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| Product | Description | |
|---|---|---|
| 3-hydroxyphenylacetate 6-hydroxylase | 3-hydroxyphenylacetate 6-hydroxylase from Flavobacterium sp. is highly specific for 3-hydroxyphenylacetate and uses NADH and NADPH as electron donors with similar efficiency. Group: Enzymes. Synonyms: 3-hydroxyphenylacetate 6-monooxygenase. Enzyme Commission Number: EC 1.14.13.63. CAS No. 114705-01-0. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-0870; 3-hydroxyphenylacetate 6-hydroxylase; EC 1.14.13.63; 114705-01-0; 3-hydroxyphenylacetate 6-monooxygenase. Cat No: EXWM-0870. |  |
| 3-ketovalidoxylamine C-N-lyase | Requires Ca2+. Eliminates 4-nitroaniline from 4-nitrophenyl-3-ketovalidamine, or 4-nitrophenol from 4-nitrophenyl-α-D-3-dehydroglucoside. Involved in the degradation of the fungicide validamycin A by Flavobacterium saccharophilum. Group: Enzymes. Synonyms: 3-ketovalidoxylamine A C-N-lyase; p-nitrophenyl-3-ketovalidamine p-nitroaniline lyase; 4-nitrophenyl-3-ketovalidamine 4-nitroaniline-lyase. Enzyme Commission Number: EC 4.3.3.1. CAS No. 99889-98-2. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-5302; 3-ketovalidoxylamine C-N-lyase; EC 4.3.3.1; 99889-98-2; 3-ketovalidoxylamine A C-N-lyase; p-nitrophenyl-3-ketovalidamine p-nitroaniline lyase; 4-nitrophenyl-3-ketovalidamine 4-nitroaniline-lyase. Cat No: EXWM-5302. | |
| Chondroitinase AC from Flavobacterium heparinum, Recombinant | Chondroitinase AC from Flavobacteriun heparinum is an eliminase that degrades chondroitin sulfates A and C, but not chondroitin sulfate B. The enzyme cleaves, via an elimination mechanism, both sulfated and non-sulfated polysaccharide chains that contain (1?4)-linkages between hexosamines and glucuronic acid residues. The reaction yields oligosaccharide products, mainly disaccharides, with unsaturated uronic acids that can be detected by UV spectroscopy at 232 nm. Applications: Chondroitinase ac was shown to inhibit melanoma invasion and proliferation, endothelial proliferation, and angiogenesis. chondroitinase ac, but not chondroitinase b, has also been shown t..., and protease activities. ChnAC. Activity: >200 units/mg protein. Appearance: Powder. Storage: Store the product at -20?C. When stored properly and unopened at -20?C, the enzyme has a recommended retest date of 2 years. After reconstitution, the product may be kept at 4?C for 4 days, but it is recommended to store the solution in working aliquots at -20 ?C. Form: The enzyme is supplied as a lyophilized powder containing potassium phosphate, NaCl, and a stabilizer. Source: E. coli. Species: Flavobacterium heparinum. chondroitinase (ambiguous); chondroitin sulfate lyase; chondroitin AC eliminase; chondroitinase AC; ChnAC; 9047-57-8; EC 4.2.2.5. Cat No: NATE-1738. | |
| Chondroitinase B from Flavobacterium heparinum, Recombinant | In enzymology, a chondroitin B lyase (EC 4.2.2.19) is an enzyme that catalyzes the chemical reaction:Eliminative cleavage of dermatan sulfate containing 1,4-beta-D-hexosaminyl and 1,3-beta-D-glucurosonyl or 1,3-alpha-L-iduronosyl linkages to disaccharides containing 4-deoxy-beta-D-gluc-4-enuronosyl groups to yield a 4,5-unsaturated dermatan-sulfate disaccharide (deltaUA-GalNAc-4S). This enzyme belongs to the family of lyases, specifically those carbon-oxygen lyases acting on polysaccharides. The enzyme cleaves, via an elimination mechanism, polysaccharide chains containing 1-4 linkages between hexosamines and iduronic acid residues in dermatan sulfate (chondroit...preparation of di-and oligo-saccharides of dermatan sulfate. 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. Purity: > 90 % by reversed phase HPLC analysis. ChonB. Mole weight: 54,779 Da. Activity: > 550 IU/mg (substrate: dermatan sulfate). Stability: Expiration is 30 months from manufacturing date, frozen at -70°C in aqueous buffers containing Sodium Chloride, Sodium Phosphate and Sucrose 5%. Source: Flavobacterium heparinum. Species: Flavobacterium heparinum. Chondroitinase B; EC 4.2.2.19; chondroitin B lyase; ChonB; ChnB. Pack: vial of 5 ug. Cat No: NATE-0130. | |
| Endoglycosidase F1 from Elizabethkingia miricola, Recombinant | An Endoglycosidase is an enzyme that releases oligosaccharides from glycoproteins or glycolipids. It may also cleave polysaccharide chains between residues that are not the terminal residue, although releasing oligosaccharides from conjugated protein and lipid molecules is more common. It breaks the glycosidic bonds between two sugar monomer in the polymer. It is different from exoglycosidase that it does not do so at the terminal residue. Hence, it is used to release long carbohydrates from conjugated molecules. If an exoglycosidase were used, every monomer in the polymer would have to be removed, one by one from the chain, taking a long time. An endoglycosida...ules. if an exoglycosidase were used, every monomer in the polymer would have to be removed, one by one from the chain, taking a long time. an endoglycosidase cleaves, giving a polymeric product. Group: Enzymes. Synonyms: Endoglycosidase; Endo F1; Endo-β-N-acetylglucosaminidase F1; Endoglycosidase F1 from Chryseobacterium meningosepticum; Endoglycosidase F1 from Elizabethkingia meningoseptica; Endoglycosidase F1 from Flavobacterium meningosepticum; Endoglycosidase F1; EC 3.2.1.96; 231-791-2. Enzyme Commission Number: EC 3.2.1.96. CAS No. 231-791-2. Endo-β-N-acetylglucosaminidase. Activity: > 16 U/mg, buffered aqueous solution. Storage: 2-8°C. Form: buf | |
| FatI | One unit of the enzyme is the amount required to hydrolyze 1 μg of pUC19 DNA in 1 hour at 55°C in a total reaction volume of 50 μl. Applications: After 2-fold overdigestion with enzyme more than 90% of the dna fragments can be ligated and recut. Group: Restriction Enzymes. Purity: 100U; 500U. ↑CATG GTAC&darr. Activity: 5000u.a./ml. Appearance: 10 X SE-buffer G. Storage: -20°C. Form: Liquid. Source: An E.coli strain that carries the cloned Fat I gene from Flavobacterium aquatile NL3. Pack: 10 mM Tris-HCl (pH 7.5); 50 mM KCl; 0,1 mM EDTA; 1 mM DTT; 200 μg/ml BSA; and 50% glycerol. Cat No: ET-1108RE. | |
| Fau I | One unit of the enzyme is the amount required to hydrolyze 1 μg of Lambda DNA in 1 hour at 55°C in a total reaction volume of 50 μl. Applications: After 2-fold overdigestion with enzyme more than 90% of the dna fragments can be ligated and of these 95% can be recut. Group: Restriction Enzymes. Purity: 100U; 500U. CCCGC(N)4↑ GGGCG(N)6&darr. Activity: 2000u.a./ml. Appearance: 10 X SE-buffer B. Storage: -20°C. Form: Liquid. Source: An E.coli strain that carries the cloned Fau I gene from Flavobacterium aquatili. Pack: 10 mM Tris-HCl (pH 7.5); 50 mM NaCl; 0.1 mM EDTA; 1 mM DTT; 200 μg/ml BSA; 50% glycerol. Cat No: ET-1109RE. | |
| FauND I | One unit of the enzyme is the amount required to hydrolyze 1 μg of Lambda DNA in 1 hour at 37°C in a total reaction volume of 50 μl. Applications: After 10-fold overdigestion with enzyme 80% of the dna fragments can be ligated and recut. in the presence of 10% peg ligation is better. Group: Restriction Enzymes. Purity: 1000U; 5000U. CA↑TATG GTAT↓AC. Activity: 10000u.a./ml. Appearance: 10 X SE-buffer Y, BSA. Storage: -20°C. Form: Liquid. Source: An E.coli strain that carries the cloned FauND I gene from Flavobacterium aquatili ND. Pack: 10 mM Tris-HCl (pH 7.5); 50 mM KCl; 0,1 mM EDTA; 1mM DTT; 200 μg/ml BSA, 50% glycerol. Cat No: ET-1110RE. | |
| Fbl I | One unit of the enzyme is the amount required to hydrolyze 1 μg of Lambda DNA in 1 hour at 55°C in a total reaction volume of 50 μl. Applications: After 2-fold overdigestion with enzyme approximately 90% of the dna fragments can be ligated and recut. Group: Restriction Enzymes. Purity: 100U; 500U. GT↑MKAC CAKM↓TG. Activity: 1000-2000u.a./ml. Appearance: 10 X SE-buffer Y. Storage: -20°C. Form: Liquid. Source: An E.coli strain that carries the cloned Fbl I gene from Flavobacterium balustinum. Pack: 10 mM Tris-HCl (pH 7.5); 200 mM NaCl; 0.1 mM EDTA; 7 mM 2-mercaptoethanol; 200 μg/ml BSA, and 50% glycerol. Cat No: ET-1111RE. | |
| flavastacin | A zinc metalloendopeptidase in peptidase family M12 (astacin family), secreted by the bacterium Flavobacterium meningosepticum. The specificity is similar to that of EC 3.4.24.33, peptidyl-Asp metalloendopeptidase from Pseudomonas fragi but the two are reported to be structurally dissimilar. Group: Enzymes. Enzyme Commission Number: EC 3.4.24.76. CAS No. 167973-66-2. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4360; flavastacin; EC 3.4.24.76; 167973-66-2. Cat No: EXWM-4360. | |
| Fok I | One unit of the enzyme is the amount required to hydrolyze 1 μg of Lambda DNA in 1 hour at 37°C in a total reaction volume of 50 μl. Applications: After 2-fold overdigestion with enzyme more than 95% of the dna fragments can be ligated and recut. Group: Restriction Enzymes. Purity: 100U; 500U. GGATG(N)9↑ CCTAC(N)13&darr. Activity: 1000-2000u.a./ml. Appearance: 10 X SE-buffer Y. Storage: -20°C. Form: Liquid. Source: An E.coli strain that carries the cloned Fok I gene from Flavobacterium okeanokoites. Pack: 10 mM Tris-HCl (pH 7.5); 50 mM NaCl; 0,1 mM EDTA; 1 mM DTT; 200 μg/ml BSA; 50% glycerol. Cat No: ET-1112RE. | |
| Fsp4H I | One unit of the enzyme is the amount required to hydrolyze 1 μg of Lambda DNA in 1 hour at 37°C in a total reaction volume of 50 μl. Applications: After 5-fold overdigestion with enzyme about 5% of the dna fragments can be ligated and recut. Group: Restriction Enzymes. Purity: 200U; 1000U. GC↑NGC CGN↓CG. Activity: 3000-5000u.a./ml. Appearance: 10 X SE-buffer Y. Storage: -20°C. Form: Liquid. Source: An E.coli strain that carries the cloned Fsp4H I gene from Flavobacterium species 4H. Pack: 10 mM Tris-HCl (pH 7.5); 100 mM NaCl; 0.1 mM EDTA; 200ug/ml BSA; 1mM DTT; 50% glycerol. Cat No: ET-1114RE. | |
| Heparinase I | This enzyme selectively cleaves highly sulfated polysaccharide chains containing 1-4 linkages between N-sulfated glucaoamine and 2-O-sulfated iduronic acid. It cleaves heparin sulfate but only to a limited extent in the sulfated zone. It also cleaves the antithrombin III pentasaccharide unit in the heparin molecule. Optimum pH 7.0-7.6. Stabilised with 0.2-0.4% BSA, 0.22 μm sterile filtered and dispensed into sterile tubes/vials. Synonyms: Native Flavobacterium Heparinum Heparinase I; EC 4.2.2.7; Heparinase I; Heparin Eliminase; Heparinase; Heparin Lyase; Heparinase I From Bacteroides Eggerthii, Recombinant. Grades: 95%. CAS No. 9025-39-2. Mole weight: 42.8 kDa. |  |
| Heparinase I from Bacteroides eggerthii, Recombinant | 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. Bacteroides heparinase i cloned from bacteroides eggerthii, also called heparin lyase i, is active on heparin and the highly sulfated domains of heparan sulfate. the reaction yields oligosaccharide products containing unsaturated uroni...heparinase i has a much higher rate of cleavage for 2-o sulfated iduronic acid residues. limited digest of porcine mucosal heparin with flavobacterium heparinum heparinase i results in sulfated heparin oligosaccharides structures previously reported. limited digest of porcine mucosal heparin with the bacteroides heparinase i results in heparin oligosaccharides with a lower extent of sulfation as reported. Group: Enzymes. Synonyms: Heparinase; Heparin lyase; Heparin eliminase; Heparin-sulfate lyase; Heparin-sulfate eliminase; Heparitin-sulfate lyase; Heparinase I; Heparinase III; Heparin lyase II; Heparinase II. CAS No. 9025-39-2. Purity: > 95% determined by SDS-PAGE | |
| Heparinase I from Flavobacterium heparinum, Recombinant | 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; Heparin eliminase; Heparin-sulfate lyase; Heparin-sulfate eliminase; Heparitin-sulfate lyase; Heparinase I. Enzyme Commission Number: EC 4.2.2.7. CAS No. 9025-39-2. Heparinase. Activity: > 400 IU/mg. Stability: Expiration of heparinase I is 12 months from manufacturing date, frozen at -96 to -20 °C in PBS. Form: Solution. Source: E.coli. Species: Flavobacterium heparinum. Heparinase; Heparin lyase; Heparin eliminase; Heparin-sulfate lyase; Heparin-sulfate eliminase; Heparitin-sulfate lyase; Heparinase I. Cat No: NATE-1946. | |
| Heparinase II from Flavobacterium heparinum, Recombinant | 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. Activity: > 15 IU/mg (heparin as substrate), > 18 IU/mg (heparan sulfate as substrate). Stability: Expiration of heparinase II is 12 months from manufacturing date, frozen at -96 to -20 °C in PBS. Form: Solution. Source: E.coli. Species: Flavobacterium heparinum. Heparinase; Heparin lyase II; Heparinase II; 149371-12-0. Cat No: NATE-1947. | |
| Heparinase III | The enzyme cleaves 1-4 linkages between N-acetylated or N-sulphated glucosamine and glucuronic acid residues. It is only active towards heparan sulfate in the low sulphated zone and does not cleave heparin or low molecular weight heparins. Highly sulfated zones are resistant to it and activity towards iduronic acid is very low. Stabilised with 0.2-0.4% BSA, 0.22 μm sterile filtered and dispensed into sterile tubes/vials. Synonyms: Heparinase III from Flavobacterium heparinum; Heparin Lyase III; Heparitinase I; Heparan monosulfate lyase; Heparin sulfate eliminase; Heparin-sulfate lyase. CAS No. 37290-86-1. Mole weight: 70.8 kDa. | |
| Heparinase III from Flavobacterium heparinum, Recombinant | 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: EC 4.2.2.8; Heparinase III; 37290-86-1; heparin-sulfate eliminase; heparitin-sulfate lyase. Enzyme Commission Number: EC 4.2.2.8. CAS No. 37290-86-1. Heparinase. Activity: > 200 IU/mg (heparan sulfate as substrate). Stability: Expiration of heparinase III is 12 months from manufacturing date, frozen at -96 to -20 °C in PBS. Form: Solution. Source: E.coli. Species: Flavobacterium heparinum. EC 4.2.2.8; Heparinase III; 37290-86-1; heparin-sulfate eliminase; heparitin-sulfate lyase. Cat No: NATE-1948. | |
| 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 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 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. | |
| N-sulfoglucosamine-3-sulfatase | The enzyme from Flavobacterium heparinum also hydrolyses N-acetyl-D-glucosamine 3-O-sulfate; the mammalian enzyme acts only on the disulfated residue. Group: Enzymes. Synonyms: chondroitinsulfatase. Enzyme Commission Number: EC 3.1.6.15. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-3748; N-sulfoglucosamine-3-sulfatase; EC 3.1.6.15; chondroitinsulfatase. Cat No: EXWM-3748. | |
| PNGase F from Flavobacterium meningosepticum, Recombinant | 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, peptide n-glycosidase f, is a recombinantly expressed endoglycosidase from flavobacterium meningosepticum that cleaves the β-aspartylglucosami...cetyl-β-glucosaminyl)asparagine amidase; EC 3.5.1.52; PNGase F; 83534-39-8. CAS No. 83534-39-8. Purity: >95% by SDS-PAGE. PNGase F. Mole weight: 34,800 daltons (Apparent). Activity: >10 U/mg. Stability: 1 year. Storage: 2-8°C. Avoid multiple freeze/thaw cycles. Form: 20 mM Tris - pH 7.5, 50 mM NaCl, 0.5 mM EDTA. Source: E. coli. Species: 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-1287. | |
| 2-O-Sulphatase from Flavobacterium heparinum | The 2-O-sulphatase acts on 2-O-sulphated ?4,5-unsaturated termini of disaccharides, tetrasaccharides, etc., produced by lyase action on a glycosaminoglycan. Group: Enzymes. Synonyms: 2-O-Sulphatase; Sulphatase. Enzyme Commission Number: EC 3.1.6.-. 2-O-Sulphatase. Mole weight: 41.8 kDa. Form: The enzyme is stabilised with 0.2% BSA, 0.22 um sterile-filtered and dispensed into sterile vials. To preserve high activity, the enzyme solution is stored frozen at -60°C and is supplied world-wide as a frozen solution. Source: Flavobacterium heparinum (ATCC 13125). 2-O-Sulphatase; Sulphatase. Cat No: NATE-1943. | |
| ?-4,5-Glycuronidase from Flavobacterium heparinum | The ?-4,5-Glycuronidase acts on the non-sulphated, unsaturated termini of disaccharides, tetrasaccharides, etc., produced either directly by lyase action on a glycosaminoglycan or by the action of the 2-O-sulphatase on an unsaturated disaccharide, tetrasaccharide, etc. Group: Enzymes. Synonyms: ?-4,5-Glycuronidase; Glycuronidase. Enzyme Commission Number: EC 3.2.1-. β-Glucosidase. Storage: Store frozen at -20 or below upon receipt. Avoid repeated freezethawing. Form: The enzyme is stabilised with 0.2% BSA, 0.22 um sterile-filtered and dispensed into sterile vials. To preserve high activity, the enzyme solution is stored frozen at -60°C and is supplied world-wide as a frozen solution. Source: Flavobacterium heparinum (ATCC 13125). ?-4,5-Glycuronidase; Glycuronidase. Cat No: NATE-1942. | |
| FaeI | One unit of the enzyme is the amount required to hydrolyze 1 μg of pUC19 DNA in 1 hour at 37°C in a total reaction volume of 50 μl. Applications: After 3-fold overdigestion with enzyme more then 90% of the dna fragments can be ligated with t4 dna ligase at 16°c and recut. Group: Restriction Enzymes. Purity: 500 U; 2500U. CATG↑ ↓GTAC. Activity: 500-2000 u.a./ml. Appearance: 10 X SE-buffer FaeI, BSA. Storage: -20°C. Form: Liquid. Source: Flavobacterium aquatile N3. Pack: 10 mM Tris-HCl (pH 7.5); 50 mM KCl; 0,1 mM EDTA; 7 mM 2-mercaptoethanol; 200 μg/ml BSA; 50% glycerol. Cat No: ET-1105RE. | |
| FaiI | One unit is defined as the amount of enzyme required to cleave 1 pmol of the double-stranded oligonucleotide of the above indicated structure in 1 hour at 50°C in a total reaction volume of 20 μl. Applications: After 3-fold overdigestion with enzyme about 90% of the puc19 dna fragments can be ligated with dna ligase and recut. Group: Restriction Enzymes. Purity: 100U; 500U. YA↑TR RT↓AY. Activity: 2000u.a./ml. Appearance: 10 X SE-buffer B. Storage: -20°C. Form: Liquid. Source: Flavobacterium aquatile B15. Pack: 10 mM Tris-HCl (pH 7.5); 100 mM KCl; 0,1 mM EDTA; 7 mM 2-mercaptoethanol; 200 μg/ml BSA; 50% glycerol. Cat No: ET-1106RE. | |
| FalI | One unit of the enzyme is the amount required to hydrolyze 1 μg of Lambda DNA in 1 hour at 37°C in a total reaction volume of 50 μl. Applications: After 3-fold overdigestion with enzyme 20% of the dna fragments can be ligated and of these 80% can be recut. in the presence of 10%peg ligation is better. Group: Restriction Enzymes. Purity: 100U; 500U. ↑(N)8AAGNNNNNCTT(N)13↑ ↓(N)13TTCNNNNNGAA(N)8&darr. Activity: 1000-3000u.a./ml. Appearance: 10 X SE-buffer W, SAM. Storage: -20°C. Form: Liquid. Source: Flavobacterium aquatile Ob10. Pack: 10 mM Tris-HCl (pH 7.5); 250 mM NaCl; 0,1 mM EDTA; 7 mM 2-mercaptoethanol; 200 μg/ml BSA; 50% glycerol. Cat No: ET-1107RE. | |
| FriO I | One unit of the enzyme is the amount required to hydrolyze 1 μg of Lambda DNA in 1 hour at 37°C in a total reaction volume of 50 μl. Applications: After 20-fold overdigestion with enzyme more than 90% of the dna fragments can be ligated and recut. Group: Restriction Enzymes. Purity: 1000U; 5000U. GRGCY↑C C↓YCGRG. Activity: 20000u.a./ml. Appearance: 10 X SE-buffer Y, BSA. Storage: -20°C. Form: Liquid. Source: Flavobacterium rigense O. Pack: 10 mM Tris-HCl (pH 7.5); 200 mM KCl; 0.1 mM EDTA; 200 μg/ml BSA; 7 mM 2-mercaptoethanol; 50% glycerol. Cat No: ET-1113RE. | |
| glutamate carboxypeptidase | A zinc enzyme produced by pseudomonads, Flavobacterium sp. and Acinetobacter sp. Its ability to hydrolyse pteroyl-L-glutamate (folic acid) has led to its use as a folate-depleting, antitumour agent. Type example of peptidase family M20. Group: Enzymes. Synonyms: carboxypeptidase G; carboxypeptidase G1; carboxypeptidase G2; glutamyl carboxypeptidase; N-pteroyl-L-glutamate hydrolase. Enzyme Commission Number: EC 3.4.17.11. CAS No. 9074-87-7. Carboxypeptidase G. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4063; glutamate carboxypeptidase; EC 3.4.17.11; 9074-87-7; carboxypeptidase G; carboxypeptidase G1; carboxypeptidase G2; glutamyl carboxypeptidase; N-pteroyl-L-glutamate hydrolase. Cat No: EXWM-4063. | |
| Heparinase II from Flavobacterium heparinum | This enzyme cleaves most links in heparin and heparin sulfate. It is relatively non-specific for 1-4 links in sulfated polysaccharide chains between hexosamines and glucuronic acid plus iduronic acids, but does not fully depolymerise either. Optimum pH 7.0-7.6. Stabilised with 0.2-0.4% BSA, 0.22 μm sterile filtered and dispensed into sterile tubes/vials. Synonyms: Heparinase II; Heparin lyase II; EC 4.2.2.8. CAS No. 149371-12-0. Mole weight: 84.1 kDa. | |
| 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 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 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. | |
| prolyl oligopeptidase | Found in vertebrates, plants and Flavobacterium. Generally cytosolic, commonly activated by thiol compounds. Type example of peptidase family S9. Group: Enzymes. Synonyms: post-proline cleaving enzyme; proline-specific endopeptidase; post-proline endopeptidase; proline endopeptidase; endoprolylpeptidase; prolyl endopeptidase. Enzyme Commission Number: EC 3.4.21.26. CAS No. 72162-84-6. PE. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4124; prolyl oligopeptidase; EC 3.4.21.26; 72162-84-6; post-proline cleaving enzyme; proline-specific endopeptidase; post-proline endopeptidase; proline endopeptidase; endoprolylpeptidase; prolyl endopeptidase. Cat No: EXWM-4124. | |
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