 1. Storage: -70°C. Form: aqueous glycerol solution. Source: Human. calpain 1, μ-calpain; calcium-activated neutral protease I; EC 3.4.22.52. Cat No: NATE-0100. | |
| Native Human Cancer Antigen 125 | Cancer Antigen 125 (CA125) is a surface antigen associated with epithelial ovarian cancer. In serum, CA125 is associated with a high molecular weight glycoprotein. Published studies have indicated that elevated serum CA125 levels can be found in individuals with serious endometroid, clear-cell and undifferentiated ovarian carcinoma. Applications: Diagnostic controls; calibrators & standards; immunoassays; clinical chemistry; testing/assay validation; life science; elisa; blotting; manufacturing; tumor markers. Group: Others. Synonyms: MUCIN 16; muc16; CA-125; Cancer Antigen 125. Purity: > 95% (SDS-PAGE). Stability: 2 years. Storage: Store at -20°C. Form: Liquid in phosphate buffered saline, pH 7.4 with sucrose. Source: Human Ascites Fluid. Species: Human. MUCIN 16; muc16; CA-125; Cancer Antigen 125; MUC16. Cat No: NATE-0952. | |
| Native Human Cancer Antigen 15-3 | Native Human Cancer Antigen 15-3. Applications: Turbid, light yellow solution. Group: Others. Synonyms: CA 15-3; Tumor Marker 15-3; Mucin-1; MUC-1; Breast carcinoma-associated antigen DF3; Breast Tumor Antigen. CA 15-3. Activity: > 5,000 IU/mL. Stability: 2 years. Storage: at -20°C. Form: Solution in 1 M sodium chloride, 1% Triton(TM) X-100, 0.05% sodium azide, pH 7.4. Source: Human Ascites Fluid. CA 15-3; Tumor Marker 15-3; Mucin-1; MUC-1; Breast carcinoma-associated antigen DF3; Breast Tumor Antigen. Cat No: NATE-1929. | |
| Native Human Cancer Antigen 19-9 | Cancer Antigen 19-9 is a tumor marker elevated in blood of patients with carcinoma of the gastro-intestinal tract. Primarily used distinguishing pancreatic cancer from pancreatitis, CA 19-9 is not sufficiently specific for use as a cancer screening test. The specificity for pancreatic cancer increases with increasing levels, high levels showing a specificity of >97% for tumor presence. CA 19-9 can be elevated in many types of gastrointestinal cancer, such as colorectal cancer, esophageal cancer and hepatocellular carcinoma. A group of mucin type glycoprotein Sialosyl Lewis Antigens (SLA), such as CA19-9 and CA19-5, have come to be recognized as circulating cancer associated a...plications: Diagnostic controls; calibrators & standards; immunoassays; testing/assay validation; life science; validation studies; manufacturing; tumor markers. Group: Others. Synonyms: Tumor Marker 19-9; CA 19-9; Cancer Antigen 19-9; carbohydrate antigen 19-9; Sialylated Lewis (a) Antigen. Purity: High Purity - Low Cross Contamination of other cancer antigens (Gel filtration & ion-exchange chromatography). Activity: Typically > 500 kU/mL. Stability: 2 years. Appearance: Clear and Colorless. Storage: Store at -20°C. Form: Liquid in phosphate buffered saline, pH 7.4 with sucrose and 0.05% sodium azide. Source: Human Liver Metastases. Species: Human. Tumor Marker 19-9; CA 19-9 | |
| Native Human Cancer Antigen 242 | CA-242 is a tumor marker for sialylated Lewis carbohydrates associated with adenocarcinomas and e-selectin mediated metastatic risk. It has been found to be an early detector of Pancreatic Cancer. Applications: Diagnostic controls; calibrators & standards; immunoassays; clinical chemistry; testing/assay validation; life science; elisa; blotting; manufacturing; tumor markers. Group: Others. Synonyms: Cancer Antigen 242; CA-242. Activity: > 25 kU/mL. Stability: 2 years. Storage: Store at -20°C. Form: Liquid in PBS, pH 7.4. Source: Human Cell Culture. Species: Human. Cancer Antigen 242; CA-242. Cat No: NATE-0955. | |
| Native Human Cancer Antigen 50 | The CA-50 tumor marker test measures the blood level of cancer antigen 50, which is a carbohydrate present on the surface of certain cancer cells and released into the blood stream where they can be detected immunologically; this test is more useful for determining the effectiveness of treatment, rather than for cancer screening. CA 50 is most prevalent in gastrointestinal cancers, but can also be associated with cancer outside the digestive tract. Applications: Diagnostic controls; calibrators & standards; immunoassays; clinical chemistry; testing/assay validation; life science; tumor markers. Group: Others. Synonyms: CA-50; Cancer Antigen 50; Serum tumor marker. Activity: > 10 kU/mL. Stability: 2 years. Storage: Store at -20°C. Form: Liquid in 0.1M PBS buffer, pH 7.4. Source: Human Cell Culture. Species: Human. CA-50; Cancer Antigen 50; Serum tumor marker. Cat No: NATE-0954. | |
| Native Human Cancer Antigen 72-4 | Elevated CA 72-4 levels in serum and plasma have been reported in various malignant diseases including carcinomas of pancreas, stomach, gallbladder, colon, ovaries, cervix and endometrium. The highest diagnostic sensitivities, according to current studies, are found for carcinomas of the gastrointestinal tract and ovaries. Although some benign diseases such as rheumatic diseases or ovary cysts may also result in elevated levels of CA 72-4, clinical studies demonstrated diagnostic specificity of more than 95% for gastrointestinal and ovarian malignancies. There is a good correlation between CA 72-4 levels and tumor stage and size. CA 72-4 is the marker of choice for the therap...dependent marker for the therapeutic monitoring and follow-up care of ovarian cancer patients, in particular in CA 125 negative patients. Applications: Diagnostic controls; calibrators & standards; immunoassays; clinical chemistry; testing/assay validation; life science; elisa; blotting; manufacturing; tumor markers. Group: Others. Synonyms: CA 72-4; Cancer Antigen 72-4. Purity: > 90% (SDS-PAGE). Activity: > 100 kU/mL. Stability: 2 years. Appearance: Clear and colorless. Storage: Store at -20°C. Form: Liquid in phosphate buffered saline, pH 7.4 with sucrose and 0.05% sodium azide. Source: Human Liver Metastases. Species: Human. CA 72-4; Cancer Antigen 72-4. Cat No: NATE-0953. | |
| Native Human Carbonic Anhydrase | Carbonic anhydrase (carbonate dehydratase) catalyzes the following reaction: CO2 + H2O ------> H2CO3 The enzyme is widespread in nature. In animals it plays an important role in respiration by facilitating the transport of carbon dioxide. In plants, carbonic anhydrases are involved in the photosynthetic fixation of CO2.Mammalian erythrocytes contain two distinct forms of carbonic anhydrase distinguished by differences in their catalytic activities. The enzyme requires zinc for its activity and it has a molecular weight of 30,000. 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. Activity: 2000 U/mg protein. Storage: Store at -20° C. Form: Freeze-dried powder. Source: Human Liver. Species: Human. 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-1678. | |
| Native Human Carbonic Anhydrase I | Carbonic anhydrase is a zinc metalloenzyme that has a molecular weight of approximately 30 kDa Da. The enzyme catalyzes the hydRation of carbon dioxide to carbonic acid. It is involved in vital processes such as pH and CO2 homeostasis, transport of bicarbonate and CO2, biosynthetic reactions, bone resorption, calcification, and tumorigenicity. Therefore, this enzyme is an important target for inhibitors with clinical applications in various pathologies such as glaucoma, epilepsy and Parkinsons disease. Applications: Carbonic anhydrase from human erythrocytes (hca) has been used to study the molten-globule state of carbonic anhydrase (ca). chaperone-like α-crystallin bi...on-small cell lung cancer. Group: Enzymes. Synonyms: Carbonic Anhydrase I; carbonate dehydRatase; carbonic anhydrase; anhydrase; carbonate anhydrase; carbonic acid anhydrase; carboxyanhydrase; carbonic anhydrase A; carbonate hydro-lyase; EC 4.2.1.1; 9001-03-0; CA-I; CA1. Enzyme Commission Number: EC 4.2.1.1. CAS No. 9001-03-0. Carbonic Anhydrase. Activity: 100-500 W-A units/mg protein. Form: powder. Source: Human erythrocytes. Species: Human. Carbonic Anhydrase I; carbonate dehydRatase; carbonic anhydrase; anhydrase; carbonate anhydrase; carbonic acid anhydrase; carboxyanhydrase; carbonic anhydrase A; carbonate hydro-lyase; EC 4.2.1.1; 9001-03-0; CA-I; CA1. Cat No: NATE-0097. | |
| Native Human Carboxypeptidase B | Carboxypeptidase B (or peptidyl-L-lysine (-L-arginine) hydrolase) catalyzes the hydrolysis of the basic amino acids, lysine, arginine, and ornithine from the C-terminal position of polypeptides. It has been shown to be a single polypeptide of 34 kDa Da. Trypsin is capable of converting native enzyme to the active enzyme, carboxypeptidase B II in vitro. The optimum pH is found to be 9.0. The enzyme may be used for sequence analysis by successive cleavage of C-terminal basic amino acids. It can also be used as a serum marker for the diagnosis of acute pancreatitis. Applications: Carboxypeptidase b from creative enzymes has been used as a reference for assaying carboxypeptidase ...ino acids, to get a distinct band for each allotype during c4 electrophoresis. Group: Enzymes. Synonyms: carboxypeptidase B; protaminase; CPB1; pancreatic carboxypeptidase B; tissue carboxypeptidase B; peptidyl-L-lysine [L-arginine]hydrolase; EC 3.4.17.2; 9025-24-5. Enzyme Commission Number: EC 3.4.17.2. CAS No. 9025-24-5. CPB1. Activity: 50-55 units/mg protein carboxypeptidase B. Storage: -20°C. Form: Solution in 0.05 M NaOAc pH 5.0 + 1.0 M NaCl + 0.01% NaN3. Source: Human pancreas. Species: Human. carboxypeptidase B; protaminase; CPB1; pancreatic carboxypeptidase B; tissue carboxypeptidase B; peptidyl-L-lysine [L-arginine]hydrolase; EC 3.4.17.2; 9025-24-5. Cat No: NATE-0151. | |
| Native Human 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. Protein determined by biuret. 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. Purity: > 90% (SDS-PAGE). CAT. Mole weight: tetramer mol wt ~250 kDa. Activity: > 30,000 units/mg protein. Storage: -20°C. Form: buffered aqueous solution. Solution in 50 mM Tris, pH 8.0. Source: Human erythrocytes. Species: Human. EC 1.11.1.6; Catalase; catalase; equilase; caperase; optidase; catalase-peroxidase; CAT; H2O2:H2O2 oxidoreductase; 9001-05-2. Cat No: NATE-0108. | |
| Native Human Cathepsin B | Cathepsin B has been found to cleave procaspase 1 and procaspase 11 and to induce apoptosis in digitonin-permeabilized cells. Translocation of cathepsin B from the cytoplasm to the nucleus contributes to bile salt induced apoptosis of rat hepatocytes. Levels of cathepsin B in PC12 cells significantly decrease 12 to 24 hours after apoptosis is induced. Group: Enzymes. Synonyms: CTSB; cathepsin B; cathepsin B1; APPS; CPSB; EC 3.4.22.1; 9047-22-7; cathepsin II; CatB. Enzyme Commission Number: EC 3.4.22.1. CAS No. 9047-22-7. Cathepsin B. Activity: > 2 ,000 units/mg protein (E1%/280). Storage: -20°C. Form: buffered aqueous solution. Solution in 50 mM sodium acetate, pH 5.0, with 1 mM EDTA. Source: Human liver. Species: Human. CTSB; cathepsin B; cathepsin B1; APPS; CPSB; EC 3.4.22.1; 9047-22-7; cathepsin II; CatB. Cat No: NATE-0168. | |
| Native Human Cathepsin 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; CLN10; CPSD; HEL-S-130P; EC 3.4.23.5; 9025-26-7. Enzyme Commission Number: EC 3.4.23.5. CAS No. 9025-26-7. CTSD. Activity: > 250 units/mg protein (E1%/280). Storage: -20°C. Form: lyophilized powder. Source: Human liver. Species: Human. CTSD; cathepsin D; CLN10; CPSD; HEL-S-130P; EC 3.4.23.5; 9025-26-7. Cat No: NATE-0172. | |
| Native Human Cathepsin G | Cathepsin G is an enzymatic protein belonging to the peptidase or protease families. In humans, it is coded by the CTSG gene. The protein encoded by this gene, a member of the peptidase S1 protein family, is found in azurophil granules of neutrophilic polymorphonuclear leukocytes. The encoded protease has a specificity similar to that of chymotrypsin C, but it is most closely related to other immune serine proteases, such as neutrophil elastase and the granzymes. Cathepsin G may participate in the killing and digestion of engulfed pathogens, and in connective tissue remodeling at sites of inflammation. It also localizes to Neutrophil extracellular traps (NETs), via its high affinity for DNA, an unusual property for serine proteases. Transcript variants utilizing alternative polyadenylation signals exist for this gene. Group: Enzymes. Synonyms: CTSG; cathepsin G; CG; CATG; EC 3.4.21.20; chymotrypsin-like proteinase; neutral proteinase. Enzyme Commission Number: EC 3.4.21.20. CAS No. 56645-49-9. Purity: > 96% (SDS-PAGE). CTSG. Activity: > 5 U/mL. Appearance: Clear, colorless solution. Storage: 2-8°C. Form: Liquid. Source: Human Neutrophils. Species: Human. CTSG; cathepsin G; CG; CATG; EC 3.4.21.20; chymotrypsin-like proteinase; neutral proteinase. Cat No: NATE-0173. | |
| Native Human Cathepsin H | Cathepsin H is a protein that in humans is encoded by the CTSH gene. The protein encoded by this gene is a lysosomal cysteine proteinase important in the overall degradation of lysosomal proteins. It is composed of a dimer of disulfide-linked heavy and light chains, both produced from a single protein precursor. The encoded protein, which belongs to the peptidase C1 protein family, can act both as an aminopeptidase and as an endopeptidase. Increased expression of this gene has been correlated with malignant progression of prostate tumors. Two transcript variants encoding different isoforms have been found for this gene. Group: Enzymes. Synonyms: CTSH; cathepsin H; CPSB; ACC-4; ACC-5; ACC4; ACC5; CPSB; minichain. Purity: > 95% (SDS-PAGE). CTSH. Mole weight: 28 kDa. Storage: -40°C. Form: Liquid. Source: Human Liver. Species: Human. CTSH; cathepsin H; CPSB; ACC-4; ACC-5; ACC4; ACC5; CPSB; minichain. Cat No: NATE-0176. | |
| Native Human Cathepsin L | Cathepsin L (EC 3.4.22.15, Aldrichina grahami cysteine proteinase) is an important lysosomal endopeptidase enzyme which is involved in the initiation of protein degradation. It is a member of the Peptidase C1 family, which play an important role in diverse processes including normal lysosome mediated protein turnover, antigen and proprotein processing, and apoptosis. Cathepsin L has been reported in many organisms including fish, birds and mammals. Applications: The most powerful of the lysosomal proteinases. it has a higher specific activity than cathepsin b and h in the degradation of a variety of physiological protein substrates. Group: Enzymes. Synonyms: cathepsin L; CTSL; EC 3.4.22.15; Aldrichina grahami cysteine proteinase; 60616-82-2. Enzyme Commission Number: EC 3.4.22.15. CAS No. 60616-82-2. CTSL. Activity: > 0.5 units/mg protein. Storage: -20°C. Form: Solution in in 20 mM malonate, pH 5.5, 1 mM EDTA, and 400 mM NaCl. Source: Human liver. Species: Human. cathepsin L; CTSL; EC 3.4.22.15; Aldrichina grahami cysteine proteinase; 60616-82-2. Cat No: NATE-0177. | |
| Native Human Cathepsin S | Cathepsin S is a lysosomal cysteine protease found primarily in the spleen and in lung macrophages. Its level is elevated in the brain tissue of those with Alzheimer's disease and Down syndrome. Cathepsin S may function in the processing of amyloid precursor protein to amyloid beta peptides. Applications: Cathepsin s from human spleen has been used in a study to assess the sequence identification, tissue distribution and polymorphism of the porcine cathepsin d (ctsd) gene. cathepsin s from human spleen has also been used in a study to investigate a new promising camptothecin analogue-polysaccharide conjugate. Group: Enzymes. Synonyms: CTSS; cathepsin S; EC 3.4.22.27; FLJ50259; MGC3886. Enzyme Commission Number: EC 3.4.22.27. CTSS. Storage: -70°C. Form: lyophilized powder. Lyophilized from 100 mM sodium acetate, pH 5.5, and 1 mM EDTA. Source: Human spleen. Species: Human. CTSS; cathepsin S; EC 3.4.22.27; FLJ50259; MGC3886. Cat No: NATE-0178. | |
| Native Human Creatine Kinase BB | Creatine Kinase BB is concentrated in the brain and lungs Because the CKBB isoenzyme, CPK-1 isoenzyme is predominately found in the brain and lungs, injury to either of these organs (for example, stroke or lung injury due to a pulmonary embolism) are associated with elevated levels of this isoenzyme. Group: Enzymes. Synonyms: CPK-1; CKBB isoenyzme; CK-BB; 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; BB-CK. Enzyme Commission Number: EC 2.7.3.2. CAS No. 9001-15-4. Purity: CK-BB: > 99%. CK-MM: < 1%. CK-MB: < 1%. Activity:> 500 U/mL. Storage: Store at -20° C. Form: Liquid, 50% Glycerol, 25 mM Imidazole, 1 mM DTE, pH 6.5. Source: Human Brain. Species: Human. CPK-1; CKBB isoenyzme; CK-BB; 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; BB-CK. Cat No: NATE-1885. | |
| Native Human Creatine Kinase MB Fraction | In the cells, the "cytosolic" CK enzymes consist of two subunits, which can be either B (brain type) or M (muscle type). There are, therefore, three different isoenzymes:CK-MM, CK-BB and CK-MB. The genes for these subunits are located on different chromosomes:B on 14q32 and M on 19q13. In addition to those three cytosolic CK isoforms, there are two mitochondrial creatine kinase isoenzymes, the ubiquitous and sarcomeric form. The functional entity of the latter two mitochondrial CK isoforms is an octamer consisting of four dimers each. Applications: The mb isoenzyme of creatine kinase (mbck) can be used as a diagnostic marker for acute myocardial infarction. Group: Enzymes. Synonyms: CK-MB; CKMB; Creatine Kinase MB Fraction; Creatine Kinase MB. Purity: > 70% (SDS-PAGE). Activity: > 1,000 U/mL. Form: liquid. Source: Human heart. Species: Human. CK-MB; CKMB; Creatine Kinase MB Fraction; Creatine Kinase MB. Cat No: NATE-0141. | |
| Native Human Creatine Kinase MB/MM Mix | 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. The molecular mass of the protein is found to be approximately 80 kDa. It is made up of 2 subunits, each having a molecular weight of 40 kDa ± 2000. The lighter subunit is present in larger amounts. Applications: Diagnostic controls, calibrators & standards; immunoassays; clinical chemistry; testing/assay validation; life science; cardiac markers; manufacturing. Group: Enzymes. Synonyms: Creatine Kinase MB/MM Mix; CK-MB/MM; ATP:creatine phosphotransferase; Creatine Kinase; CK; CPK; MM-CK; MB-CK; creatine phosphokinase; creatine phosphot. CAS No. 9001-15-4. CK. Activity: > 500 U/mL. Stability: 2 years. Storage: Store at -20°C. Form: Glycerol solution. Source: Human Heart. Species: Human. Creatine Kinase MB/MM Mix; CK-MB/MM; ATP:creatine phosphotransferase; Creatine Kinase; CK; CPK; MM-CK; MB-CK; creatine phosphokinase; creatine phosphotransferase; phosphocreatine kinase; adenosine triphosphate-creatine transphosphorylase; Mi-CK; CK-MM; CK-MB; CKMiMi; MiMi-CK; 9001-15-4. Cat No: NATE-0957. | |
| Native Human Creatine Kinase mix | 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. Applications: Research life science elisa assay clinical chemistry. Group: Enzymes. Synonyms: 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. Enzyme Commission Number: EC 2.7.3.2. CAS No. 9001-15-4. CK. Activity: >10%. Storage: -20°C. Source: Human Cardiac Tissue. Species: Human. 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-0137. | |
| Native Human Creatine Kinase MM | Human CK-MM isoenzyme also known as human CPK-3 isoenzyme is normally responsible for almost all human CPK enzyme activity in healthy people. When human (CK-MM) CKMM isoenzyme is elevated, this usually indicates injury or stress to skeletal muscle. Group: Enzymes. Synonyms: CKM; creatine kinase, muscle; CKMM; creatine kinase M-type; creatine kinase-M; creatine kinase M chain; CK-MM. Enzyme Commission Number: EC 2.7.3.2. CAS No. 9001-15-4. Purity: CK-MM: > 99% CK-MB: < 1%CK-BB: < 1%. CK. Activity:> 100 U/mg. Stability: 3 years. Appearance: White to off-white powder. Storage: Store at -20° C. Form: Lyophilized from tris chloride, EDTA and DTT, pH 7.5. Source: Human Skeletal Muscle. Species: Human. CKM; creatine kinase, muscle; CKMM; creatine kinase M-type; creatine kinase-M; creatine kinase M chain; CK-MM. Cat No: NATE-1883. | |
| Native Human Creatine Kinase MM Fraction | Creatine kinase, muscle also known as CKM is a creatine kinase that in humans is encoded by the CKM gene. In the figure to the right, the crystal structure of the muscle-type M-CK monomer is shown. In vivo, two such monomers arrange symmetrically to form the active MM-CK enzyme. In heart, in addition to the MM-CK homodimer, also the heterodimer MB-CK consisting of one muscle (M-CK) and one brain-type (B-CK) subunit is expressed. The latter may be an important serum marker for myocardial infarction, if released from damaged myocardial cells into the blood where it can be detected by clinical chemistry. Applications: May be used as a control or calibrator in monitoring myoc...stoperative cardiac medical therapy in emergency coronary artery bypass grafting for acute myocardial infarction. creatine kinase mm fraction from human heart has also been used in a study to investigate the circadian dependence of infarct size and left ventricular function after st slevation myocardial infarction. Group: Enzymes. Synonyms: CKM; creatine kinase, muscle; CKMM; creatine kinase M-type; creatine kinase-M; creatine kinase M chain; M-CK; MM-CK. Activity: > 200 U/mg. Form: lyophilized powder. Source: Human heart. Species: Human. CKM; creatine kinase, muscle; CKMM; creatine kinase M-type; creatine kinase-M; creatine kinase M chain; M-CK; MM-CK. Cat No: NATE-0142. | |
| Native Human Creatine Kinase Total | 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. The molecular mass of the protein is found to be approximately 80 kDa. It is made up of 2 subunits, each having a molecular weight of 40 kDa ± 2000. The lighter subunit is present in larger amounts. Applications: Diagnostic controls, calibrators & standards; immunoassays; clinical chemistry; testing/assay validation; life science; elisa; blotting; cardiac markers; manufacturing. Group: Enzymes. Synonyms: EC 2.7.3.2; ATP:creatine phosphotransferase; CK; CPK; MM-CK; MB-CK; BB-CK; creatine phosphokinase; creatine phosphotransferase; ph. Enzyme Commission Number: EC 2.7.3.2. CAS No. 9001-15-4. CK. Activity: > 5 U/mg. Stability: 3 years. Storage: Store at -20°C. Form: Lyophilized. Source: Human Heart/Brain. Species: Human. 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-0961. | |
| Native Human Dipeptidyl Peptidase-4 | Native DPPIV is a ubiquitous type II transmembrane glycoprotein and a serine protease of the S9 prolyl-oligopeptidase family. In vivo, it is synthesized with a signal peptide, which functions as the membrane anchoring domain. There is an 88% sequence homology between the human and porcine kidney enzymes. Both exist as homodimers with a subunit molecular weight of ~30 kDa. The high mannose 100 kDa DPPIV precursor is processed in the Golgi to yield a 124 kDa heavily N-and O-linked mature glycoprotein. It is then sorted to the apical membrane through the concerted action of both N-and O-linked glycans and its association with lipid microdomains. The porcine enzyme contains 18....Store at -20°C. Form: Liquid. Source: Human Placenta. Species: Human. EC 3.4.14.5; 54249-88-6; DPPIV; DPP4; dipeptidyl aminopeptidase IV; Xaa-Pro-dipeptidyl-aminopeptidase; Gly-Pro naphthylamidase; postproline dipeptidyl aminopeptidase IV; lymphocyte antigen CD26; glycoprotein GP110; dipeptidyl peptidase IV; glycylproline aminopeptidase; glycylproline aminopeptidase; X-prolyl dipeptidyl aminopeptidase; pep X; leukocyte antigen CD26; glycylprolyl dipeptidylaminopeptidase; dipeptidyl-peptide hydrolase; glycylprolyl aminopeptidase; dipeptidyl-aminopeptidase IV; DPP IV/CD26; amino acyl-prolyl dipeptidyl aminopeptidase; T cell triggering molecule Tp103; X-PDAP. Cat No: NATE-0962. | |
| Native Human Elastase | Neutrophil elastase is a serine proteinase in the same family as chymotrypsin and has broad substrate specificity. Secreted by neutrophils and macrophages during inflammation, it destroys bacteria and host tissue. It also localizes to Neutrophil extracellular traps (NETs), via its high affinity for DNA, an unusual property for serine proteases. Leuk ocyte elastase is a 29 kda serine endoprotease of the proteinase s1 family. it exists as a single 238 amino acid-peptide chain with four disulfide bonds. it contains two or thee n-linked glycans of variable composition which account for its three major isoforms. Applications: Elastase from creative enzymes has been used to digest fibro...mal models. Group: Enzymes. Synonyms: ELANE; elastase; EC 3.4.21.37; leukocyte elastase; ELA2; elastase 2; neutrophil elaszym; serine elastase; lysosomal elastase; neutrophil elastase; polymorphonuclear leukocyte elastase; elaszym; granulocyte elastase. Enzyme Commission Number: EC 3.4.21.37. CAS No. 9004-6-2. ELA2. Mole weight: 29 kDa. Activity: > 50 units/mg protein (Bradford). Storage: -20°C. Form: Lyophilized from 0.05 M sodium acetate (pH 5.5) and 0.6 M NaCl. Source: Human leuk ocytes. Species: Human. ELANE; elastase; EC 3.4.21.37; leukocyte elastase; ELA2; elastase 2; neutrophil elaszym; serine elastase; lysosomal elastase; neutrophil elastase; polymorphonuclear leukocyte ela | |
| Native Human Eosinophil Peroxidase | Eosinophil peroxidase is an enzyme found within the eosinophil granulocytes, innate immune cells of humans and mammals. This oxidoreductase protein is encoded by the gene EPX, expressed within these myeloid cells. EPO shares many similarities with its orthologous peroxidases, myeloperoxidase (MPO), lactoperoxidase (LPO), and thyroid peroxidase (TPO). The protein is concentrated in secretory granules within eosinophils. Eosinophil peroxidase is a heme peroxidase, its activities including the oxidation of halide ions to bacteriocidal reactive oxygen species, the cationic disruption of bacterial cell walls, and the post-translational modification of protein amino acid residues....8% (SDS-PAGE). Peroxidase. Mole weight: 77 kda (~53 kDa mw heavy chain, ~13 kDa mw light chain). Activity: > 1,000 U/mL (Enzymatic). Appearance: Clear, green to brown liquid. Storage: 2-8°C. Form: Liquid. Source: Human Eosinophils. Species: Human. EPX; eosinophil peroxidase; EPO; EPP; EPX PEN; EPX-PEN; EC 1.11.1.7; 9003-99-0; peroxidase; lactoperoxidase; guaiacol peroxidase; plant peroxidase; Japanese radish peroxidase; horseradish peroxidase (HRP); soybean peroxidase (SBP); extensin peroxidase; heme peroxidase; oxyperoxidase; protoheme peroxidase; pyrocatechol peroxidase; scopoletin peroxidase; Coprinus cinereus peroxidase; Arthromyces ramosus peroxidase. Cat No: NATE-0228. | |
| Native Human erythrocytes Acetylcholinesterase | Acetylcholinesterase, also known as AChE or acetylhydrolase, is a hydrolase that hydrolyzes the neurotransmitter acetylcholine. AChE is found at mainly neuromuscular junctions and cholinergic brain synapses, where its activity serves to terminate synaptic transmission. It belongs to carboxylesterase family of enzymes. It is the primary target of inhibition by organophosphorus compounds such as nerve agents and pesticides. The activity obtained using acetylcholine as substrate is 30-100 times that obtained with butyrylcholine, using acetylcholinesterase from electric eel. Applications: Acetylcholinesterase (ache) from creative enzymes has been used in the structure-activity study of phosphoramido acid esters as inhibitors of ache. Group: Enzymes. Synonyms: true cholinesterase; choline esterase I; cholines. Enzyme Commission Number: EC 3.1.1.7. CAS No. 9000-81-1. Acetylcholinesterase. Mole weight: ~80 kDa. Activity: > 500 units/mg protein (BCA). Storage: 2-8°C. Form: buffered aqueous solution. Solution in 20 mM HEPES, pH 8.0, containing 0.1% TRITON X-100. Source: Human erythrocytes. Species: Human. true cholinesterase; choline esterase I; cholinesterase; acetylthiocholinesterase; acetylcholine hydrolase; acetyl; β-methylcholinesterase; AcCholE; EC 3.1.1.7; 9000-81-1; Acetylcholinesterase; AChE; acetylhydrolase. Cat No: NATE-0019. | |
| Native Human Factor α-XIIa | Human Factor α-XIIa is a serine protease responsible for the activation of Factor XI to XIa in the contact activation system. Human Factor XII and prekallikrein are thought to be involved in a reciprocal activation mechanism in which Factor XIIa activates prekallikrein to kallikrein, which in turn converts Factor XII to XIIa. Factor XIIa activates Factor XI to XIa thereby triggering the Contact Factor cascade. ERL offers Factor α-XIIa which is activated by the autoactivation process with Dextran Sulfate and re-purified to remove the activator. The protein purity is determined by SDS-PAGE and activity is determined via clotting assay. Group: Enzymes. Synonyms: Human Factor Alpha-XIIa; Factor Alpha-XIIa; Factor α-XIIa. Factor α-XIIa. Mole weight: 80 kDa. Activity: 69.51 PEU/mg. Storage: < -60°C. Source: Human. Species: Human. Human Factor Alpha-XIIa; Factor Alpha-XIIa; Factor α-XIIa. Cat No: NATE-0882. | |
| Native Human Factor IXa β | Prepared from Human Factor IX by activation with Bovine Factor XIa. This Bovine Factor XIa is removed after activation. Complete activation is observed by SDS-PAGE. The Factor XIa activates Factor IX 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: Human Factor IXa Beta; Factor IXa Beta; Factor IXa. Factor IXa Beta. Mole weight: 45 kDa. Activity: 12500.00 PEU/mg. Storage: < -60°C. Source: Human. Species: Human. Human Factor IXa Beta; Factor IXa Beta; Factor IXa. Cat No: NATE-0883. | |
| Native Human Factor VIIa | Prepared from purified Human Factor VII using Human Factor XIIa. The Factor Xlla is removed using affinity chromatography. Purity is determined by SDS-PAGE. Human Factor VIIa reduces to 29,500 and 23,500 with the addition of 2-mercaptoethanol. Activity is determined via clotting assay. Factor Vlla, in the presence of calcium ions and Tissue factor, activates Factors IX and X to their enzymatically active forms, Factor IXa and Xa. Group: Enzymes. Synonyms: Human Factor VII; Factor VII. Factor VIIa. Mole weight: 50 kDa. Activity: 53833.00 PEU/mg. Storage: < -60°C. Source: Human. Species: Human. Human Factor VII; Factor VII. Cat No: NATE-0884. | |
| Native Human Factor Xa | Human Factor Xa is prepared from Human 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 along with cofactor Va, phospholipids and calcium ions, (the prothrombinase complex) catalyzes the rapid conversion of prothrombin to thrombin. Group: Enzymes. Synonyms: Human Factor Xa; Factor Xa. Factor Xa. Mole weight: 46 kDa. Activity: 218.00 IU/mg. Storage: < -60°C. Source: Human. Species: Human. Human Factor Xa; Factor Xa. Cat No: NATE-0885. | |
| Native Human Factor XIa | Prepared from Human Factor XI using Human Factor Xlla. This Xlla was removed using a corn trypsin inhibitor column. Complete activation is observed by SDS-PAGE. Factor XI, through the contact factor pathway cascade, is activated to Factor XIa via Factor Xlla and High Molecular Weight Kininogen. During activation by Factor Xlla and HK, FXI undergoes proteolytic cleavage in which the Mr=80,000 chain reportedly is cleaved to a heavy and light chain with Mr of about 48,000 and 33,000. This Factor XIa is responsible for the activation of Factor IX to Factor IXa. Unlike other examples of activation of Vitamin K-dependent blood-clotting proteins, Factor XIa proteolysis of Factor IX does not require membrane surfaces. Group: Enzymes. Synonyms: Human Factor XIa; Factor XIa. Factor XIa. Mole weight: 160 kDa. Storage: < -60°C. Source: Human. Species: Human. Human Factor XIa; Factor XIa. Cat No: NATE-0886. | |
| Native Human Factor XIIIa | Human Factor XIII is cleaved with human alpha thrombin. The thrombin is subsequently removed via chromatography. The above protein was purified from Human plasma that was tested and found negative by FDA accepted methods fro Anti-HIV1/2, Anti-HTLV I & II, HBsAg, Anti-HCV, Syphilis, ABC ab, HIV-1 p24 Ag or HIV-1 RNA, HCV RNA and HBV RNA. Donors are screened for CJD (Creutzfeldt-Jakob Disease). Group: Enzymes. Synonyms: Human Factor XIIIa; Factor XIIIa. Factor XIIIa. Mole weight: 312 kDa. Activity: 1968.00 Loewy u/mg. Storage: -20°C. Source: Human. Species: Human. Human Factor XIIIa; Factor XIIIa. Cat No: NATE-0887. | |
| Native Human 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 pathophysiology. Applications: Research life science elisa assay clinical chemistry. Group: Enzymes. Synonyms: EC 2.3.2.2; glutamyl tr. Enzyme Commission Number: EC 2.3.2.2. CAS No. 9046-27-9. γ-GT. Activity: >50 U/mg. Storage: 4°C. Source: Human Liver. Species: Human. 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-0792. | |
| Native Human 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. At the reported ph optimum of 8.8, we have found the activity to be approx. 10 times that at ph 7.0. however, to remain consistent with literature and avoid complications arising from non-enzymatic oxidation of gsh, our unit is defined at ph 7.0. 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. GSH-Px. Activity: > 30 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing 25% sucrose, 3% dithiothreitol, and sodium phosphate buffer salts. Source: Human erythr ocytes. Species: Human. 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-0323. | |
| Native Human Glutathione S-Transferase | Glutathione S-transferases are a family of proteins that catalyze the conjugation of reduced glutathione with a variety of hydrophobic chemicals containing electrophilic centers. Group: Enzymes. Synonyms: EC 2.5.1.18; glutathione S-transferase; glutathione S-alkyltransferase; glutathione S-aryltransferase; S-(hydroxyalkyl)glutathione lyase; glutathione S-aralkyltransferase; glutathione S-alkyl transferase; GST; 50812-37-8. Enzyme Commission Number: EC 2.5.1.18. CAS No. 50812-37-8. Glutathione S-Transferase. Activity: 25-125 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing Tris buffer salts, reduced glutathione and EDTA. Source: Human placenta. Species: Human. EC 2.5.1.18; glutathione S-transferase; glutathione S-alkyltransferase; glutathione S-aryltransferase; S-(hydroxyalkyl)glutathione lyase; glutathione S-aralkyltransferase; glutathione S-alkyl transferase; GST; 50812-37-8. Cat No: NATE-0326. | |
| Native Human Glyceraldehyde-3-phosphate Dehydrogenase | Glyceraldehyde-3-phosphate dehydrogenase catalyzes the conversion of glyceraldehyde-3-phosphate to 1,3-bisphosphoglycerate as part of glycolysis. It has also been shown to have roles in initiation of apoptosis, transcription activation and the shuttling of ER to Golgi vesicles. Group: Enzymes. Synonyms: EC 1.2.1.12; GAPDH; glyceraldehyde-3-phosphate dehydrogenase (phosphorylating); triosephosphate dehydrogenase; dehydrogenase, glyceraldehyde phosphate; phosphoglyceraldehyde dehydrogenase; 3-phosphoglyceraldehyde dehydrogenase; NAD+-dependent glyceraldehyde phosphate dehydrogenase; glyceralde. Enzyme Commission Number: EC 1.2.1.12. CAS No. 9001-50-7. Glyceraldehyde-3-phosphate Dehydrogenase. Activity: 50-150 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing sodium Citrate buffer salts. Source: Human erythrocytes. Species: Human. EC 1.2.1.12; GAPDH; glyceraldehyde-3-phosphate dehydrogenase (phosphorylating); triosephosphate dehydrogenase; dehydrogenase, glyceraldehyde phosphate; phosphoglyceraldehyde dehydrogenase; 3-phosphoglyceraldehyde dehydrogenase; NAD+-dependent glyceraldehyde phosphate dehydrogenase; glyceraldehyde phosphate dehydrogenase (NAD+); glyceraldehyde-3-phosphate dehydrogenase (NAD+); NADH-glyceraldehyde phosphate dehydrogenase; glyceraldehyde-3-P-dehydrogenase; 9001-50-7. Cat No: NATE-0280. | |
| Native Human Kallikrein | Plasma kallikrein is an enzyme. This enzyme catalyses the following chemical reaction:Selective cleavage of some Arg-and Lys-bonds, including Lys-Arg and Arg-Ser in (human) kininogen to release bradykinin. This enzyme is formed from plasma prokallikrein (Fletcher factor) by factor XIIa. Group: Enzymes. Synonyms: serum kallikrein; kininogenin; kallikrein I; kallikrein II; kininogenase; kallikrein; callicrein; glumorin; padreatin; padutin; kallidinogenase; bradykininogenase; panceatic kallikrein; onokrein P; dilminal D; depot-Padutin; urokallikrein; urinary kallikrein; 9001-01-8; EC 3.4.21.34; plasma kallikrein. Enzyme Commission Number: EC 3.4.21.34. CAS No. 9001-1-8. Kallikrein. Activity: Type I, > 5 units/mg protein; Type II, 1-5 units/mg protein. Storage: -20°C. Form: Type I, buffered aqueous solution, Solution in 20 mM Tris-HCl, pH 7.8 with 100 mM NaCl; Type II, lyophilized powder. Source: Human plasma. Species: Human. serum kallikrein; kininogenin; kallikrein I; kallikrein II; kininogenase; kallikrein; callicrein; glumorin; padreatin; padutin; kallidinogenase; bradykininogenase; panceatic kallikrein; onokrein P; dilminal D; depot-Padutin; urokallikrein; urinary kallikrein; 9001-01-8; EC 3.4.21.34; plasma kallikrein. Cat No: NATE-0361. | |
| Native Human Lactate Dehydrogenase | A lactate dehydrogenase (LDH or LD) is an enzyme found in nearly all living cells (animals, plants, and prokaryotes). LDH catalyzes the conversion of pyruvate to lactate and back, as it converts NADH to NAD+ and back. A dehydrogenase is an enzyme that transfers a hydride from one molecule to another. Applications: Research clinical chemistry life science. Group: Enzymes. Synonyms: EC 1.1.1.27; 9001-60-9; lactate dehydrogenase; LDH; LD; (S)-Lactate:NAD+ oxidoreductase, L-LDH; LAD; L-Lactic Dehydrogenase; lactic acid dehydrogenase; L (+)-nLDH; L-(+)-lactate dehydrogenase; L-lactic acid dehydrogenase; lactate dehydrogenase NAD-dependent; lactic dehydrogenase; NAD-lactate dehydrogenase. Enzyme Commission Number: EC 1.1.1.27. CAS No. 9001-60-9. LDH. Activity: >90%. (>200U/mL). Storage: 4°C. Source: Human Cardiac Tissue. Species: Human. EC 1.1.1.27; 9001-60-9; lactate dehydrogenase; LDH; LD; (S)-Lactate:NAD+ oxidoreductase, L-LDH; LAD; L-Lactic Dehydrogenase; lactic acid dehydrogenase; L (+)-nLDH; L-(+)-lactate dehydrogenase; L-lactic acid dehydrogenase; lactate dehydrogenase NAD-dependent; lactic dehydrogenase; NAD-lactate dehydrogenase. Cat No: NATE-0380. | |
| Native Human Lactate Dehydrogenase 1 | A lactate dehydrogenase (LDH or LD) is an enzyme found in nearly all living cells (animals, plants, and prokaryotes). LDH catalyzes the conversion of pyruvate to lactate and back, as it converts NADH to NAD+ and back. A dehydrogenase is an enzyme that transfers a hydride from one molecule to another. Applications: Research clinical chemistry life science. Group: Enzymes. Synonyms: EC 1.1.1.27; 9001-60-9; lactate dehydrogenase; LDH; LD; (S)-Lactate:NAD+ oxidoreductase, L-LDH; LAD; L-Lactic Dehydrogenase; lactic acid dehydrogenase; L (+)-nLDH; L-(+)-lactate dehydrogenase; L-lactic acid dehydrogenase; lactate dehydrogenase NAD-dependent; lactic dehydrogenase; NAD-lactate dehydrogenase. Enzyme Commission Number: EC 1.1.1.27. CAS No. 9001-60-9. LDH. Activity: >90%. (>200U/mL). Storage: 4°C. Source: Human Cardiac Tissue. Species: Human. EC 1.1.1.27; 9001-60-9; lactate dehydrogenase; LDH; LD; (S)-Lactate:NAD+ oxidoreductase, L-LDH; LAD; L-Lactic Dehydrogenase; lactic acid dehydrogenase; L (+)-nLDH; L-(+)-lactate dehydrogenase; L-lactic acid dehydrogenase; lactate dehydrogenase NAD-dependent; lactic dehydrogenase; NAD-lactate dehydrogenase. Cat No: NATE-0384. | |
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