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| Product | Description | |
|---|---|---|
| Endoproteinase Asp-N | Endoproteinase Asp-N (Asp-N) is a metalloprotease that can specifically cleave the N-terminal side of aspartyl and cysteic acid residues [1]. Uses: Scientific research. Group: Signaling pathways. Alternative Names: Asp-N. CAS No. 55576-49-3. Pack Sizes: 2 μg. Product ID: HY-E70196. |  |
| Endoproteinase Glu-C | Endoproteinase GluC (V8 protease) is a serine proteinase. Endoproteinase GluC is able to hydrolyze some serpins and all classes of mammalian immunoglobulins [1]. Uses: Scientific research. Group: Signaling pathways. Alternative Names: V8 protease; Glu-C. CAS No. 137010-42-5. Pack Sizes: 100 μg. Product ID: HY-E70194. | |
| Endoproteinase GluC from Staphylococcus aureus, Recombinant | Protease S. aureus V8 (Endoproteinase-Glu-C) specifically cleaves peptide bonds on the COOH-terminal side of either aspartic or glutamic acids. In the presence of ammonium, the enzyme specificity is limited to glutamic sites. It has a molecular weight of 27 kDa daltons and optimum pH's of 4.0 and 7.8 with hemoglobin as the substrate. Protease S. aureus V8 is inhibited by diisopropylfluorophosphate and monovalent anions such as F-, Cl-, CH3COO-and NO3. Enzyme activity is determined by the casein digestion assay described by Drapeau. Endoproteinase gluc (staphylococcus aureus protease v8) is a serine proteinase which selectively cleaves peptide bonds c-terminal to...tide identification. Group: Enzymes. Synonyms: EC 3.4.21.19; Staph aureus V8 Protease; Protease, Staph aureus (Endoproteinase Glu-C); Glutamyl endopeptidase; V8 proteinase, endoproteinase Glu-C; staphylococcal serine proteinase. CAS No. 66676-43-5. V8 Protease. Mole weight: 29849 daltons. Activity: 38.3 μmol/min/mg. Storage: at -20°C. Form: Supplied freeze-dried from a Tris-HCl and sodium chloride buffer. Source: Bacillus subtilis. Species: Staphylococcus aureus. EC 3.4.21.19; Staph aureus V8 Protease; Protease, Staph aureus (Endoproteinase Glu-C); Glutamyl endopeptidase; V8 proteinase, endoproteinase Glu-C; staphylococcal serine proteinase. Cat No: NATE-1270. |  |
| Endoproteinase Lys-C | Endoproteinase Lys-C is a protease that cleaves proteins on the C-terminal side of lysine residues and is commonly used for protein sequencing [1]. Uses: Scientific research. Group: Signaling pathways. CAS No. 72561-05-8. Pack Sizes: 50 mg; 100 mg; 250 mg; 1 mg; 5 mg; 10 mg. Product ID: HY-P3208. | |
| Immobilized Endoproteinase Glu-C on F7m | Endoproteinase Glu-C hydrolyzes peptide and ester linkages specifically at the carboxyl end of glutamic acid (-Glu/-X; in ammonium carbonate pH 7. 8, or ammonium acetate pH 4. 0, buffer A) or of glutamic and aspartic acid (-Glu/-X and -Asp/-X; in phosphate buffer pH 7. 8, buffer B). F7m: 1. 0 mg endoproteinase Glu-C immobilized on matrix F7m per CR-column. 900 units immobilized per CR-column. Nr. 7 Storage buffer: 50 mM Tris/HCl at pH 7. 5, 5 mM EDTA. Nr. 31 Reaction buffer A: 25 mM ammonium acetate, pH 4. 0 (see above)Nr. 32 Washing buffer A: 25 mM ammonium acetate, pH 4. 0, 1 M NaClNr. 62 Reaction buffer B: 50 mM phosphate buffer, pH 7. 8 (see above)Nr. 63 Washing buffer B: 50 mM phosphate buffer, pH 7. 8, 1 M NaCl. Group: Enzymes. Synonyms: EC 3. 4. 21. 19; Staph aureus V8 Protease; Protease, Staph aureus (Endoproteinase Glu-C); Glutamyl endopeptidase; V8 proteinase, endoproteinase Glu-C; staphylococcal serine proteinase. Enzyme Commission Number: EC 3. 4. 21. 19. Storage: 4 °C. Source: Staphylococcus aureus. EC 3. 4. 21. 19; Staph aureus V8 Protease; Protease, Staph aureus (Endoproteinase Glu-C); Glutamyl endopeptidase; V8 proteinase, endoproteinase Glu-C; staphylococcal serine proteinase; Immobilized Endoproteinase Glu-C. Cat No: NATE-1763. | |
| Immobilized Endoproteinase Glu-C on G3m | Endoproteinase Glu-C hydrolyzes peptide and ester linkages specifically at the carboxyl end of glutamic acid (-Glu/-X; in ammonium carbonate pH 7. 8, or ammonium acetate pH 4. 0, buffer A) or of glutamic and aspartic acid (-Glu/-X and -Asp/-X; in phosphate buffer pH 7. 8, buffer B). G3m: 25 ug (22 units) endoproteinase Glu-C per CR-column immobilized on dextran. This CR-column cuts at least 12 ug tubulin or 5 ug BSA per application in phosphate buffer. Nr. 7 Storage buffer: 50 mM Tris/HCl at pH 7. 5, 5 mM EDTA. Nr. 31 Reaction buffer: 25 mM NH4-acetate, pH 4. 0 (see above)Nr. 32 Washing buffer: 25 mM NH4-acetate, pH 4. 0, 1 M NaClNr. 62 Reaction buffer: 50 mM phosphate buffer, pH 7. 8 (see above)Nr. 63 Washing buffer: 50 mM phosphate buffer, pH 7. 8, 1 M NaCl. Group: Enzymes. Synonyms: EC 3. 4. 21. 19; Staph aureus V8 Protease; Protease, Staph aureus (Endoproteinase Glu-C); Glutamyl endopeptidase; V8 proteinase, endoproteinase Glu-C; staphylococcal serine proteinase. Enzyme Commission Number: EC 3. 4. 21. 19. Storage: 4 °C. Source: Staphylococcus aureus. EC 3. 4. 21. 19; Staph aureus V8 Protease; Protease, Staph aureus (Endoproteinase Glu-C); Glutamyl endopeptidase; V8 proteinase, endoproteinase Glu-C; staphylococcal serine proteinase; Immobilized Endoproteinase Glu-C. Cat No: NATE-1764. | |
| 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 Lysobacter enzymogenes Endoproteinase Lys-C | Endoproteinase Lys-C inactivates the enzyme inositol monophosphatase by cleaving it at a single site directly after Lys 36. Endoproteinase lys-c is an enzyme that preferentially cleaves at the carboxyl side of lysine residues. Applications: Endoproteinase lys-c from lysobacter enzymogenes is useful in the determination of primary structures of proteins. it has been used in a study to investigate the evidence for trisulfide bonds in a recombinant variant of a human igg2 mon oclonal antibody. endoproteinase lys-c has been used for the digestion mon oclonal antibodies for disulfide bond assignment. Group: Enzymes. Synonyms: EC 3.4.21.50; chromobacter proteinase I; Achromobacter lyticus alkaline proteinase I; protease I; achromopeptidase; lysyl bond specific proteinase; 72561-05-8; Achromobacter proteinase I; Endoproteinase Lys-C. Enzyme Commission Number: EC 3.4.21.50. CAS No. 72561-05-8. Achromopeptidase. Storage: 2-8°C. Form: lyophilized powder. Source: Lysobacter enzymogenes. EC 3.4.21.50; chromobacter proteinase I; Achromobacter lyticus alkaline proteinase I; protease I; achromopeptidase; lysyl bond specific proteinase; 72561-05-8; Achromobacter proteinase I; Endoproteinase Lys-C. Cat No: NATE-0220. | |
| Native Mouse Endoproteinase Arg-C | 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 endoglycosidase cleaves, giving a polymeric product. Group: Enzymes. Synonyms: EC 3.4.21.35; glandular kallikrein; pancreatic kallikrein; submandibular. Enzyme Commission Number: EC 3.4.21.35. CAS No. 82047-85-6. Kallikrein. Storage: -20°C. Form: lyophilized powder. Source: Mouse submaxillary gland. Species: Mouse. EC 3.4.21.35; glandular kallikrein; pancreatic kallikrein; submandibular kallikrein; submaxillary kallikrein; kidney kallikrein; urinary kallikrein; kallikrein; salivary kallikrein; kininogenin; kininogenase; callicrein; glumorin; padreatin; padutin; kallidinogenase; bradykininogenase; depot-padutin; urokallikrein; dilminal D; onokrein P; 82047-85-6. Pack: vial of 5 μg. Cat No: NATE-0218. | |
| Native Pseudomonas fragi mutant strain Endoproteinase Asp-N | Peptidyl-Asp metalloendopeptidase (EC 3.4.24.33, endoproteinase Asp-N, peptidyl-Asp metalloproteinase) is an enzyme. This enzyme catalyses the following chemical reaction:Cleavage of Xaa-Asp, Xaa-Glu and Xaa-cysteic acid bonds. This metalloenzyme is isolated from Pseudomonas fragi. Group: Enzymes. Synonyms: endoproteinase Asp-N; peptidyl-Asp metalloproteinase; EC 3.4.24.33; 9001-92-7; peptidyl-Asp metalloendopeptidase. Enzyme Commission Number: EC 3.4.24.33. CAS No. 9001-92-7. Endoproteinase Asp-N. Storage: 2-8°C. Form: lyophilized powder. Source: Pseudomonas fragi mutant strain. endoproteinase Asp-N; peptidyl-Asp metalloproteinase; EC 3.4.24.33; 9001-92-7; peptidyl-Asp metalloendopeptidase. Pack: vial of 2 μg. Cat No: NATE-0222. | |
| Native Staph aureus V8 Protease (Endoproteinase Glu-C) | Protease S. aureus V8 (Endoproteinase-Glu-C) specifically cleaves peptide bonds on the COOH-terminal side of either aspartic or glutamic acids. In the presence of ammonium, the enzyme specificity is limited to glutamic sites. It has a molecular weight of 27 kDa daltons and optimum pH's of 4.0 and 7.8 with hemoglobin as the substrate. Protease S. aureus V8 is inhibited by diisopropylfluorophosphate and monovalent anions such as F-, Cl-, CH3COO-and NO3. Enzyme activity is determined by the casein digestion assay described by Drapeau. Protease s. aureus v8 (endoproteinase-glu-c) specifically cleaves peptide bonds on the cooh-terminal side of either aspartic or glutamic acids. Group: Enzymes. Synonyms: EC 3.4.21.19; Staph aureus V8 Protease; Prot. Enzyme Commission Number: EC 3.4.21.19. CAS No. 137010-42-5. Purity: Chromatographically purified. V8 Protease. Mole weight: 27 kDa (Drapeau 1978). Activity: > 500 units per mg dry weight. Stability: Autolysis occurs at temperatures > 40°C. The enzyme is fully active in USP 0.2% SDS. Stable for 12 months at 2-8°C. Storage: Store at 2-8°C. Form: Lyophilized powder. Source: Staph aureus V8. EC 3.4.21.19; Staph aureus V8 Protease; Protease, Staph aureus (Endoproteinase Glu-C); Glutamyl endopeptidase; V8 proteinase, endoproteinase Glu-C; staphylococcal serine proteinase. Cat No: NATE-0730. | |
| glutamyl endopeptidase | From Staphylococcus aureus strain V8. In appropriate buffer the specificity is restricted to Glu?. In peptidase family S1 (trypsin family). Group: Enzymes. Synonyms: V8 proteinase; endoproteinase Glu-C; staphylococcal serine proteinase. Enzyme Commission Number: EC 3.4.21.19. CAS No. 137010-42-5. V8 Protease. 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-4118; glutamyl endopeptidase; EC 3.4.21.19; 137010-42-5; V8 proteinase; endoproteinase Glu-C; staphylococcal serine proteinase. Cat No: EXWM-4118. | |
| kexin | A Ca2+-activated peptidase of peptidase family S8, containing Cys near the active site His, and inhibited by p-mercuribenzoate. Similar enzymes occur in mammals. Group: Enzymes. Synonyms: yeast KEX2 protease; proteinase yscF; prohormone-processing endoprotease; paired-basic endopeptidase; yeast cysteine proteinase F (misleading); paired-basic endopeptidase; andrenorphin-Gly-generating enzyme; endoproteinase Kex2p; gene KEX2 dibasic proteinase; Kex 2p proteinase; Kex2 endopeptidase; Kex2 endoprotease; Kex2 endoproteinase; Kex2 protease; proteinase Kex2p; Kex. Enzyme Commission Number: EC 3.4.21.61. CAS No. 99676-46-7. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4152; kexin; EC 3.4.21.61; 99676-46-7; yeast KEX2 protease; proteinase yscF; prohormone-processing endoprotease; paired-basic endopeptidase; yeast cysteine proteinase F (misleading); paired-basic endopeptidase; andrenorphin-Gly-generating enzyme; endoproteinase Kex2p; gene KEX2 dibasic proteinase; Kex 2p proteinase; Kex2 endopeptidase; Kex2 endoprotease; Kex2 endoproteinase; Kex2 protease; proteinase Kex2p; Kex2-like precursor protein processing endoprotease; prohormone-processing KEX2 proteinase; prohormone-processing proteinase; proprotein convertase; protease KEX2; Kex2 proteinase; Kex2-like endoproteinase. Cat No: EXWM-4152. | |
| Leupeptin | Leupeptin reversibly inhibits serine proteinases (trypsin (Ki=3.5 nM), plasmin (Ki= 3.4 nM), porcine kallikrein), and cysteine proteinases (papain, cathepsin B (Ki = 4.1 nM), endoproteinase Lys-C). Leupeptin has been shown to inhibit activation-induced programmed cell death. Synonyms: 2-(2-acetamido-4-methylvaleramido)-n-(1-formyl-4-guanidinobutyl)-4-methylval; 2-(2-acetamido-4-methylvaleramido)-n-(1-formyl-4-guanidinobutyl)-4-valeramid; leupeptinac-ll; l-leucinamide,n-acetyl-l-leucyl-n-(4-((aminoiminomethyl)amino)-1-formylbutyl; Leupeptin; Leupeptin Ac-LL; N-Acetyl-L-leucyl-L-leucyl-L-argininal; NK-381; NK 381; NK381. Grades: >98%. CAS No. 24365-47-7. Molecular formula: C20H38N6O4. Mole weight: 426.55. |  |
| lysyl endopeptidase | From Achromobacter lyticus. Enzymes with similar specificity are produced by Lysobacter enzymogenes (Endoproteinase Lys-C;) and Pseudomonas aeruginosa (Ps-1;). In peptidase family S1 (trypsin family). Group: Enzymes. Synonyms: Achromobacter proteinase I (also see Comment); Achromobacter lyticus alkaline proteinase I; protease I; achromopeptidase; lysyl bond specific proteinase. Enzyme Commission Number: EC 3.4.21.50. CAS No. 123175-82-6. Achromopeptidase. 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-4144; lysyl endopeptidase; EC 3.4.21.50; 123175-82-6; Achromobacter proteinase I (also see Comment); Achromobacter lyticus alkaline proteinase I; protease I; achromopeptidase; lysyl bond specific proteinase. Cat No: EXWM-4144. | |
| Native Bacillus licheniformis Alkaline Protease | Proteinase catabolizes proteins by hydrolysis of peptide bonds. Proteases are inactivated by serine active-site inhibitors, such as phenylmethylsulfonyl fluoride (PMSF) and diisopropylfluorophosphate. Subtilisin a is a member of the serine s8 endoproteinase family. it has broad specificity with a preference for a large uncharged residue in the p1 position. it hydrolyzes native and denatured proteins, and is active under alkaline conditions. Applications: The enzyme has been used to optimize release of all mitochondrial populations from homogenized ventricular tissue of rat heart.1 it has also been used in the pre-hybridisation treatment of formalin fixed, paraffin wax...ex); MCP; proteasome; large multicatalytic protease; multicatalytic proteinase; proteasome organelle; alkaline protease; 26S protease; triCorn proteinase; triCorn protease; EC 3.4.25.1. Enzyme Commission Number: EC 3.4.25.1. CAS No. 140879-24-9. Alkaline Protease. Mole weight: 27 Kda. Activity: 7.0-14.0 units/mg. Form: lyophilized powder. Source: Bacillus licheniformis. ingensin; macropain; multicatalytic endopeptidase complex; prosome; multicatalytic proteinase (complex); MCP; proteasome; large multicatalytic protease; multicatalytic proteinase; proteasome organelle; alkaline protease; 26S protease; triCorn proteinase; triCorn protease; EC 3.4.25.1. Cat No: NATE-0444. | |
| Native Bacillus licheniformis Protease | Protease catabolizes proteins by hydrolysis of peptide bonds. Proteases are inactivated by serine active-site inhibitors, such as phenylmethylsulfonyl fluoride (PMSF) and diisopropylfluorophosphate. Protease is a serine endoproteinase with a broad specificity towards native and denatured proteins, and is active under alkaline conditions. It is active in some organic solvents such as dry octane. The enzyme is found to be stable at ph 8-10, retaining activity of up to 90% for 24 hours. it shows maximum activity at temperatures between 55-60°c. Applications: The product has been used with other enzymes for in situ proteolysis to produce crystals suitable for structure determi...f bacillus licheniformis. it is a serine endoproteinase with a broad specificity towards native and denatured proteins, and is active under alkaline conditions. Group: Enzymes. Synonyms: Protease; 9014-01-1; Subtilisin A; EC 3.4.21.62; Alcalase. Enzyme Commission Number: EC 3.4.21.62. CAS No. 9001-92-7. Protease. Mole weight: Subtilisin is a non-glycosylated single polypeptide chain without disulfide bonds and has a molecular weight of 27 KDa. Activity: Type VIII, 7-15 units/mg solid; Type I, > 2.4 U/g. Form: Type VIII, lyophilized powder; Type I, aqueous solution. Source: Bacillus licheniformis. Protease; 9014-01-1; Subtilisin A; EC 3.4.21.62; Alcalase. Cat No: NATE-0633. | |
| Native Bovine Factor X Activated (Xa) | Factor Xa catalyzes the hydrolysis of the Arg-Thr and then Arg-Ile bonds in prothrombin to yield active thrombin. The fairly strict recognition sequence is Ile-Glu (or Asp)-Gly-Arg-↓-X. It may sometimes cleave at other basic residues, depending on the conformation of the target protein. Factor Xa will not cleave if a proline residue follows the arginine of the recognition sequence. Factor xa is a serine endoproteinase and a member of the s1 peptidase family. factor xa plays a critical role in the coagulation cascade by catalyzing the proteolytic conversion of prothrombin to active thrombin. factor xa?s prothrombin conversion activity is greatly enhanced in vivo when c...d with 10 μg of factor xa for 2.5 hours at 37 oc. Group: Enzymes. Synonyms: EC 3.4.21.6; 9002-05-5; thrombokinase; prothrombase; prothrombinase; activated blood-coagulation factor X; autoprothrombin C; thromboplastin; plasma thromboplastin; factor Xa; activated Stuart-Prower factor; activated factor X; coagulation factor Xa. Enzyme Commission Number: EC 3.4.21.6. CAS No. 9002-5-5. Factor Xa. Storage: -20°C. Form: aqueous glycerol solution. Source: Bovine plasma. Species: Bovine. EC 3.4.21.6; 9002-05-5; thrombokinase; prothrombase; prothrombinase; activated blood-coagulation factor X; autoprothrombin C; thromboplastin; plasma thromboplastin; factor Xa; activated Stuart-Pr | |
| Native Clostridium histolyticum Clostripain | Clostripain from Clostridium histolyticum is composed of two polypeptide chains, with molecular masses of 41.7 kDa and 15.4 kDa. Clostripain has a highly restricted substRate specificity for Arg-Xaa peptide bonds. Therefore, clostripain has been explored as a potential enzyme for protein sequencing purposes. It has also been studied as a catalyst for condensation of pharmaceutically important peptides containing Arg-Pro bonds. The isoelectric point of the enzyme is 4.8-4.9 (at 8°C), and optimum pH is 7.4~7.8 (against α-benzoyl-arginine ethyl ester). Group: Enzymes. Synonyms: clostridiopeptidase B; clostridium histolyticum proteinase B; α-clostridipain; clostridiopeptidase; Endoproteinase Arg-C; EC 3.4.22.8; 9028-00-6. Enzyme Commission Number: EC 3.4.22.8. CAS No. 9028-00-6. Kallikrein. Activity: > 20 units/mg solid. Storage: 2-8°C. Form: lyophilized powder. Source: Clostridium histolyticum. clostridiopeptidase B; clostridium histolyticum proteinase B; α-clostridipain; clostridiopeptidase; Endoproteinase Arg-C; EC 3.4.22.8; 9028-00-6. Cat No: NATE-0143. | |
| peptidyl-Asp metalloendopeptidase | A metalloenzyme isolated from Pseudomonas fragi. Useful in protein sequencing applications because of its limited specificity. In peptidase family M72. Group: Enzymes. Synonyms: endoproteinase Asp-N; peptidyl-Asp metalloproteinase. Enzyme Commission Number: EC 3.4.24.33. CAS No. 55576-49-3. Endoproteinase Asp-N. 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-4315; peptidyl-Asp metalloendopeptidase; EC 3.4.24.33; 55576-49-3; endoproteinase Asp-N; peptidyl-Asp metalloproteinase. Cat No: EXWM-4315. | |
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