Creative Enzymes - Products
Enzyme manufacturing for life science research and medicines, food, alcohol, fabric, paper etc. Uses include: drug discovery, cancer and infectious disease research, microbiology and personalized medicine.
| Product | Description | |
|---|---|---|
| Native Escherichia coli Penicillin Amidase | The biosynthesis of Penicillin amidase in E. coli by hydrophobic protein chromatography is an inducible reaction which is regulated by metabolized carbon source (e.g. polyols, carboxylic acid etc.). It is also influenced by catabolite repression. It catalyzes the formation of amide bonds through an acyl-enzyme intermediate. Penicillin amidase is a periplasmic 80k heterodimer with a and b chains (209 and 566 amino acids, respectively). it is widely distributed among microorganisms, including bacteria, yeast and filamentous fungi. among all the sources, the enzyme produced by e. coli is most well-characterized and common for industrial application. Applications: Penicillin...; benzylpenicillin acylase; novozym 217; semacylase; α-acylamino-β-lactam acylhydrolase; ampicillin acylase; EC 3.5.1.11; 9014-06-6. Enzyme Commission Number: EC 3.5.1.11. CAS No. 9014-6-6. Penicillin Amidase. Mole weight: Mr ~70 kDa. Activity: Type I, 5-10 units/mg protein; Type II, > 10 units/mg protein (E1%/280). Storage: 2-8°C. Form: Type II, ammonium sulfate suspension, Suspension in 0.1 M phosphate, pH 7.5 and 3 M ammonium sulfate. Source: Escherichia coli. penicillin amidase; penicillin acylase; benzylpenicillin acylase; novozym 217; semacylase; α-acylamino-β-lactam acylhydrolase; ampicillin acylase; EC 3.5.1.11; 9014-06-6. Cat No: NATE-0541. |  |
| Native Escherichia coli Superoxide Dismutase | Superoxide dismutase (SOD) catalyzes the dismutation of superoxide radicals to hydrogen peroxide and molecular oxygen. SOD plays a critical role in the defense of cells against the toxic effects of oxygen radicals. SOD competes with nitric oxide (NO) for superoxide anion (which reacts with NO to form peroxynitrite), thereby SOD promotes the activity of NO. SOD has also been shown to suppress apoptosis in cultured rat ovarian follicles, neural cell lines, and transgenic mice by preventing the conversion of NO to peroxynitrate, an inducer of apoptosis. Superoxide dismutases are a group of low molecular weight metalloproteins present in all aerobic cells of plants, animals...5.1.1; superoxidase dismutase; copper-zinc superoxide dismutase; Cu-Zn superoxide dismutase; ferrisuperoxide dismutase; superoxide dismutase I; superoxide dismutase II; SOD; Cu,Zn-SOD; Mn-SOD; Fe-SOD; SODF; SODS; SOD-1; SOD-2; SOD-3; SOD-4; hemocuprein; erythrocuprein; cytocuprein; cuprein ; hepatocuprein; 9054-89-1. Enzyme Commission Number: EC 1.15.1.1. CAS No. 9054-89-1. SOD. Mole weight: mol wt 32.5 kDa. Activity: > 1 ,000 units/mg protein. Storage: -20°C. Form: Lyophilized powder containing Tris buffer salts. Source: Escherichia coli. Superoxide dismutases; EC 1.15.1.1; superoxidase dismutase; copper-zinc superoxide dismutase; Cu-Zn superoxide dismutase; ferrisuper | |
| Native Escherichia coli Thioredoxin Reductase | Thioredoxin reductase (TrxR) is an NADPH-dependent oxidoreductase containing one FAD per subunit that reduces the active site disulfide in oxidised thioredoxin (Trx). The molecular weight of the isozymes from mammalian sources vary between 55-67 kDa as compared with 35 kDa in prokaryotes, plants or yeast. The substrate specificity of the mammalian enzyme is much broader than the prokaryotic enzyme reducing both mammalian and E. coli thioredoxins as well as well as non-disulfide substrates such selenite, lipoic acids, lipid hydroperoxides and hydrogen peroxide. Applications: Thioredoxin reductase from escherichia coli can be used in peroxidase-coupled thioredoxin system assay for assessing the peroxidase activitiy of cys-based thiol peroxidases. the product was used for determining the enzymatic activity of his6-ahp1p. Group: Enzymes. Synonyms: NADP-thioredoxi. Enzyme Commission Number: EC 1.8.1.9. CAS No. 9074-14-0. TrxR. Activity: >25 units/mg protein (Bradford). Storage: 2-8°C. Form: ammonium sulfate suspension; Suspension in 3.6 M (NH4)2SO4 containing 30 mM potassium phosphate buffer, pH 7.5, and 2 mM EDTA. Source: Escherichia coli. NADP-thioredoxin reductase; NADPH-thioredoxin reductase; thioredoxin reductase (NADPH); NADPH2:oxidized thioredoxin oxidoreductase; thioredoxin-disulfide reductase; EC 1.8.1.9; TrxR. Cat No: NATE-0718. | |
| Native Fig tree latex Ficin | Ficin is classified as a thiol protease. It contains a single reactive cysteine at its active site. The amino acid homology of the active site is similar to that of papain. Ficin will cleave proteins at the carboxyl side of Gly, Ser, Thr, Met, Lys, Arg, Tyr, Ala, Asn, and Val. The reported Km for the chromogenic substrate pGlu-Phe-Leu-p-nitroanilide is 0.43 mM. Ficin is inhibited by iodoacetamide, iodoacetic acid, N-ethylmaleimide, mercuric chloride, DFP (diisopropyl fluorophosphate), TLCK (Na-p-Tosyl-lysine chloromethyl ketone), and TPCK (N-Tosyl-L-phenylalanine chloromethyl ketone). Ficin can be used to generate high yielding F (ab')2 fragments from mouse IgG1. Group: Enzymes. Synonyms: ficin; debricin; higueroxyl delabarre; EC 3.4.22.3; 9001-33-6; ficain. Enzyme Commission Number: EC 3.4.22.3. CAS No. 9001-33-6. Ficin. Mole weight: 23.8 kDa. Activity: > 1.0 units/mg protein. Form: saline suspension or lyophilized powder. Source: Fig tree latex. ficin; debricin; higueroxyl delabarre; EC 3.4.22.3; 9001-33-6; ficain. Cat No: NATE-0255. | |
| Native Flavobacterium heparinum 2-O-Sulfatase | Hydrolyses the terminal 2-O-sulphate on the unsaturated di-and oligo-saccharides produced by the action of lyases on sulphated glycosaminoglycans. Hydrolyses the terminal 2-o-sulphate on the unsaturated di-and oligo-saccharides produced by the action of lyases on sulphated glycosaminoglycans. Applications: 2-o-sulfatase from flavobacterium heparinum has been used in a study to determine that oversulfated chondroitin sulfate is a contaminant in heparin associated with adverse clinical events. 2-o-sulfatase from flavobacterium heparinum has also been used in a study to determine the structure of oligosaccharides prepared from acharan sulfate. Group: Enzymes. Synonyms: 2-O-Sulfatase. 2-O-Sulfatase. Activity: 10-40 (units/ml). Storage: -20°C. Form: Solution contains 10 mM tris-acetate, pH 7.3, 80 mM NaCl, 10 mM potassium phosphate, 0.2% BSA. Source: Flavobacterium heparinum. 2-O-Sulfatase. Cat No: NATE-0002. | |
| Native Flavobacterium heparinum Chondroitinase AC | Chondroitinase AC from Flavobacterium heparinum is an enzyme that cleaves sulfated and non-sulfated polysaccharide chains with (1-4) linkages between hexosamines and glucuronic acid residues, by an elimination mechanism. The resulting oligosaccharide products are mainly disaccharides with unsatuRated uronic acids. Chondroitinase AC specifically degrades chondroitin sulfates A and C, but not chondroitin sulfate B (dermatan sulfate). Applications: Chondroitinase ac from creative enzymes has been used for the large scale preparation of glycosaminoglycan (gag) fractions during the study of structural and sequence motifs in dermatan sulfate. Group: Enzymes. Synonyms: EC 4.2.2.5; 9047-57-8; chondroitin AC lyase; chondroitinase; chondroitin sulfate lyase; chondroitin AC eliminase; chondroitin AC lyase; chondroitinase AC; ChnAC. Enzyme Commission Number: EC 4.2.2.5. CAS No. 9047-57-8. ChnAC. Activity: 0.5-1.5 units/mg solid (using chondroitin sulfate A as substrate, also cleaves chondroitin sulfate C). Storage: -20°C. Form: lyophilized powder. Source: Flavobacterium heparinum. EC 4.2.2.5; 9047-57-8; chondroitin AC lyase; chondroitinase; chondroitin sulfate lyase; chondroitin AC eliminase; chondroitin AC lyase; chondroitinase AC; ChnAC. Cat No: NATE-0126. | |
| Native Flavobacterium heparinum Chondroitinase B | Chondroitinase B cleaves, via an elimination mechanism, polysaccharide chains containing 1-4 linkages between hexosamines and iduronic acid residues in dermatan sulfate (chondroitin B).The reaction yields oligosaccharide products (mainly disaccharides) containing unsaturated uronic acids which can be detected by UV spectroscopy at 232 nm. Applications: Research reagent (glycobiology, preparation of oligosaccharide libraries from dermatan sulfate).determination of contents of chondrotin sulfates by hplc. Group: Enzymes. Synonyms: Chondroitinase B; EC 4.2.2.19; chondroitin B lyase; ChonB; ChnB. Enzyme Commission Number: EC 4.2.2.19. CAS No. 52227-83-5. ChonB. Mole weight: 55 kDa. Activity: >200 IU/mg (substrate: dermatan sulfate). Stability: 12 months frozen at -20°C in aqueous buffers containing sodium phosphate and sucrose 5%. Source: Flavobacterium heparinum. Chondroitinase B; EC 4.2.2.19; chondroitin B lyase; ChonB; ChnB. Cat No: NATE-1950. | |
| Native Flavobacterium heparinum Chondroitinase C | Chondroitinase C acts upon chondroitin sulfate C, releasing unsatuRated 6-sulfated disaccharides. The enzyme also acts on hyaluronic acid, producing unsatuRated nonsulfated disaccharides. The enzyme is strongly inhibited by NaCl, Fe2+, Co2+ and phosphate ions. Group: Enzymes. Synonyms: EC 4.2.2.x,; 60184-91-0; Chondroitinase C; Chondroitin C lyase. Enzyme Commission Number: EC 4.2.2.x. CAS No. 60184-91-0. Chondroitinase C. Activity: > 200 units/mg solid. Storage: -20°C. Form: lyophilized powder. Source: Flavobacterium heparinum. EC 4.2.2.x,; 60184-91-0; Chondroitinase C; Chondroitin C lyase. Cat No: NATE-0132. | |
| Native Flavobacterium heparinum Heparinase I | In enzymology, a heparin lyase (EC 4.2.2.7) is an enzyme that catalyzes the chemical reaction: Eliminative cleavage of polysaccharides containing 1,4-linked D-glucuronate or L-iduronate residues and 1,4-alpha-linked 2-sulfoamino-2-deoxy-6-sulfo-D-glucose residues to give oligosaccharides with terminal 4-deoxy-alpha-D-gluc-4-enuronosyl groups at their non-reducing ends. This enzyme belongs to the family of lyases, specifically those carbon-oxygen lyases acting on polysaccharides. Group: Enzymes. Synonyms: EC 4.2.2.7; Heparinase I; 9025-39-2; heparin eliminase; heparinase; heparin lyase. Enzyme Commission Number: EC 4.2.2.7. CAS No. 9025-39-2. Heparinase. Mole weight: mol wt 42.8 kDa. Activity: > 200 units/mg protein (enzyme + BSA). Storage: -20°C. Source: Flavobacterium heparinum. EC 4.2.2.7; Heparinase I; 9025-39-2; heparin eliminase; heparinase; heparin lyase. Cat No: NATE-0338. | |
| Native Flavobacterium heparinum Heparinase I and III Blend | Heparin-degrading lyase that recognizes heparin sulfate proteoglycan as its primary substrate. Heparinase I and III plays vital role in various biological processes: modulate cell-growth factor interactions, cell-lipoprotein interactions, neovascularization. It cleaves highly sulphated polysaccharide chains in presence of 2-O-sulfated α-L-idopyranosyluronic acid and β-D-glucopyranosyluronic acid residues of polysaccharides. Heparinase is an inducible, non-extracellular heparin-degrading enzyme. three types of heparinises are produced by flavobacterium heparinum and contains specific sequences of heparin. Applications: Heparinase i and iii may be used for the study of heparin production during fermentation and specific activity of heparinise. Group: Enzymes. Synonyms: Heparinase; Heparin lyase; Heparin eliminase; Heparin-sulfate lyase; Heparin-sulfate eliminase; Heparitin-sulfate lyase; Heparinase I; Heparinase III. Heparinase. Storage: -20°C. Source: Flavobacterium heparinum. Heparinase; Heparin lyase; Heparin eliminase; Heparin-sulfate lyase; Heparin-sulfate eliminase; Heparitin-sulfate lyase; Heparinase I; Heparinase III. Cat No: NATE-0337. | |
| Native Flavobacterium heparinum Heparinase II | Heparin-degrading lyase that recognizes heparin sulfate proteoglycan as its primary substrate. Heparinase I and III plays vital role in various biological processes: modulate cell-growth factor interactions, cell-lipoprotein interactions, neovascularization. It cleaves highly sulphated polysaccharide chains in presence of 2-O-sulfated α-L-idopyranosyluronic acid and β-D-glucopyranosyluronic acid residues of polysaccharides. Group: Enzymes. Synonyms: Heparinase; Heparin lyase II; Heparinase II; 149371-12-0. CAS No. 149371-12-0. Heparinase. Mole weight: mol wt 84.1 kDa. Activity: > 100 units/mg protein (enzyme + BSA). Form: Lyophilized powder stabilized with approx. 25% bovine serum albumin. Source: Flavobacterium heparinum. Heparinase; Heparin lyase II; Heparinase II; 149371-12-0. Cat No: NATE-0339. | |
| Native Flavobacterium heparinum Heparinase III | Heparin-degrading lyase that recognizes heparin sulfate proteoglycan as its primary substrate. In enzymology, a heparin-sulfate lyase (EC 4.2.2.8) is an enzyme that catalyzes the chemical reaction:Elimination of sulfate; appears to act on linkages between N-acetyl-D-glucosamine and uronate. Product is an unsaturated sugar. This enzyme belongs to the family of lyases, specifically those carbon-oxygen lyases acting on polysaccharides. Group: Enzymes. Synonyms: EC 4.2.2.8; Heparinase III; 37290-86-1; heparin-sulfate eliminase; heparitin-sulfate lyase; heparitinase I; heparitinase II; heparin-sulfate lyase. Enzyme Commission Number: EC 4.2.2.8. CAS No. 37290-86-1. Heparinase. Mole weight: mol wt 70.8 kDa. Activity: > 100 units/mg protein (enzyme + BSA). Storage: -20°C. Source: Flavobacterium heparinum. EC 4.2.2.8; Heparinase III; 37290-86-1; heparin-sulfate eliminase; heparitin-sulfate lyase; heparitinase I; heparitinase II; heparin-sulfate lyase. Cat No: NATE-0340. | |
| Native Flavobacterium menigosepticum Endoproteinase AspN | Endopeptidase or endoproteinase are proteolytic peptidases that break peptide bonds of nonterminal amino acids (i.e. within the molecule), in contrast to exopeptidases, which break peptide bonds from end-pieces of terminal amino acids. For this reason, endopeptidases cannot break down peptides into monomers, while exopeptidases can break down proteins into monomers. A particular case of endopeptidase is the oligopeptidase, whose substrates are oligopeptides instead of proteins. Endoproteinase aspn (flavastacin) is a zinc metalloendopeptidase which selectively cleaves peptide bonds n-terminal to aspartic acid residues. this enzyme is recommended to digest peptides with molecular weights of 5 kda or less. Applications: O digestion of proteins for proteomic analysis by mass spectrometry o protein and peptide identification. Group: Enzymes. Synonyms: Endopeptidase; endoproteinase. CAS No. 9001-92-7. Endoproteinase Asp-N. Mole weight: 40089.9 daltons. Activity: 25 μmol/min/mg. Storage: at -20°C. Form: Supplied in lyophilized form. Source: Flavobacterium menigosepticum. Endopeptidase; endoproteinase; Endoproteinase AspN; Endoproteinase Asp-N. Cat No: NATE-1274. | |
| Native Flavobacterium meningosepticum Glycerol kinase | The activity of glycerol kinase is found widely in nature. In microorganisms GK makes possible the utilization of glycerol as a carbon source. In mammals the enzyme represents a juncture of sugar and fat metabolism; The enzyme is important to the clinical chemist in the determination of glycerol. GK is also useful in the assay of glyceraldehydes and dihydroxyacetone following their quantitative reduction to glycerol with sodium borohydride. Applications: Useful for the measurement of triglyceride. Group: Enzymes. Synonyms: glycerokinase; GK; ATP: glycerol-3-phosphotransferase; glycerol kinase phosphorylating; glyceric kinase; EC 2.7.1.30. Enzyme Commission Number: EC 2.7.1.30. GK. Mole weight: 150 kDa (TSK G3000SWXL) 50 kDa (SDS-PAGE). Activity: More than 70 U/mg solid. Appearance: White to light grayish white amorphous powder, lyophilized. Storage: Storage at -20°C in the presence of a desiccant is recommended. Form: Freeze dried powder. Source: Flavobacterium meningosepticum. glycerokinase; GK; ATP: glycerol-3-phosphotransferase; glycerol kinase phosphorylating; glyceric kinase; EC 2.7.1.30. Cat No: NATE-1155. | |
| Native Flavobacterium meningosepticum PNGase F | In enzymology, a peptide-N4-(N-acetyl-beta-glucosaminyl) asparagine amidase (EC 3.5.1.52) is an enzyme that catalyzes a chemical reaction that cleaves a N4-(acetyl-beta-D-glucosaminyl)asparagine residue in which the glucosamine residue may be further glycosylated, to yield a (substituted) N-acetyl-beta-D-glucosaminylamine and a peptide containing an aspartate residue. This enzyme belongs to the family of hydrolases, specifically those acting on carbon-nitrogen bonds other than peptide bonds in linear amides. Pngase f is purified from flavobacterium meningosepticum (3) and it is free of proteases and endo f activities. the following reagents are supplied with this produ...osaminyl)asparagine amidase; EC 3.5.1.52; PNGase F; 83534-39-8. Enzyme Commission Number: EC 3.5.1.52. CAS No. 83534-39-8. PNGase F. Mole weight: 36 kDa. Activity: 500,000 units/ml. Stability: Storage Conditions: 20 mM Tris-HCl, 50 mM NaCl, 5 mM Na2EDTA, 50% Glycerol, pH 7.5 25°C Heat Inactivation: 75°C for 10 min. Storage: Store at -20°C. Source: Flavobacterium meningosepticum. glycopeptide N-glycosidase; glycopeptidase; N-oligosaccharide glycopeptidase; N-glycanase; glycopeptidase; Jack-bean glycopeptidase; PNGase A; PNGase F; glycopeptide N-glycosidase; peptide-N4-(N-acetyl-β-glucosaminyl)asparagine amidase; EC 3.5.1.52; PNGase F; 83534-39-8. Cat No: NATE-0603. | |
| Native Flavobacterium sp. Creatinase | In enzymology, a creatinase (EC 3.5.3.3) is an enzyme that catalyzes the chemical reaction:creatine + H2O<-> sarcosine + urea. Thus, the two substrates of this enzyme are creatine and H2O, whereas its two products are sarcosine and urea. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amidines. Creatinase accelerates the conversion reaction of creatine and water molecule to sarcosine and urea. It always acts in homodimer state and is induced by choline chloride. Group: Enzymes. Synonyms: Creatine amidinohydrolase; creatinase; 37340-58-2; EC 3.5.3.3. Enzyme Commission Number: EC 3.5.3.3. CAS No. 37340-58-2. Creatinase. Activity: 10-20 units/mg protein. Stability: 2-8°C. Form: lyophilized powder. Source: Flavobacterium sp. Creatine amidinohydrolase; creatinase; 37340-58-2; EC 3.5.3.3. Cat No: NATE-0161. | |
| Native Flavobacterium sp. Proline specific endopeptidase | Prolyl endopeptidase (PE) also known as prolyl oligopeptidase or post-proline cleaving enzyme is an enzyme that in humans is encoded by the PREP gene. Applications: This enzyme is useful for the determination of amino acid sequences of peptides and proteins containing proline residues. Group: Enzymes. Synonyms: EC 3.4.21.26; post-proline cleaving enzyme; proline-specific endopeptidase; post-proline endopeptidase; proline endopeptidase; endoprolylpeptidase; prolyl endopeptidase; prolyl oligopeptidase; PE. Enzyme Commission Number: EC 3.4.21.26. CAS No. 72162-84-6. PE. Mole weight: approx. 78 kDa. Activity: Grade? 5.0U/mg-solid or more. Stability: Stable at-20°C. Appearance: White amorphous powder, lyophilized. Source: Flavobacterium sp. EC 3.4.21.26; post-proline cleaving enzyme; proline-specific endopeptidase; post-proline endopeptidase; proline endopeptidase; endoprolylpeptidase; prolyl endopeptidase; prolyl oligopeptidase; PE. Cat No: DIA-213. | |
| Native Fructose-bisphosphate aldolase from Thermophillic bacteria | Fructose-bisphosphate aldolase (EC 4.1.2.13), often just aldolase, is an enzyme catalyzing a reversible reaction that splits the aldol, fructose 1,6-bisphosphate, into the triose phosphates dihydroxyacetone phosphate (DHAP) and glyceraldehyde 3-phosphate (G3P). Aldolase can also produce DHAP from other (3S,4R)-ketose 1-phosphates such as fructose 1-phosphate and sedoheptulose 1,7-bisphosphate. Gluconeogenesis and the Calvin cycle, which are anabolic pathways, use the reverse reaction. Glycolysis, a catabolic pathway, uses the forward reaction. Aldolase is divided into two classes by mechanism. Applications: Carbon bond formation between dihydroxyacetone phosphate and linear aldehydes. Group: Enzymes. Synonyms: aldolase; fructose-1,6-bisphosphate triosephosphate-lyase; Fructose-bisphosphate aldolase; fructose diphosphate aldolase; D-fructose-1,6-bisphosphate D-glyceraldehyde-3-phosphate-lyase; EC 4.1.2.13; 9024-52-6. Enzyme Commission Number: EC 4.1.2.13. CAS No. 9024-52-6. Aldolase. Storage: Store at -20°C. Form: Frozen liquid. Source: Thermophillic bacteria. aldolase; fructose-1,6-bisphosphate triosephosphate-lyase; Fructose-bisphosphate aldolase; fructose diphosphate aldolase; D-fructose-1,6-bisphosphate D-glyceraldehyde-3-phosphate-lyase; EC 4.1.2.13; 9024-52-6. Cat No: NATE-1152. | |
| Native Galactose-adapted yeast Galactose-1-phosphate Uridyltransferase | Galactose-1-phosphate uridyltransferase (GALT) facilitates the simultaneous conversion of uridine diphosphoglucose (UDP-glucose) and galactose-1-phosphate (gal-1P) to uridine diphosphogalactose (UDP-galactose) and glucose-1-phosphate. Classic Galactosemia (CG) is an inherited metabolic condition caused by deficiency of GALT activity. Group: Enzymes. Synonyms: EC 2.7.7.12; UDP-glucose-hexose-1-phosphate uridylyltransferase; uridyl transferase; hexose-1-phosphate uridylyltransferase; uridyltransferase; hexose 1-phosphate uridyltransferase; UDP-glucose:alpha-D-galactose-1-phosphate uridylyltransferase; 9016-11-9. Enzyme Commission Number: EC 2.7.7.12. CAS No. 9026-21-5. GALT. Activity: 20-60 units/mg protein (modified Warburg-Christian). Storage: -20°C. Form: lyophilized powder; Contains buffer salts as Citrate and reduced glutathione. Source: Galactose-adapted yeast. EC 2.7.7.12; UDP-glucose-hexose-1-phosphate uridylyltransferase; uridyl transferase; hexose-1-phosphate uridylyltransferase; uridyltransferase; hexose 1-phosphate uridyltransferase; UDP-glucose:alpha-D-galactose-1-phosphate uridylyltransferase; 9016-11-9. Cat No: NATE-0277. | |
| Native Galactose-adapted yeast Uridine-5'-diphosphogalactose 4-epimerase | The enzyme UDP-glucose 4-epimerase (EC 5.1.3.2), also known as UDP-galactose 4-epimerase or GALE, is a homodimeric epimerase found in bacterial, fungal, plant, and mammalian cells. This enzyme performs the final step in the Leloir pathway of galactose metabolism, catalyzing the reversible conversion of UDP-galactose to UDP-glucose. GALE tightly binds nicotinamide adenine dinucleotide (NAD+), a co-factor required for catalytic activity. Group: Enzymes. Synonyms: UDP-galactose 4-epimerase; uridine diphosphoglucose epimerase; galactowaldenase; UDPG-4-epimerase; uridine diphosphate galactose 4-epimerase; uridine diphospho-gal. Enzyme Commission Number: EC 5.1.3.2. CAS No. 9032-89-7. UDP-Glc 4-epimerase. Activity: 10-20 units/mg protein (modified Warburg-Christian). Storage: -20°C. Form: Lyophilized powder containing approx. 40% buffer salts. Source: Galactose-adapted yeast. UDP-galactose 4-epimerase; uridine diphosphoglucose epimerase; galactowaldenase; UDPG-4-epimerase; uridine diphosphate galactose 4-epimerase; uridine diphospho-galactose-4-epimerase; UDP-glucose epimerase; UDP-galactose 4-epimerase; 4-epimerase; UDPG-4-epimerase; uridine diphosphoglucose 4-epimerase; uridine diphosphate glucose 4-epimerase; UDP-D-galactose 4-epimerase; EC 5.1.3.2; UDP-glucose 4-epimerase; GALE. Pack: vial. Cat No: NATE-0275. | |
| Native Geobacillus stearothermophilus Thermolysin | Thermolysin is a thermostable neutral metalloproteinase enzyme produced by the Gram-positive bacteria Bacillus thermoproteolyticus. It requires one zinc ion for enzyme activity and four calcium ions for structural stability. Thermolysin specifically catalyzes the hydrolysis of peptide bonds containing hydrophobic amino acids. However thermolysin is also widely used for peptide bond formation through the reverse reaction of hydrolysis. Thermolysin is the most stable member of a family of metalloproteinases produced by various Bacillus species. These enzymes are also termed 'neutral' proteinases or thermolysin-like proteinases (TLPs). Suitable for cell culture. Applica... of n-terminal to phe which is preferred over the others. often used to do limited proteolysis for peptide mapping and studies of protein structure and conformational changes. Group: Enzymes. Synonyms: thermolysin; Bacillus thermoproteolyticus neutral proteinase; thermoase; thermoase Y10; TLN; EC 3.4.24.27. Enzyme Commission Number: EC 3.4.24.27. CAS No. 9073-78-3. TLN. Activity: 30-175 units/mg protein (E1%/280). Storage: -20°C. Form: lyophilized powder containing calcium and sodium acetate buffer salts. Source: Geobacillus stearothermophilus. thermolysin; Bacillus thermoproteolyticus neutral proteinase; thermoase; thermoase Y10; TLN; EC 3.4.24.27. Cat No: NATE-0704. | |
| Native Gliocladium roseum Glycerophosphocholine phosphodiesterase | In enzymology, a glycerophosphocholine phosphodiesterase (EC 3.1.4.2) is an enzyme that catalyzes the chemical reaction: sn-glycero-3-phosphocholine + H2O<-> choline + sn-glycerol 3-phosphate. Thus, the two substrates of this enzyme are sn-glycero-3-phosphocholine and H2O, whereas its two products are choline and sn-glycerol 3-phosphate. Native glycerophosphocholine phosphodiesterase (ec 3.1.4.2) was purified from gliocladium roseum. Group: Enzymes. Synonyms: glycerophosphocholine phosphodiesterase; EC 3.1.4.2; sn-glycero-3-phosphocholine glycerophosphohydrolase; glycerophosphinicocholine diesterase; glycerylphosphorylcholinediesterase; sn-glycero-3-phosphorylcholine diesterase; glycerolphosphorylcholine phospho. Enzyme Commission Number: EC 3.1.4.2. CAS No. 9025-85-8. Glycerophosphocholine phosphodiesterase. Activity: > 10.0 U/mg. Appearance: White to brownish powder. Storage: Store in tightly closed containers, desiccated, protected from light, at-20°C. Form: Freeze dried powder. Source: Gliocladium roseum. glycerophosphocholine phosphodiesterase; EC 3.1.4.2; sn-glycero-3-phosphocholine glycerophosphohydrolase; glycerophosphinicocholine diesterase; glycerylphosphorylcholinediesterase; sn-glycero-3-phosphorylcholine diesterase; glycerolphosphorylcholine phosphodiesterase; glycerophosphohydrolase. Cat No: DIA-153. | |
| Native Gluconobacter industrius D-Fructose Dehydrogenase | D-fructose dehydrogenase is a heterotrimeric membrane-bound enzyme commonly seen in various Gluconobacter sp. especially in Gluconobacter japonicus (Gluconobacter industrius). It has a molecular mass of ca. 140 kDa, consisting of subunits I (67kDa), II (51 kDa), and III (20 kDa) and catalyzes the oxidation of D-fructose to produce 5-keto-D-fructose. The enzyme is a flavoprotein-cytochrome c complex with subunits I and II covalently bound to flavin adenine dinucleotide (FAD) and heme C as prosthetic groups, respectively. Applications: D-fructose dehydrogenase is used as a biosensor to detect the presence of d-fructose. fructose dehydrogenase (fdh) is used in a numb...he bio-industry. a direct electron transfer reaction of d-fructose dehydrogenase adsorbed on a porous carbon electrode surface has been used to describe a batch-type coulometric d-fructose biosensor. Group: Enzymes. Synonyms: EC 1.1.99.11; fructose 5-dehydrogenase; D-fructose dehydrogenase; D-fructose:(acceptor) 5-oxidoreductase; 37250-85-4. Enzyme Commission Number: EC 1.1.99.11. CAS No. 37250-85-4. D-Fructose Dehydrogenase. Activity: 400-1,200 units/mg. Storage: -20°C. Form: Lyophilized powder. Source: Gluconobacter industrius. EC 1.1.99.11; fructose 5-dehydrogenase; D-fructose dehydrogenase; D-fructose:(acceptor) 5-oxidoreductase; 37250-85-4. Cat No: NATE-0184. | |
| Native Gluconobacter sp. D-Fructose Dehydrogenase | D-fructose dehydrogenase is a heterotrimeric membrane-bound enzyme commonly seen in various Gluconobacter sp. especially in Gluconobacter japonicus (Gluconobacter industrius). It has a molecular mass of ca. 140 kDa, consisting of subunits I (67kDa), II (51 kDa), and III (20 kDa) and catalyzes the oxidation of D-fructose to produce 5-keto-D-fructose. The enzyme is a flavoprotein-cytochrome c complex with subunits I and II covalently bound to flavin adenine dinucleotide (FAD) and heme C as prosthetic groups, respectively. Applications: D-fructose dehydrogenase is used as a biosensor to detect the presence of d-fructose. this enzyme is also used in a number of basic res...tic determination of d-fructose in clinical analysis. Group: Enzymes. Synonyms: EC 1.1.99.11; fructose 5-dehydrogenase; D-fructose dehydrogenase; D-fructose: (acceptor) 5-oxidoreductase; 37250-85-4. Enzyme Commission Number: EC 1.1.99.11. CAS No. 37250-85-4. D-Fructose Dehydrogenase. Mole weight: mol wt ~140 kDa. Activity: > 20 units/mg solid; 400-1,200 units/mg protein. Storage: -20°C. Form: lyophilized powder. supplied as a lyophilized powder containing approx 80% stabilizers, sugars, amino acids and BSA. Source: Gluconobacter sp. EC 1.1.99.11; fructose 5-dehydrogenase; D-fructose dehydrogenase; D-fructose: (acceptor) 5-oxidoreductase; 37250-85-4. Cat No: NATE-0185. | |
| Native Glutamate dehydrogenase (NADP+) from Yeast | 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 (NADP+); glutamic dehydrogenase; dehydrogenase; glutamate (nicotinamide adenine dinucleotide (phosphate)); glutamic acid dehydrogenase; L-glutamate dehydrogenase; L-glutamic acid dehydrogenase; NAD(P)-glutamate dehydrogenase; NAD(P)H-dependent glutamate dehydrogenase; glutamate d. Enzyme Commission Number: EC 1.4.1.4. CAS No. 9029-11-2. GLDH. Activity: > 10 U/mg protein. Storage: Below -20°C. Form: Lyophilized Powder. Source: Yeast. glutamate dehydrogenase (NADP+); glutamic dehydrogenase; dehydrogenase; glutamate (nicotinamide adenine dinucleotide (phosphate)); glutamic acid dehydrogenase; L-glutamate dehydrogenase; L-glutamic acid dehydrogenase; NAD(P)-glutamate dehydrogenase; NAD(P)H-dependent glutamate dehydrogenase; glutamate dehydrogenase (NADP); EC 1.4.1.4; GLDH. Cat No: NATE-1037. | |
| Native Glutamine Synthetase from Microorganism | Glutamine synthetase (GS) (EC 6.3.1.2) is an enzyme that plays an essential role in the metabolism of nitrogen by catalyzing the condensation of glutamate and ammonia to form glutamine: Glutamate + ATP + NH3 ? Glutamine + ADP + phosphate. Glutamine Synthetase uses ammonia produced by nitrate reduction, amino acid degradation, and photorespiration. The amide group of glutamate is a nitrogen source for the synthesis of glutamine pathway metabolites. Group: Enzymes. Synonyms: Glutamine synthetase; GS; EC 6.3.1.2; Glutamate-ammonia ligase. Enzyme Commission Number: EC 6.3.1.2. CAS No. 9023-70-5. GS. Mole weight: ca. 900 kDa. Activity: > 7 U/mg lyophilizate. Appearance: Light yellow lyophilizate. Storage: at -20°C. Source: Microorganism. Glutamine synthetase; GS; EC 6.3.1.2; Glutamate-ammonia ligase. Cat No: DIA-411. | |
| 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 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. | |
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