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| Product | Description | |
|---|---|---|
| Proteinase K | 100mg Pack Size. Group: Biochemicals, Diagnostic Raw Materials, Research Organics & Inorganics. Formula: C29H27N2O12P. CAS No. 39450-01-6. Prepack ID 49085587-100mg. Molecular Weight 626.5. See USA prepack pricing. |  |
| Proteinase K | Proteinase K (Protease K) is a nonspecific serine protease that is useful for general digestion of proteins. Proteinase K is active in the presence of SDS or urea and over a wide range of pH (4-12), salt concentrations, and temperatures. Proteinase K can be use for promoting methods of viral nucleic acid extraction, and detection [1] [2] [3] [4]. Uses: Scientific research. Group: Signaling pathways. Alternative Names: Protease K. CAS No. 39450-01-6. Pack Sizes: 25 mg; 50 mg; 100 mg; 500 mg. Product ID: HY-108717. |  |
| Proteinase K from Tritirachium album limber, Recombinant | Proteinase K is a stable and highly reactive serine protease. Evidence from crystal and molecular structure studies indicates the enzyme belongs to the subtilisin family with an active-site catalytic triad (Asp39-His69-Ser224). It is stable in a broad range of environments:pH, buffer salts, detergents (SDS), and temperature. In the presence of 0.1-0.5% SDS, proteinase K retains activity and will digest a variety of proteins and nucleases in DNA preparations without compromising the integrity of the isolated DNA. Group: Enzymes. Synonyms: Proteinase K; EC 3.4.21.64; Tritirachium alkaline proteinase; Tritirachium album serine proteinase; Tritirachium album proteinase K; endopeptidase K; 39450-01-6; protease K. CAS No. 39450-01-6. Purity: > 95%. Proteinase K. Activity: > 30U/mg. Storage: 4°C~-20°C. Form: Powder. Source: Pichia pastoris. Species: Tritirachium album limber. Proteinase K; EC 3.4.21.64; Tritirachium alkaline proteinase; Tritirachium album serine proteinase; Tritirachium album proteinase K; endopeptidase K; 39450-01-6; protease K. Cat No: NATE-1240. |  |
| Immobilized Proteinase K on Eupergit(R) C | Proteinase K hydrolyses keratin by cleaving peptide bonds adjacent to the carboxyl group of aliphatic and aromatic amino acids. Group: Enzymes. Synonyms: Tritirachium alkaline proteinase; Tritirachium album serine proteinase; proteinase K; Tritirachium album proteinase K; endopeptidase K; EC 3. 4. 21. 64; 39450-01-6. Enzyme Commission Number: EC 3. 4. 21. 64. Activity: >1500 U/g. Storage: 2-8°C. Form: powder (granular). Source: Tritirachium album. Tritirachium alkaline proteinase; Tritirachium album serine proteinase; proteinase K; Tritirachium album proteinase K; endopeptidase K; EC 3. 4. 21. 64; 39450-01-6; Immobilized Proteinase K. Cat No: NATE-1776. | |
| Immobilized Proteinase K on G3m | Proteinase K is an unspecific serine protease with strong proteolytic activity on denatured (in SDS) and high molecular weight native proteins. It cleaves peptide bonds mostly after the carboxyl group of N-substituted hydrophobic, aliphatic and aromatic amino acids. G3m: 25 ug proteinase K immobilized on matrix G3m per CR-column. 0.7 mAnson units immobilized per CR-column. This CR-column cuts at least 370 ug BSA per application. Nr. 5 Storage buffer: 50 mM Tris/HCl, pH 7. 5Nr. 16 Reaction buffer: 50 mM Tris/HCl, 5 mM NaCl, pH 8. 0Nr. 17 Washing buffer: 50 mM Tris/HCl, 1. 0 M NaCl, pH 8. 0The columns are more active in 0.1% SDS and at 40°C. Also active in PBS buffer (20 mM Na-phosphate, 150 mM NaCl at pH 7. 6). Group: Enzymes. Synonyms: Tritirachium alkaline proteinase; Tritirachium album serine proteinase; proteinase K; Tritirachium album proteinase K; endopeptidase K; EC 3. 4. 21. 64; 39450-01-6. Enzyme Commission Number: EC 3. 4. 21. 64. Purity: Chromatographically purified, free of ribo- and deoxyribonucleases. Storage: 4 °C. Source: Tritirachium album. Tritirachium alkaline proteinase; Tritirachium album serine proteinase; proteinase K; Tritirachium album proteinase K; endopeptidase K; EC 3. 4. 21. 64; 39450-01-6; Immobilized Proteinase K. Cat No: NATE-1768. | |
| Native Streptomyces sp. Alkalophilic proteinase | Native Streptomyces sp. Alkalophilic proteinase. Applications: This enzyme is more active at a higher ph range than the known alkaline protease, showing the proteolytic activity even in 0.2n naoh solution. this enzyme is useful for proteolysis of insoluble protein and for structure investigation of protein. Group: Enzymes. Synonyms: Alkalophilic proteinase; EC 3.4.21.-. Enzyme Commission Number: EC 3.4.21.-. Alkalophilic proteinase. Mole weight: approx. 50 kDa. Activity: Grade ? 20U/mg-solid or more. Stability: Stable at-20?C for at least one year. Appearance: White amorphous powder, lyophilized. Form: Freeze dried powder. Source: Streptomyces sp. Alkalophilic proteinase; EC 3.4.21.-. Cat No: DIA-183. | |
| Native Tritirachium album limber Proteinase K | Proteinase K (PROK) is a serine protease with broad specificity towards aliphatic, aromatic and other hydrophobic amino acids. PROK has a molecular weight of 27,000 daltons and is Ca2+ dependent. It is not inactivated by metal ion chelating agents such as EDTA, sulfhydryl reagents, PCMB, TLCK, or TPCK. It also retains activity in 0.5% SDS. It can be inhibited by PMSF or DFP. Applications: Useful for the proteolytic inactivation of nucleases during the isolation of dna and rna. removes endotoxins that bind to cationic proteins such as lysozyme and ribonuclease a. reported useful for the isolation of hepatic, yeast, and mung bean mit ochondria determination of enzyme l o...oteinase; Tritirachium album proteinase K; endopeptidase K; 39450-01-6; protease K. Enzyme Commission Number: EC 3.4.21.64. CAS No. 39450-01-6. Purity: Purified to remove DNase and RNase. Proteinase K. Mole weight: 27 kDa. Activity: Type I, > 20 units per mg dry weight; Type II, > 400 u/ml. Storage: Powder: 2-8°C; Liquid: -20°C. Form: Type I, powder; Type II, Liquid in 20mg/ml in 10mM Tris-HCl, 1mM calcium acetate, pH 7.5 containing 50% glycerol. Source: Tritirachium album limber. Proteinase K; EC 3.4.21.64; Tritirachium alkaline proteinase; Tritirachium album serine proteinase; Tritirachium album proteinase K; endopeptidase K; 39450-01-6; protease K. Cat No: NATE-0637. | |
| Native Tritirachium album Proteinase K | Proteinase K is a stable and highly reactive serine protease. Evidence from crystal and molecular structure studies indicates the enzyme belongs to the subtilisin family with an active-site catalytic triad (Asp39-His69-Ser224). It is stable in a broad range of environments:pH, buffer salts, detergents (SDS), and temperature. In the presence of 0.1-0.5% SDS, proteinase K retains activity and will digest a variety of proteins and nucleases in DNA preparations without compromising the integrity of the isolated DNA. Applications: Proteinase k is useful for the proteolytic inactivation of nucleases during the isolation of dna and rna. it is used for the removal of endotoxins bo... used to facilitate the access of probes to rrna using fish techniques to detect pathogenic staphylococcus aureus. useful for the proteolytic inactivation of nucleases during the isolation of dna and rna. removes endotoxins that bind to cationic proteins such as lysozyme and ribonuclease a. reported useful for the isolation of hepatic, yeast, and mung bean mitochondria determination of enzyme localization on membranes treatment of paraffin embedded tissue sections to expose antigen binding sites for antibody labeling. digestion of proteins from brain tissue samples for prions in transmissible spongiform encephalopathies (tse) research. Group: Enzymes. Synonyms: Tritirachiu | |
| Proteinase inhibitor,PDI (potato 20.6-kilodalton protein moiety reduced) (9CI) | Heterocyclic Organic Compound. CAS No. 126731-59-7. Catalog: ACM126731597. |  |
| 1,4-Diaminoanthraquinone | An anthraquinone derivative that is a potent and selective protein kinase CK1 delta inhibitor. Studies suggest that it has potential solar cell applications. Used in studies as a potential competitive non-peptidic inhibitor of HIV-1 proteinase. Group: Biochemicals. Alternative Names: 1,4-Diamino-9,10-anthraquinone; Acetate Red Violet R; Acetoquinone Light Heliotrope NL; Acetylon Fast Red Violet R; Akasperse Violet 3R; Amacel Heliotrope R; Cibacet Violet 2R; C.I. 61100; NSC 63807; NSC 7833; Krisolamine; Violet 14447. Grades: Highly Purified. CAS No. 128-95-0. Pack Sizes: 2.5g. US Biological Life Sciences. |  Worldwide |
| Ac-DEVD-CHO | Ac-DEVD-CHO is a potent aldehyde inhibitor of Group II caspases with Ki values of 0.2 nM and 0.3 nM for for caspase-3 and caspase-7, respectively. Weak inhibition for caspase-2. Uses: Cysteine proteinase inhibitors. Synonyms: N-acetyl-asp-glu-val-asp-al; Ac-Asp-Glu-Val-Asp-Aldehyde; L-Valinamide,N-acetyl-L-a-aspartyl-L-a-glutamyl-N-(2-carboxy-1-formylethyl)-. Grades: 95 %. CAS No. 169332-60-9. Molecular formula: C20H30N4O11. Mole weight: 502.47. |  |
| actinidain | From the kiwi fruit or Chinese gooseberry (Actinidia chinensis). In peptidase family C1 (papain family). Group: Enzymes. Synonyms: actinidin; Actinidia anionic protease; proteinase A2 of Actinidia chinensis. Enzyme Commission Number: EC 3.4.22.14. CAS No. 39279-27-1. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4194; actinidain; EC 3.4.22.14; 39279-27-1; actinidin; Actinidia anionic protease; proteinase A2 of Actinidia chinensis. Cat No: EXWM-4194. | |
| adamalysin | From the venom of the eastern diamondback rattlesnake (Crotalus adamanteus). Two isoenzymes of approx. 24 kDa that inactivate α1-proteinase inhibitor by a single cleavage. In peptidase family M12 (astacin family). Group: Enzymes. Synonyms: Crotalus adamanteus metalloendopeptidase; proteinase I and II; Crotalus adamanteus venom proteinase II; adamalysin II. Enzyme Commission Number: EC 3.4.24.46. CAS No. 74812-51-4. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4328; adamalysin; EC 3.4.24.46; 74812-51-4; Crotalus adamanteus metalloendopeptidase; proteinase I and II; Crotalus adamanteus venom proteinase II; adamalysin II. Cat No: EXWM-4328. | |
| Adenovirus Proteinase Inhibitor, NSC 37249 (2- (Dicyclohexylamino) -N- (4- (4- ( (2- (dicyclohexylamino) acetyl) amino) phenyl) sulfonylphenyl) acetamide, N, N?- (Sulfonyldi-4, 1-phenylene) bis (2- (dicyclohexylamino) acetamide, AVP Inhibitor) | A sulfonyl diphenyl ene -bis-dicyclohexyl aminoacetamide compound that acts as a potent and selective inhibitor against adenovirus cysteine proteinase AVP by targeting simultaneously AVP co-factor pVIc (GVQSLKRRRCF) N-terminal binding pocket (Ki = 150nM) and AVP-pVIc substrate-binding site (Ki = 400nM), blocking both AVP-pVIc active complex formation (IC50 = 140nM; [substrate] = 5uM & [pVIc] = 40uM) and catalytic activity (IC50 = 490nM; [substrate] = 5uM) without affecting trypsin or papain protease activity even at concentrations as high as 10uM. Group: Biochemicals. Grades: Purified. CAS No. 2907-88-2. Pack Sizes: 10mg. Molecular Formula: C??H??N?O?S. US Biological Life Sciences. | Worldwide |
| Aprotinin, Bovine (Pancreatic trypsin inhibitor) | Aprotinin is a competitive serine protease inhibitor that inhibits trypsin, chymotrypsin, kallikrein and plasmin. Aprotinin forms stable complexes with and blocks the active sites of enzymes. Binding is reversible with most aprotinin-protease complexes, dissociating at pH >10 or <3. Effective concentration is equimolar with protease. Group: Biochemicals. Alternative Names: Antikrein; Antilysin; Antilysine; Aprostat; Aprotinin; BPTI; BPTI Trypsin Inhibitor; Basic Pancreatic Trypsin Inhibitor; Bayer A 128; Bovine Basic Pancreatic Trypsin Inhibitor; Bovine Pancreatic Trypsin Inhibitor; Bovine Trypsin Inhibitor; Fosten; Kallikrein-trypsin Inactivator; Kiker 52G; Kir Richter; Kunitz Pancreatic Trypsin Inhibitor; Kunitz Protease Inhibitor; Kunitz Trypsin Inhibitor; Kunitz-type Inhibitor; Kunitz-type Proteinase Inhibitor; Kunitz-type Trypsin Inhibitor; Onquinin; Pancreatic Basic Trypsin Inhibitor; Pancreatic Trypsin Inhibitor; Pancreatic Trypsin Inhibitor (Kunitz); Protease Inhibitor, Kunitz Type; RP 9921; Repulson; Trasuylol; Trasylol; Trazinin; Triazinin; Trypsin Inhibitor, Trasylol; Trypsin-kallikrein Inhibitor (Kunitz); Zymofren. Grades: Highly Purified. CAS No. 9087-70-1. Pack Sizes: 100mg, 250mg, 500mg, 1g. Molecular Formula: C???H???N??O??S?, Molecular Weight: 6511.45. US Biological Life Sciences. | Worldwide |
| aspergillopepsin I | Found in a variety of Aspergillus species (imperfect fungi): Aspergillus awamori (awamorin, aspergillopepsin A:), A. foetidus (aspergillopepsin F:), A. fumigatus, A. kawachii, A. niger (proteinase B, proctase B:), A. oryzae (trypsinogen kinase:), A. saitoi (aspergillopeptidase A:), and A. sojae. In peptidase family A1 (pepsin A family). Formerly included in EC 3.4.23.6. Group: Enzymes. Synonyms: Aspergillus acid protease; Aspergillus acid proteinase; Aspergillus aspartic proteinase; Aspergillus awamori acid proteinase; Aspergillus carboxyl proteinase; (see also Comments); carboxyl proteinase; Aspergillus kawachii aspartic proteinase; Aspergillus saitoi acid proteinase; pepsin-type aspartic proteinase. Enzyme Commission Number: EC 3.4.23.18. CAS No. 9025-49-4. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4255; aspergillopepsin I; EC 3.4.23.18; 9025-49-4; Aspergillus acid protease; Aspergillus acid proteinase; Aspergillus aspartic proteinase; Aspergillus awamori acid proteinase; Aspergillus carboxyl proteinase; (see also Comments); carboxyl proteinase; Aspergillus kawachii aspartic proteinase; Aspergillus saitoi acid proteinase; pepsin-type aspartic proteinase; Aspergillus niger acid proteinase; sumizyme AP; proctase P; denapsin; denapsin XP 271; proctase. Cat No: EXWM-4255. | |
| astacin | A 22.6 kDa digestive endopeptidase from the cardia of the crayfish Astacus fluviatilis. Type example of peptidase family M12. Group: Enzymes. Synonyms: Astacus proteinase; crayfish small-molecule proteinase. Enzyme Commission Number: EC 3.4.24.21. CAS No. 143179-21-9. 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-4302; astacin; EC 3.4.24.21; 143179-21-9; Astacus proteinase; crayfish small-molecule proteinase. Cat No: EXWM-4302. | |
| atrolysin A | A hemorrhagic endopeptidase of 68 kDa, one of six hemorrhagic toxins in the venom of western diamondback rattlesnake. The 60 kDa hemorrhagic toxin 1 of Crotalus ruber ruber shows identical specificity. In peptidase family M12 (astacin family). Related metalloendopeptidases from rattlesnake venoms are EC 3.4.24.41 (atrolysin B), EC 3.4.24.42 (atrolysin C), EC 3.4.24.43 (atroxase), EC 3.4.24.44 (atrolysin E), EC 3.4.24.45 (atrolysin F), EC 3.4.24.46 (adamalysin), EC 3.4.24.47 (horrilysin), and EC 3.4.24.48 (ruberlysin). Group: Enzymes. Synonyms: Crotalus atrox metalloendopeptidase a; hemorrhagic toxin a; Crotalus atrox α-proteinase; Crotalus atrox proteinase; bothropasin. Enzyme Commission Number: EC 3.4.24.1. CAS No. 37288-82-7. 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-4291; atrolysin A; EC 3.4.24.1; 37288-82-7; Crotalus atrox metalloendopeptidase a; hemorrhagic toxin a; Crotalus atrox α-proteinase; Crotalus atrox proteinase; bothropasin. Cat No: EXWM-4291. | |
| barrierpepsin | A secreted endopeptidase known from bakers yeast (Saccharomyces cerevisiae). In peptidase family A1 (pepsin A family). Group: Enzymes. Synonyms: barrier proteinase; Bar proteinase. Enzyme Commission Number: EC 3.4.23.35. CAS No. 152060-38-3. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4272; barrierpepsin; EC 3.4.23.35; 152060-38-3; barrier proteinase; Bar proteinase. Cat No: EXWM-4272. | |
| Benzamidine hydrochloride | Benzamidine is a reversible inhibitor of serine proteases, including trypsin, plasmin, and thrombin (Kis = 35, 350, and 220 μM, respectively). Benzamidine inhibits the autoactivation of human blood coagulation factor VII, useful as a tool for studying the interactions between this and other relevant growth factors. Uses: Serine proteinase inhibitors. Synonyms: Benzenecarboximidamide, hydrochloride (1:1); Benzamidine, monohydrochloride; Benzenecarboximidamide, monohydrochloride; Amidinobenzene hydrochloride; Benzamidinium chloride; Benzimidamide hydrochloride. Grades: ≥98%. CAS No. 1670-14-0. Molecular formula: C7H8N2.HCl. Mole weight: 156.61. | |
| CA 074 | CA 074 is a potent and selective inhibitor of cathepsin B (Ki = 2-5 nM). It reduces bone metastasis in a 4T1.2 breast cancer model. Uses: Cysteine proteinase inhibitors. Synonyms: CA-074; CA074; CA 074; N-[[(2S,3S)-3-[(Propylamino)carbonyl]-2-oxiranyl]carbonyl]-L-isoleucyl-L-proline. Grades: ≥98% by HPLC. CAS No. 134448-10-5. Molecular formula: C18H29N3O6. Mole weight: 383.44. | |
| Calpain Inhibitor II | Calpain inhibitor II is a cell-permeable inhibitor of calpain I (Ki = 120 nM), calpain II (Ki = 230 nM), cathepsin B (Ki = 100 nM), and cathepsin L (Ki = 600 pM). It inhibits activation-induced programmed cell death and restores defective immune responses in HIV+ donors. Calpain inhibitor II can block nitric oxide production by interfering with transcription of the inducible nitric oxide synthase gene, which is a weak inhibitor of proteasome. It has been used to demonstrate the involvement of ubiquitin-proteasome protein degradation in various biological systems. Uses: Cysteine proteinase inhibitors. Synonyms: L-Leucinamide, N-acetyl-L-leucyl-N-[(1S)-1-formyl-3-(methylthio)propyl]-; L-Leucinamide, N-acetyl-L-leucyl-N-[1-formyl-3-(methylthio)propyl]-, (S)-; N-Acetyl-L-leucyl-N-[(1S)-1-formyl-3-(methylthio)propyl]-L-leucinamide; ALLM; Calp II; CI 2; SUAM 312; N-acetylleucyl-leucyl-methioninal; Ac-Leu-Leu-Met-al; N-acetyl-L-leucyl-L-leucyl-L-methioninal. Grades: ≥98%. CAS No. 110115-07-6. Molecular formula: C19H35N3O4S. Mole weight: 401.57. | |
| Calpeptin | Calpeptin is a potent, cell-permeable calpain inhibitor with ID50 of 52 nM, 34 nM, 138 nM, and 40 nM for Calpain I (porcine erythrocytes), Calpain II (porcine kidney), Papainb, and Calpain I (human platelets), respectively. Uses: Cysteine proteinase inhibitors. Synonyms: Benzylcarbonyl-leu-nleu-H; Cbz-Leu-Nle-al. Grades: >98%. CAS No. 117591-20-5. Molecular formula: C20H30N2O4. Mole weight: 362.46. | |
| carboxypeptidase D | A carboxypeptidase with optimum pH 4.5-6.0, inhibited by diisopropyl fluorophosphate, and sensitive to thiol-blocking reagents (reviewed in). In peptidase family S10 (carboxypeptidase C family). Group: Enzymes. Synonyms: cereal serine carboxypeptidase II; Saccharomyces cerevisiae KEX1 gene product; carboxypeptidase Kex1; gene KEX1 serine carboxypeptidase; KEX1 carboxypeptidase; KEX1 proteinase; KEX1DELTAp; CPDW-II; serine carboxypeptidase (misleading); Phaseolus proteinase. Enzyme Commission Number: EC 3.4.16.6. CAS No. 153967-26-1. CPDW-II. 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-4060; carboxypeptidase D; EC 3.4.16.6; 153967-26-1; cereal serine carboxypeptidase II; Saccharomyces cerevisiae KEX1 gene product; carboxypeptidase Kex1; gene KEX1 serine carboxypeptidase; KEX1 carboxypeptidase; KEX1 proteinase; KEX1DELTAp; CPDW-II; serine carboxypeptidase (misleading); Phaseolus proteinase. Cat No: EXWM-4060. | |
| caspase-1 | From mammalian monocytes. This enzyme is part of the family of inflammatory caspases, which also includes caspase-4 (EC 3.4.22.57) and caspase-5 (EC 3.4.22.58) in humans and caspase-11 (EC 3.4.22.64), caspase-12, caspase-13 and caspase-14 in mice. Contains a caspase-recruitment domain (CARD) in its N-terminal prodomain, which plays a role in procaspase activation. Cleaves pro-interleukin-1β (pro-IL-1β) to form mature IL-1β, a potent mediator of inflammation. Also activates the proinflammatory cytokine, IL-18, which is also known as interferon-γ-inducing factor. Inhibited by Ac-Tyr-Val-Ala-Asp-CHO. Caspase-11 plays a critical role in the activation of caspase-1 in mi...proteinase; ICE. Enzyme Commission Number: EC 3.4.22.36. CAS No. 122191-40-6. 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-4211; caspase-1; EC 3.4.22.36; 122191-40-6; interleukin 1β-converting enzyme; protease VII; protease A; interleukin 1β precursor proteinase; interleukin 1 converting enzyme; interleukin 1β-converting endopeptidase; interleukin-1β convertase; interleukin-1β converting enzyme; interleukin-1β precursor proteinase; prointerleukin 1β protease; precursor interleukin-1β converting enzyme; pro-interleukin 1β proteinase; ICE. Cat No: EXWM-4211. | |
| cathepsin E | Found in stomach, spleen, erythrocyte membrane; not lysosomal. Pro-cathepsin E is an 86 kDa disulfide-linked dimer; activation or reduction produces monomer. In peptidase family A1 (pepsin A family). Group: Enzymes. Synonyms: slow-moving proteinase; erythrocyte membrane aspartic proteinase; SMP; erythrocyte membrane aspartic proteinase; EMAP; non-pepsin proteinase; cathepsin D-like acid proteinase; cathepsin E-like acid proteinase; cathepsin D-type proteinase. Enzyme Commission Number: EC 3.4.23.34. CAS No. 110910-42-4. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4271; cathepsin E; EC 3.4.23.34; 110910-42-4; slow-moving proteinase; erythrocyte membrane aspartic proteinase; SMP; erythrocyte membrane aspartic proteinase; EMAP; non-pepsin proteinase; cathepsin D-like acid proteinase; cathepsin E-like acid proteinase; cathepsin D-type proteinase. Cat No: EXWM-4271. | |
| Cathepsin F from Human, Recombinant | Cathepsin F, also known as CTSF, belongs to the cathepsin family. Cathepsins are papain familycysteine proteinases that represent a major component of the lysosomal proteolytic system. The CTSF gene isubiquitously expressed, and it maps to chromosome 11q13, close to the gene encoding cathepsin W. CTSF isthought to play a role in normal protein catabolism, and because it is highly expressed in some cancer cell lines, itmay be involved in degradative processes occurring during tumor progression. Recombinant human CTSF protein,fused to His-tag at N-terminus, was expressed in E.coli. Group: Enzymes. Enzyme Commission Number: EC 3.4.22.41. Mole weight: This protein is fused with a 6× His tag at N-terminus and has a calculated MW of 26 kDa. Form: Liquid. Source: E. coli. Species: Human. Cat No: NATE-1666. | |
| Cathepsin K from Human, recombinant | Cathepsin K, a member of the papain cysteine proteinase family is the predominant proteinase responsible for the resorption of the bone matrix. Cathepsin cleaves proteins such as collagen type I, collagen type II and osteonectin, thereby playing a role in bone remodeling and resorption in osteoporosis, osteolytic bone metastasis and rheumatoid arthritis. Group: Enzymes. Synonyms: CTSK; CTSO; CTSO3; Cathepsin O; Cathepsin O2; Cathepsin X; EC 3.4.22.38. Enzyme Commission Number: EC 3.4.22.38. CAS No. 94716-09-3. Purity: > 95% by SDS-PAGE. Activity: >900 mU/mg protein. Storage: at -80°C. Avoid freeze/thaw. Form: Liquid. Source: E. coli. Species: Human. CTSK; CTSO; CTSO3; Cathepsin O; Cathepsin O2; Cathepsin X; EC 3.4.22.38. Cat No: NATE-1705. | |
| Cathepsin K from Mouse, recombinant | Cathepsin K, a member of the papain cysteine proteinase family is the predominant proteinase responsible for the resorption of the bone matrix. Cathepsin cleaves proteins such as collagen type I, collagen type II and osteonectin, thereby playing a role in bone remodeling and resorption in osteoporosis, osteolytic bone metastasis and rheumatoid arthritis. Group: Enzymes. Synonyms: CTSK; CTSO; CTSO3; Cathepsin O; Cathepsin O2; Cathepsin X; EC 3.4.22.38. Enzyme Commission Number: EC 3.4.22.38. CAS No. 94716-09-3. Purity: > 90% by SDS-PAGE. Mole weight: 23.4 kDa (115-329 aa). Activity: >1000 mU/mg. Storage: Stable for 6 months at -80°C. Use as provided or dilute to 0.1 mg/ml with 50% glycerol. Aliquot and store at -80°C. Avoid repeated freezing and thawing cycles, as this may lead to the loss in its activity over time. Form: Liquid. Source: E. coli. Species: Mouse. CTSK; CTSO; CTSO3; Cathepsin O; Cathepsin O2; Cathepsin X; EC 3.4.22.38. Cat No: NATE-1704. | |
| Cathepsin K from Rat, recombinant | Cathepsin K, a member of the papain cysteine proteinase family is the predominant proteinase responsible for the resorption of the bone matrix. Cathepsin cleaves proteins such as collagen type I, collagen type II and osteonectin, thereby playing a role in bone remodeling and resorption in osteoporosis, osteolytic bone metastasis and rheumatoid arthritis. Group: Enzymes. Synonyms: CTSK; CTSO; CTSO3; Cathepsin O; Cathepsin O2; Cathepsin X; EC 3.4.22.38. Enzyme Commission Number: EC 3.4.22.38. CAS No. 94716-09-3. Purity: > 90% by SDS-PAGE. Mole weight: 23.5 kDa (115-329 aa). Activity: >500 mU/mg. Storage: Stable for 6 months at -80°C. Use as provided or dilute to 0.1 mg/ml with 50% glycerol. Aliquot and store at -80°C. Avoid repeated freezing and thawing cycles, as this may lead to the loss in its activity over time. Form: Liquid. Source: E. coli. Species: Rat. CTSK; CTSO; CTSO3; Cathepsin O; Cathepsin O2; Cathepsin X; EC 3.4.22.38. Cat No: NATE-1703. | |
| Cathepsin L from Human, Recombinant | 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. Group: Enzymes. Synonyms: Cathepsin L1; Major excreted protein; Cathepsin U; Cathepsin V. Enzyme Commission Number: EC 3.4.22.15. Purity: > 90% by SDS-PAGE. CTSL. Mole weight: 24.2 kDa (114-333 aa). Activity: > 10000 mU/mg. Stability: Stable for at least 6 months as supplied. Use as provided or dilute with 50% glycerol to 0.1 mg/ml. Aliquot immediately and store at -80°C. Avoid freeze/thaw cycles. Storage: Store at -80°C. Form: Liquid. Source: E. coli. Species: Human. cathepsin L; CTSL; EC 3.4.22.15; Aldrichina grahami cysteine proteinase; 60616-82-2; Cathepsin L1; Major excreted protein; Cathepsin U; Cathepsin V. Cat No: NATE-1665. | |
| Cetraxate hydrochloride | Cetraxate hydrochloride (DV-1006), an orally active anti-ulcer agent with mucosal protective effects, can be used for gastric ulcers research [1]. Cetraxate hydrochloride is a potent acrosomal proteinase acrosin inhibitor with a K i and an IC 50 of 0.94 μM and 3.3 μM, respectively [2]. Uses: Scientific research. Group: Signaling pathways. Alternative Names: DV-1006. CAS No. 27724-96-5. Pack Sizes: 10 mM * 1 mL; 5 mg; 10 mg; 25 mg; 50 mg. Product ID: HY-122762. | |
| Chymase from Human, Recombinant | Chymases are a family of serine proteases found primarily in mast cells, though also present in basophil granulocytes (e.g. alpha chymase mcpt8). They show broad peptidolytic activity and are involved in a variety of functions. For example, chymases are released by mucosal mast cells upon challenge with parasites and parasite antigens promoting an inflammatory response. Chymases are also known to convert angiotensin I to angiotensin II and thus play a role in hypertension and atherosclerosis. Because of its role in inflammation it has been investigated as a target in the treatment of asthma. Applications: Chymase has been implicated in generation of angiotensin ii and cleavag... Synonyms: mast cell protease I; skeletal muscle protease; skin chymotryptic proteinase; mast cell serine proteinase, chymase; skeletal muscle (SK) protease; chymase; EC 3.4.21.39; 97501-92-3. Enzyme Commission Number: EC 3.4.21.39. CAS No. 97501-92-3. Purity: >90% (SDS-PAGE). CMA1. Mole weight: ~30 kDa. Activity: >40 units/mg protein. Storage: Store at -20°C. Form: Supplied as a solution in 20 mM Tris, 0.8 M NaCl and 25% glycerol, pH 7.6. Source: Pichia pastoris. Species: Human. mast cell protease I; skeletal muscle protease; skin chymotryptic proteinase; mast cell serine proteinase, chymase; skeletal muscle (SK) protease; chymase; EC 3.4.21.39; 97501-92-3. Cat No: NATE-0817. | |
| Chymostatin | Chymostatin is a bioactive peptide that acts as a protease inhibitor with selectivity for chymotryptase-like serine proteases. It potently inhibits chymotrypsin and chymase, but it cannot block the activity of cathepsins, papain, and leukocyte elastase effectively. It doesn't have effect on trypsin, thrombin, plasmin, pepsin, and kallikrein. Uses: Serine proteinase inhibitors. Synonyms: [(S)-1-Carboxy-2-phenylethyl]-carbamoyl-a-[2-amidohexahydro-4(S)-pyrimidyl]-(S)-glycyl-[A= Leu B=Val C=Ile]-phenylalaninal (Mixture). Grades: ≥95% (a mixture of A, B, C). CAS No. 9076-44-2. Molecular formula: CxHyN7O6. Mole weight: 607.7. | |
| Cinanserin hydrochloride | Cinanserin hydrochloride (SQ 10643) is a potent, selective and highly affinity 5-HT 2 receptor antagonist with a K i of 41 nM. Cinanserin hydrochloride has a much higher binding affinity for the 5-HT 2 than for the 5-HT 1 receptor ( K i of 3500 nM). Cinanserin is also an inhibitor of 3C-like proteinase of severe acute respiratory syndrome coronavirus and strongly reduces virus replication in vitro [1] [2] [3]. Uses: Scientific research. Group: Signaling pathways. Alternative Names: SQ 10643. CAS No. 54-84-2. Pack Sizes: 10 mM * 1 mL; 5 mg; 10 mg; 50 mg; 100 mg. Product ID: HY-100943. | |
| Cinanserin hydrochloride | Cinanserin hydrochloride (SQ 10643) is a potent, selective and highly affinity 5-HT2 receptor antagonist with a Ki of 41 nM. Cinanserin hydrochloride has a much higher binding affinity for the 5-HT2 than for the 5-HT1 receptor (Ki of 3500 nM). Cinanserin is also an inhibitor of 3C-like proteinase of severe acute respiratory syndrome coronavirus and strongly reduces virus replication in vitro. Group: Inhibitors. Alternative Names: DPTC;DPTC HYDROCHLORIDE;CINANSERIN;CINANSERIN HYDROCHLORIDE;2'-(3-DIMETHYLAMINOPROPYL-THIO)-CINNAMANILIDE HYDROCHLORIDE; N-[2-[[3- (DIMETHYLAMINO)PROPYL]THIO]PHENYL]-3-PHENYL-2-PROPENAMIDE; N-[2-[[3- (DIMETHYLAMINO)PROPYL]THIO]PHENYL]-3-PHENYL-2-PROPENAMIDE. CAS No. 54-84-2. Molecular formula: C20H25ClN2OS. Mole weight: 376.94. Purity: 0.9974. Catalog: ACM54842. | |
| clostripain | From the bacterium Clostridium histolyticum. It requires Ca2+ ions and is inhibited by EDTA. Type example of peptidase family C11. Group: Enzymes. Synonyms: clostridiopeptidase B; clostridium histolyticum proteinase B; α-clostridipain; clostridiopeptidase. Enzyme Commission Number: EC 3.4.22.8. CAS No. 9028-00-6. Kallikrein. 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-4249; clostripain; EC 3.4.22.8; 9028-00-6; clostridiopeptidase B; clostridium histolyticum proteinase B; α-clostridipain; clostridiopeptidase. Cat No: EXWM-4249. | |
| coccolysin | A 30 kDa endopeptidase found intracellularly in S. thermophilus and S. diacetilactis and in the medium of S. faecalis. In peptidase family M4 (thermolysin family). Formerly included in EC 3.4.24.4. Group: Enzymes. Synonyms: Streptococcus thermophilus intracellular proteinase; EM 19000. Enzyme Commission Number: EC 3.4.24.30. CAS No. 156859-08-4. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4312; coccolysin; EC 3.4.24.30; 156859-08-4; Streptococcus thermophilus intracellular proteinase; EM 19000. Cat No: EXWM-4312. | |
| deuterolysin | Proteolytic activity found in Penicillium roqueforti, P. caseicolum, Aspergillus sojae and A. oryzae. Optimum pH of 5 for digesting various proteins. Strong action on protamine and histones. Insensitive to phosphoramidon. About 20 kDa. A distinct Aspergillus sojae endopeptidase is larger and has a neutral pH optimum. Type example of peptidase family M35. Formerly included in EC 3.4.24.4. Group: Enzymes. Synonyms: Penicillium roqueforti protease II; microbial neutral proteinase II; acid metalloproteinase; neutral proteinase II; Penicillium roqueforti metalloproteinase. Enzyme Commission Number: EC 3.4.24.39. CAS No. 247028-11-1. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4321; deuterolysin; EC 3.4.24.39; 247028-11-1; Penicillium roqueforti protease II; microbial neutral proteinase II; acid metalloproteinase; neutral proteinase II; Penicillium roqueforti metalloproteinase. Cat No: EXWM-4321. | |
| 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. | |
| fibrolase | A 23-kDa, non-hemorrhagic enzyme from the venom of the southern copperhead snake (Agkistrodon contortix contortix). In peptidase family M12 (astacin family). Group: Enzymes. Synonyms: fibrinolytic proteinase; Agkistrodon contortrix contortrix metalloproteinase; Agkistrodon contortrix contortrix venom metalloproteinase. Enzyme Commission Number: EC 3.4.24.72. CAS No. 116036-70-5. 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-4356; fibrolase; EC 3.4.24.72; 116036-70-5; fibrinolytic proteinase; Agkistrodon contortrix contortrix metalloproteinase; Agkistrodon contortrix contortrix venom metalloproteinase. Cat No: EXWM-4356. | |
| flavivirin | Known from classical flaviviruses (yellow fever, dengue fever). The functional viral peptidase is part of the NS2B protein. Catalytic His, Asp and Ser residues are arranged as in chymotrypsin, but flavivrin is the type example of peptidase family S7. Group: Enzymes. Synonyms: Yellow fever virus (flavivirus) protease; NS2B-3 proteinase. Enzyme Commission Number: EC 3.4.21.91. CAS No. 154215-26-6. 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-4183; flavivirin; EC 3.4.21.91; 154215-26-6; Yellow fever virus (flavivirus) protease; NS2B-3 proteinase. Cat No: EXWM-4183. | |
| furin | One of a group of peptidases in peptidase family S8 (subtilisin family) that is structurally and functionally similar to kexin. All are activated by Ca2+, contain Cys near the active site His, and are inhibited by p-mercuribenzoate. At least three related enzymes are recognized in mammals: PC2, PC3 and PC4, which have somewhat different specificities. Group: Enzymes. Synonyms: prohormone convertase; dibasic processing enzyme; PACE; paired basic amino acid cleaving enzyme; paired basic amino acid converting enzyme; serine proteinase PACE; PC1; SPC3; proprotein convertase. Enzyme Commission Number: EC 3.4.21.75. CAS No. 141760-45-4. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4167; furin; EC 3.4.21.75; 141760-45-4; prohormone convertase; dibasic processing enzyme; PACE; paired basic amino acid cleaving enzyme; paired basic amino acid converting enzyme; serine proteinase PACE; PC1; SPC3; proprotein convertase. Cat No: EXWM-4167. | |
| Furin from Human, Recombinant | Furin is a dibasic endoprotease that is localized in the Golgi apparatus. It is responsible for the proteolytic maturation of many precursor proteins in the secretory and endocytic pathways of mammalian cells. Furin is a dibasic endoprotease that is localized in the Golgi apparatus. It has a molecular mass of 52.7 kDa. It is responsible for the proteolytic maturation of many precursor proteins in the secretory and endocytic pathways of mammalian cells. Furin cleaves precursor proteins at their paired basic amino acid processing sites. Some substrates of furin include von Willebrand factor, transforming growth factor beta 1 precursor, pro-beta-secretase and proparathyroid hormo...terial exotoxins, typically at sites marked by the consensus sequence arg-xaa-(lys/arg)-arg. Group: Enzymes. Synonyms: furin; prohormone convertase; dibasic processing enzyme; PACE; paired basic amino acid cleaving enzyme; paired basic amino acid converting enzyme; serine proteinase PACE; PC1; SPC3; proprotein convertase. Furin. Activity: > 2,000 unit/mL. Storage: -70°C. Form: buffered aqueous solution. Source: Baculovirus infected Sf9 cells. Species: Human. furin; prohormone convertase; dibasic processing enzyme; PACE; paired basic amino acid cleaving enzyme; paired basic amino acid converting enzyme; serine proteinase PACE; PC1; SPC3; proprotein convertase. Cat No: NATE-0268. | |
| Gabexate mesylate | Gabexate mesylate (FOY) is is a competitive and non-antigenic synthetic inhibitor of trypsin-like serine proteinases. Gabexate mesylate inhibits human thrombin, urokinase, plasmin, and Factor Xa with K i s of 0.97, 1.3, 1.6, and 8.5 μM, respectively. Gabexate mesylate binds to human and bovine tryptase with K i s of 3.4 nM and 18 μM, respectively. Gabexate mesylate exerts an anticoagulant effect on the clotting activity of thrombin and has anti-inflammatory effect by viainhibition of NF-κB, proinflammatory cytokines, and nitric oxide. Gabexate mesylate is used for pancreatitis and disseminated intravascular coagulation [1] [2] [3] [4]. Uses: Scientific research. Group: Signaling pathways. Alternative Names: FOY. CAS No. 56974-61-9. Pack Sizes: 10 mM * 1 mL; 5 mg; 10 mg; 25 mg; 50 mg; 100 mg. Product ID: HY-B0385. | |
| gingipain K | Activity is stimulated by glycine. Known from the bacterium Porphyromonas gingivalis and contributes to the pathogenicity of the organism. In peptidase family C25. Group: Enzymes. Synonyms: Lys-gingipain; PrtP proteinase. Enzyme Commission Number: EC 3.4.22.47. CAS No. 159745-69-4. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4222; gingipain K; EC 3.4.22.47; 159745-69-4; Lys-gingipain; PrtP proteinase. Cat No: EXWM-4222. | |
| Granzyme B from Human, Recombinant | Granzyme B is a component of the cytolytic granules of cytotoxic T lymphocytes and natural killer cells. Group: Enzymes. Synonyms: CTLA1; CCPII; cytotoxic cell proteinase-1; granzyme G; granzyme H; CCP1 proteinase; GzmB. Enzyme Commission Number: EC 3.4.21.79. CAS No. 143180-74-9. Purity: Partially purified by single-step affinity chromatography and gel filtration. Granzyme B. Mole weight: 25.4 kDa. Storage: -80°C. Form: Liquid. In 50mM TRIS, pH 7.4, 100mM NaCl, 10% glycerol. Source: Yeast. Species: Human. granzyme B; CTLA1; CCPII; cytotoxic cell proteinase-1; granzyme G; granzyme H; CCP1 proteinase; GzmB; EC 3.4.21.79. Cat No: NATE-1622. | |
| Granzyme B from Mouse, Recombinant | Granzyme B, a 247 amino acid polypeptide, contains a leader sequence, which is cleaved by a signal peptidase and a two amino acid prodomain, which is cleaved by the lysosomal cysteine protease DPPI. The recombinant granzyme B is expressed in Pichia pastoris as the mature form and appears on SDS-PAGE as a triplet (~34, 32, and 30 kDa) due to three different glycosylations. Granzyme B, a serine protease, is the most prominent granzyme in a family of 11 found in the cytotoxic granules. The granzymes enter the target cell with the assistance of perforin, a critical molecule of the cytotoxic granules. In the target cell, the granzymes act on specific substrates involved with the cell death via apoptosis. > 90% (sds-page), recombinant, expressed in pichia pastoris, buffered aqueous solution. pichia expressed recombinant granzyme b has the advantage over native granzyme b as the latter can be purified only in limited amounts, and over e. coli and vaccinia virus expressed enzymes that failed to generate soluble active enzyme. Group: Enzymes. Synonyms: g. CAS No. 143180-74-9. Granzyme B. Mole weight: 28.9 kDa. Activity: > 10,000 units/mg protein. Storage: -70°C. Form: buffered aqueous solution. Source: Pichia pastoris. Species: Mouse. granzyme B; CTLA1; CCPII; cytotoxic cell proteinase-1; granzyme G; granzyme H; CCP1 proteinase; GzmB. Cat No: NATE-0333. | |
| Granzyme H from Human, Recombinant (carrier-free) | Granzyme H is a member of the granzyme family of serine proteases found specifically in the cytotoxic granules of cytotoxic T lymphocytes (CTL) and natural killer (NK) cells. Granzyme Hs functions are largely unknown. The more abundant expression of Granzyme H than Granzyme B in NK cells suggests that Granzyme H may complement the pro-apoptotic function of Granzyme B in this cell type. Group: Enzymes. Synonyms: Granzyme H; GZMH; Granzyme. Enzyme Commission Number: EC 3.4.21.-. Purity: >95%, by SDS-PAGE under reducing conditions and visualized by silver stain. Alkalophilic proteinase. Mole weight: Multiple bands between 38-40 kDa, reducing conditions by SDS-PAGE. Activity: >5,000 pmol/min/ug. Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.6 months from date of receipt, -70 °C as supplied.3 months, -70 °C under sterile conditions after opening. Form: Supplied as a 0.2 μm filtered solution in HEPES, NaCl and Brij-35. Source: Mouse myeloma cell line. Species: Human. Granzyme H; GZMH; Granzyme. Cat No: NATE-1935. | |
| Granzyme K from Human, Recombinant | Granzyme K is a protein that in humans is encoded by the GZMK gene. This gene product is a member of a group of related serine proteases from the cytoplasmic granules of cytotoxic lymphocytes. Cytolytic T lymphocytes (CTL) and natural killer (NK) cells share the remarkable ability to recognize, bind, and lyse specific target cells. They are thought to protect their host by lysing cells bearing on their surface 'nonself' antigens, usually peptides or proteins resulting from infection by intracellular pathogens. The protein described here lacks consensus sequences for N-glycosylation present in other granzymes. Group: Enzymes. Synonyms: Granzyme K; GZMK; GZMK. Enzyme Commission Number: EC 3.4.21.-. Purity: >98% (SDS-PAGE). Alkalophilic proteinase. Activity: ~29 U/ug protein. Stability: Stable for at least 6 months when stored at -80°C. Dilute solutions (e. g. 1-1000ng/ml) should be used within 24 hours. Storage: at -80°C. Form: Liquid. In PBS containing 10% sucrose and ~0.5M sodium chloride. Contains no preservatives. Source: E. coli. Species: Human. Granzyme K; GZMK; GZMK. Cat No: NATE-1936. | |
| helper-component proteinase | Known from many potyviruses. The helper component-proteinase of the tobacco etch virus is a multifunctional protein with several known activities: the N-terminal region is required for aphid transmission and efficient genome amplification, the central region is required for long-distance movement in plants, and the C-terminal domain has cysteine endopeptidase activity. Type example of peptidase family C6. Group: Enzymes. Synonyms: HC-Pro. Enzyme Commission Number: EC 3.4.22.45. CAS No. 124566-20-7. 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-4220; helper-component proteinase; EC 3.4.22.45; 124566-20-7; HC-Pro. Cat No: EXWM-4220. | |
| HIV-1 retropepsin | Present in human immunodeficiency virus type 1. Contributes to the maturation of the viral particle, and is a target of antiviral drugs. Active enzyme is a dimer of identical 11-kDa subunits. Similar enzymes occur in other retroviruses. Type example of peptidase family A2. Group: Enzymes. Synonyms: human immunodeficiency virus type 1 protease; gag protease; HIV aspartyl protease; HIV proteinase; retroproteinase; HIV-1 protease; HIV-2 protease. Enzyme Commission Number: EC 3.4.23.16. CAS No. 144114-21-6. HIV 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-4253; HIV-1 retropepsin; EC 3.4.23.16; 144114-21-6; human immunodeficiency virus type 1 protease; gag protease; HIV aspartyl protease; HIV proteinase; retroproteinase; HIV-1 protease; HIV-2 protease. Cat No: EXWM-4253. | |
| HIV Protease Mutant, Recombinant | HIV-1 protease is a retroviral aspartyl protease (retropepsin) that is essential for the life-cycle of HIV, the retrovirus that causes AIDS. HIV protease cleaves newly synthesized polyproteins at the appropriate places to create the mature protein components of an infectious HIV virion. Without effective HIV protease, HIV virions remain uninfectious. Thus, mutation of HIV protease's active site or inhibition of its activity disrupts HIVs ability to replicate and infect additional cells, making HIV protease inhibition the subject of considerable pharmaceutical research. Group: Enzymes. Synonyms: human immunodeficiency virus type 1 protease; gag protease; HIV aspartyl protease; HIV proteinase; retroproteinase; HIV-1 protease; HIV-2 protease; HIV-1 retropepsin; HIV Protease Mutant; EC 3.4.23.16. Enzyme Commission Number: EC 3.4.23.16. CAS No. 144114-21-6. HIV Protease. Mole weight: mol wt ~10.8 kDa. Storage: -70°C. Form: Supplied as a solution in 0.5M Sodium Acetate, pH 4.7with 50mM Tris-HCL, 1M NaCL, 1mM EDTA, 5mM DTT and 15% glycerol. Source: E. coli. human immunodeficiency virus type 1 protease; gag protease; HIV aspartyl protease; HIV proteinase; retroproteinase; HIV-1 protease; HIV-2 protease; HIV-1 retropepsin; HIV Protease Mutant; EC 3.4.23.16. Pack: 100 unit vial containing > 100ug protein. Cat No: NATE-0344. | |
| horrilysin | A 56 kDa hemorrhagic endopeptidase from the venom of the timber rattlesnake (Crotalus horridus horridus) that cleaves basement membrane, hide powder and fibrinogen. Group: Enzymes. Synonyms: Crotalus horridus metalloendopeptidase; hemorrhagic proteinase IV; Crotalus horridus horridus venom hemorrhagic proteinase. Enzyme Commission Number: EC 3.4.24.47. CAS No. 84056-81-5. 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-4329; horrilysin; EC 3.4.24.47; 84056-81-5; Crotalus horridus metalloendopeptidase; hemorrhagic proteinase IV; Crotalus horridus horridus venom hemorrhagic proteinase. Cat No: EXWM-4329. | |
| IgA-specific metalloendopeptidase | A 190 kDa enzyme found in several pathogenic species of Streptococcus such as sanguis and pneumoniae. Type example of peptidase family M26. There is also an IgA-specific prolyl endopeptidase of the serine-type (see EC 3.4.21.72, IgA-specific serine endopeptidase). Group: Enzymes. Synonyms: immunoglobulin A1 proteinase; IgA protease; IgA1-specific proteinase; IgA1 protease; IgA1 proteinase. Enzyme Commission Number: EC 3.4.24.13. CAS No. 72231-73-3. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4294; IgA-specific metalloendopeptidase; EC 3.4.24.13; 72231-73-3; immunoglobulin A1 proteinase; IgA protease; IgA1-specific proteinase; IgA1 protease; IgA1 proteinase. Cat No: EXWM-4294. | |
| insulysin | A 110 kDa cytosolic enzyme, known from mammals and the fruit fly, Drosophila melanogaster. Inhibited by bacitracin, chelating agents EDTA and 1,10-phenanthroline, and by thiol-blocking reagents such as N-ethylmaleimide, but not by phosphoramidon. In peptidase family M16 (pitrilysin family). Group: Enzymes. Synonyms: insulinase; insulin-degrading enzyme; insulin protease; insulin proteinase; insulin-degrading neutral proteinase; insulin-specific protease; insulin-glucagon protease; metalloinsulinase; IDE. Enzyme Commission Number: EC 3.4.24.56. CAS No. 9013-83-6. IDE. 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-4338; insulysin; EC 3.4.24.56; 9013-83-6; insulinase; insulin-degrading enzyme; insulin protease; insulin proteinase; insulin-degrading neutral proteinase; insulin-specific protease; insulin-glucagon protease; metalloinsulinase; IDE. Cat No: EXWM-4338. | |
| jararhagin | Hemorrhagic endopeptidase from the venom of the jararaca snake (Bothrops jararaca). The 52-kDa enzyme contains a disintegrin domain. In peptidase family M12 (astacin family). Group: Enzymes. Synonyms: HF2-proteinase; JF1. Enzyme Commission Number: EC 3.4.24.73. CAS No. 160477-79-2. 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-4357; jararhagin; EC 3.4.24.73; 160477-79-2; HF2-proteinase; JF1. Cat No: EXWM-4357. | |
| kallikrein 13 | The enzyme is specific for prorenin from the mouse submandibular gland, as prorenin from the mouse kidney (Ren1) and human prorenin are not substrates. Site-directed mutagenesis studies have shown that the enzyme will also cleave prorenin when Lys-Arg is replaced by Arg-Arg or Gln-Arg but the rate of reaction is much slower when Lys-Lys is used. This enzyme is also able to process pro-interleukin-1β (pro-IL-1β) in mouse submandibular gland to form IL-1&beta. Belongs in peptidase family S1A. Group: Enzymes. Synonyms: KLK13; kallikrein mK13; mGK-13; mK13; mKLK13; prorenin converting enzyme 1; PRECE-1; prorenin-converting enzyme; PRECE; proteinase P. Enzyme Commission Number: EC 3.4.21.119. CAS No. 342900-44-1. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4114; kallikrein 13; EC 3.4.21.119; 342900-44-1; KLK13; kallikrein mK13; mGK-13; mK13; mKLK13; prorenin converting enzyme 1; PRECE-1; prorenin-converting enzyme; PRECE; proteinase P. Cat No: EXWM-4114. | |
| 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. | |
| legumain | Best known from legume seeds, the trematode Schistosoma mansoni and mammalian lysosomes. Not inhibited by compound E-64. Type example of peptidase family C13. Group: Enzymes. Synonyms: asparaginyl endopeptidase; citvac; proteinase B (ambiguous); hemoglobinase (ambiguous); PRSC1 gene product (Homo sapiens); vicilin peptidohydrolase; bean endopeptidase; vicilin peptidohydrolase. Enzyme Commission Number: EC 3.4.22.34. CAS No. 149371-18-6. 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-4209; legumain; EC 3.4.22.34; 149371-18-6; asparaginyl endopeptidase; citvac; proteinase B (ambiguous); hemoglobinase (ambiguous); PRSC1 gene product (Homo sapiens); vicilin peptidohydrolase; bean endopeptidase; vicilin peptidohydrolase. Cat No: EXWM-4209. | |
| 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. | |
| L-Valine chloromethyl ketone hydrochloride | L-Valine chloromethyl ketone hydrochloride acts as a reagent in the preparation of tetrapeptidyl chloromethyl ketones, which are potent inhibitors of proteinase K. Synonyms: L-Val-CMK HCl; H-Val CH2Cl HCl; H-L-Val-CMK HCl; (3S)-3-amino-1-chloro-4-methylpentan-2-one hydrochloride; L Val CMK HCl; H L Val CMK HCl. Grades: ≥ 97%. CAS No. 107831-79-8. Molecular formula: C6H12ClNO·HCl. Mole weight: 186.10. | |
| magnolysin | An endopeptidase of 58 kDa known from bovine pituitary neurosecretory granules and bovine and human corpus luteum. Inhibited by EDTA. Group: Enzymes. Synonyms: bovine neurosecretory granule protease cleaving pro-oxytocin/neurophysin; pro-oxytocin/neurophysin convertase; prooxyphysin proteinase; pro-oxytocin convertase. Enzyme Commission Number: EC 3.4.24.62. CAS No. 162875-09-4. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4345; magnolysin; EC 3.4.24.62; 162875-09-4; bovine neurosecretory granule protease cleaving pro-oxytocin/neurophysin; pro-oxytocin/neurophysin convertase; prooxyphysin proteinase; pro-oxytocin convertase. Cat No: EXWM-4345. | |
| matrilysin | Found in rat uterus; at 19 kDa, the smallest member of peptidase family M10 (interstitial collagenase family). Similar in specificity to stromelysin, but more active on azocoll. Group: Enzymes. Synonyms: matrin; uterine metalloendopeptidase; matrix metalloproteinase 7; putative (or punctuated) metalloproteinase-1; matrix metalloproteinase pump 1; MMP 7; PUMP-1 proteinase; PUMP; metalloproteinase pump-1; putative metalloproteinase; MMP. Enzyme Commission Number: EC 3.4.24.23. CAS No. 141256-52-2. 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-4304; matrilysin; EC 3.4.24.23; 141256-52-2; matrin; uterine metalloendopeptidase; matrix metalloproteinase 7; putative (or punctuated) metalloproteinase-1; matrix metalloproteinase pump 1; MMP 7; PUMP-1 proteinase; PUMP; metalloproteinase pump-1; putative metalloproteinase; MMP. Cat No: EXWM-4304. | |
| Metalloproteinase from Staphylococcus aureus | A metalloproteinase, or metalloprotease, is any protease enzyme whose catalytic mechanism involves a metal. An example of this would be meltrin which plays a significant role in the fusion of muscle cells during embryo development, in a process known as myogenesis. Most metalloproteases require zinc, but some use cobalt. The metal ion is coordinated to the protein via three ligands. The ligands co-ordinating the metal ion can vary with histidine, glutamate, aspartate, lysine, and arginine. The fourth coordination position is taken up by a labile water molecule. Treatment with chelating agents such as EDTA leads to complete inactivation. EDTA is a metal chelator that rem...tial for activity. They are also inhibited by the chelator orthophenanthroline. Applications: Enzyme used for structural and enzymological studies. specificity similar to that of thermolysin with preference to hydrophobic p1' residues. Group: Enzymes. Synonyms: Aureolysin. Enzyme Commission Number: EC 3.4.24.29. CAS No. 39335-13-2. Purity: > 95 % (SDS-PAGE). Metalloproteinase. Mole weight: 28000. Storage: at -15 °C to -25 °C. Form: Lyophilized from 20 mM Tris/HCl pH 7.8, containing 5-10 mM CaCl2. Source: Staphylococcus aureus. Aureolysin; EC 3.4.24.29; Metalloproteinase; Staphylococcus aureus neutral proteinase; Staphylococcus aureus neutral protease. Cat No: NATE-1617. | |
| microbial collagenase | Six species of metalloendopeptidase acting on native collagen can be isolated from the medium of Clostridium histolyticum. Class I has forms α (68 kDa), β (115 kDa) and γ (79 kDa); class II has Δ (100 kDa), ε (110 kDa) and ζ (125 kDa). The two classes are immunologically crossreactive, but have significantly different sequences, and different specificities such that their actions on collagen are complementary. The enzymes also act as peptidyl-tripeptidases. Variants of the enzyme have been purified from Bacillus cereus, Empedobacter collagenolyticum, Pseudomonas marinoglutinosa, and species of Vibrio, Vibrio B-30 (ATCC 21250) and V. alginolyticu...ase-8; matirx metalloproteinase-18; interstitial collagenase. Enzyme Commission Number: EC 3.4.24.3. CAS No. 9001-12-1. Collagenase. 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-4311; microbial collagenase; EC 3.4.24.3; 9001-12-1; Clostridium histolyticum collagenase; clostridiopeptidase A; collagenase A; collagenase I; Achromobacter iophagus collagenase; collagenase; aspergillopeptidase C; nucleolysin; azocollase; metallocollagenase; soycollagestin; Clostridium histolyticum proteinase A; clostridiopeptidase II; MMP-8; clostridiopeptidase I; collagen peptidase; collagen protease; collagenase MM | |
| mitochondrial processing peptidase | Known from the mitochondrial matrix of fungi and mammals. Formed from two subunits, both homologous with pitrilysin, and the products of the MAS1 and MAS2 genes in yeast. In peptidase family M16 (pitrilysin family). Group: Enzymes. Synonyms: processing enhancing peptidase (for one of two subunits); mitochondrial protein precursor-processing proteinase; matrix peptidase; matrix processing peptidase; matrix processing proteinase; mitochondrial protein precursor-processing proteinase; MPP. Enzyme Commission Number: EC 3.4.24.64. CAS No. 86280-61-7. 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-4347; mitochondrial processing peptidase; EC 3.4.24.64; 86280-61-7; processing enhancing peptidase (for one of two subunits); mitochondrial protein precursor-processing proteinase; matrix peptidase; matrix processing peptidase; matrix processing proteinase; mitochondrial protein precursor-processing proteinase; MPP. Cat No: EXWM-4347. | |
| Native Aspergillus melleus Proteinase | A protease (also called peptidase or proteinase) is any enzyme that performs proteolysis, that is, begins protein catabolism by hydrolysis of the peptide bonds that link amino acids together in a polypeptide chain. Proteases have evolved multiple times, and different classes of protease can perform the same reaction by completely different catalytic mechanisms. Proteases can be found in animals, plants, bacteria, archaea and viruses. Applications: Proteinase is an enzyme used to break down proteins by hydrolyzing peptide bonds. proteinase is used to degrade proteins, to study proteinase inhibitors and to study thermal inactivation kinetics. proteinase is used in nucleic acid isolation procedures in incubations. it is used to study proteinase-activated receptors, such as the transducers of proteinase-mediated signaling in inflammation and the immune response. it is from aspergillus melleus and has been used to non-specifically degraded xylanase from streptomyces halstedii. Group: Enzymes. Synonyms: Protease; peptidase; proteinase; 9001-92-7. CAS No. 9001-92-7. Proteinase. Activity: > 3 units/mg solid. Storage: 2-8°C. Source: Aspergillus melleus. Protease; peptidase; proteinase; 9001-92-7. Cat No: NATE-0638. | |
| 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 Proteinase | Proteinase catabolizes proteins by hydrolysis of peptide bonds. Proteases are inactivated by serine active-site inhibitors, such as phenylmethylsulfonyl fluoride (PMSF) and diisopropylfluorophosphate. Subtilisin is a non-glycosylated single polypeptide chain without disulfide bonds and has a molecular weight of 27 kda. Applications: The enzyme from creative enzymes has been used to optimize release of all mit ochondrial populations from homogenized ventricular tissue of rat heart. it has also been used in the pre-hybridisation treatment of formalin fixed, paraffin wax-embedded liver specimens for detecting human and viral dna. this is a proteolytic enzyme isolated from th...ls to study the silencing of cardiac mit ochondrial nhe1. Group: Enzymes. Synonyms: protease; peptidase; proteinase; EC 3.4.21.62; 9014-01-1; Alkaline Protease; Protease from Bacillus licheniformis; Proteinase from Bacillus licheniformis; Subtilo peptidase A. Enzyme Commission Number: EC 3.4.21.62. CAS No. 9001-92-7. Purity: crystallization. Proteinase. Mole weight: 27 KDa. Activity: 7.0-14.0 units/mg solid. Storage: -20°C. Form: lyophilized powder. Source: Bacillus licheniformis. protease; peptidase; proteinase; EC 3.4.21.62; 9014-01-1; Alkaline Protease; Protease from Bacillus licheniformis; Proteinase from Bacillus licheniformis; Subtilo peptidase A. Cat No: NATE-0639. | |
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