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| Product | Description | |
|---|---|---|
| 1,3-Bis-(Z-Leu-Leu)-diaminoacetone | 1,3-Bis-(Z-Leu-Leu)-diaminoacetone, a cysteine protease inhibitor, can specifically and efficiently inhibit the processing of p-Prl signal peptide (IC50 ca. 50 nM) without affecting the activity of signal peptidase and lysosomal cathepsin, proteasome, and other proteases. Synonyms: (Z-LL)2 Ketone; Z-Leu-Leu-NH-CH2-CO-CH2-NH-Leu-Leu-Z; 2,2'-(2-Oxo-1,3-propanediyl)bis[N-[(phenylmethoxy)carbonyl]-L-leucyl-L-leucinamide; 1,3-di-(N-carboxybenzoyl-leucyl-leucyl)aminoacetone; Dibenzyl [(4S,7S,15S,18S)-7,15-diisobutyl-2,20-dimethyl-5,8,11,14,17-pentaoxo-6,9,13,16-tetraazahenicosane-4,18-diyl]biscarbamate. Grades: ≥95%. CAS No. 313664-40-3. Molecular formula: C43H64N6O9. Mole weight: 809.00. |  |
| adenain | A cysteine endopeptidase from adenoviruses, the type example of peptidase family C5, with a protein fold unlike that known for any other peptidase. Activity is greatly stimulated by the binding to the enzyme of an 11-residue peptide from the adenovirus capsid protein pre-VI at a site separate from the active site. Group: Enzymes. Enzyme Commission Number: EC 3.4.22.39. CAS No. 369652-03-9. 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-4214; adenain; EC 3.4.22.39; 369652-03-9. Cat No: EXWM-4214. |  |
| calicivirin | Viruses that are members of the Norovirus genus (Caliciviridae family) are a major cause of epidemic acute viral gastroenteritis. The nonstructural proteins of these viruses are produced by proteolytic cleavage of a large precursor polyprotein, performed by a protease that is incorporated into the polyprotein.Cleavage sites are apparently defined by features based on both sequence and structure since several sites in the polyprotein fulfilling the identified sequence requirements are not cleaved. The presence of acidic (Asp), basic (Arg), aromatic (Tyr) or aliphatic (Leu) amino acids at the P1' position results in only minor differences in cleavage efficiency, suggesting that steric or...C-like protease; calicivirus endopeptidase; rabbit hemorrhagic disease virus 3C endopeptidase. Enzyme Commission Number: EC 3.4.22.66. 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-4242; calicivirin; EC 3.4.22.66; Camberwell virus processing peptidase; Chiba virus processing peptidase; Norwalk virus processing peptidase; Southampton virus processing peptidase; Southampton virus; norovirus virus processing peptidase; calicivirus trypsin-like cysteine protease; calicivirus TCP; calicivirus 3C-like protease; calicivirus endopeptidase; rabbit hemorrhagic disease virus 3C endopeptidase. Cat No: EXWM-4242. | |
| cathepsin L | A lysosomal enzyme in peptidase family C1 (papain family) that is readily inhibited by the diazomethane inhibitor Z-Phe-Phe-CHN2 or the epoxide inhibitor E-64. Group: Enzymes. Synonyms: Aldrichina grahami cysteine proteinase. Enzyme Commission Number: EC 3.4.22.15. CAS No. 60616-82-2. CTSL. 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-4195; cathepsin L; EC 3.4.22.15; 60616-82-2; Aldrichina grahami cysteine proteinase. Cat No: EXWM-4195. | |
| 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. | |
| cathepsin O | Cathepsin O is a lysosomal cysteine peptidase of family C1 (papain family). The recombinant human enzyme is catalytically active at pH 6.0 and is inhibited by compound E-64. Cathepsin O is ubiquitously expressed in human tissues and the human gene locus is 4q31-32. Group: Enzymes. Enzyme Commission Number: EC 3.4.22.42. CAS No. 162032-86-2. 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-4217; cathepsin O; EC 3.4.22.42; 162032-86-2. Cat No: EXWM-4217. | |
| cathepsin S | A lysosomal cysteine endopeptidase that is unusual amongst such enzymes for its stability to neutral pH. In peptidase family C1 (papain family). Group: Enzymes. Enzyme Commission Number: EC 3.4.22.27. CAS No. 71965-46-3. CTSS. 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-4201; cathepsin S; EC 3.4.22.27; 71965-46-3. Cat No: EXWM-4201. | |
| cathepsin X | Cathepsin X is a lysosomal cysteine peptidase of family C1 (papain family). The pH optimum is dependent on the substrate and is 5.0 for the carboxypeptidase activity. Unstable above pH 7.0. Compound E-64, leupeptin and antipain are inhibitors, but not cystatin C. Cathepsin X is ubiquitously distributed in mammalian tissues. The propeptide is extremely short (38 amino acid residues) and the proenzyme is catalytically active. Human gene locus: 20q13. Group: Enzymes. Synonyms: cathepsin B2; cysteine-type carboxypeptidase; cathepsin IV; cathepsin Z; acid carboxypeptidase; lysosomal carboxypeptidase B. Enzyme Commission Number: EC 3.4.18.1. CAS No. 37217-21-3. 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-4081; cathepsin X; EC 3.4.18.1; 37217-21-3; cathepsin B2; cysteine-type carboxypeptidase; cathepsin IV; cathepsin Z; acid carboxypeptidase; lysosomal carboxypeptidase B. Cat No: EXWM-4081. | |
| dipeptidyl-peptidase I | A Cl--dependent, lysosomal cysteine-type peptidase maximally active at acidic pH. Also polymerizes dipeptide amides, arylamides and esters at neutral pH. In peptidase family C1 (papain family). Group: Enzymes. Synonyms: cathepsin C; dipeptidyl aminopeptidase I; dipeptidyl transferase; cathepsin C; dipeptidyl transferase; dipeptide arylamidase I; DAP I. Enzyme Commission Number: EC 3.4.14.1. CAS No. 9032-68-2. CTSC. 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-4043; dipeptidyl-peptidase I; EC 3.4.14.1; 9032-68-2; cathepsin C; dipeptidyl aminopeptidase I; dipeptidyl transferase; cathepsin C; dipeptidyl transferase; dipeptide arylamidase I; DAP I. Cat No: EXWM-4043. | |
| ficain | The major proteolytic component of the latex of fig, Ficus glabrata. Cysteine endopeptidases with similar properties are present in other members of the large genus Ficus. In peptidase family C1 (papain family). Group: Enzymes. Synonyms: ficin; debricin; higueroxyl delabarre. Enzyme Commission Number: EC 3.4.22.3. CAS No. 9001-33-6. Ficin. 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-4204; ficain; EC 3.4.22.3; 9001-33-6; ficin; debricin; higueroxyl delabarre. Cat No: EXWM-4204. | |
| gingipain R | A secreted endopeptidase from the bacterium Porphyromonas gingivalis. Strongly activated by glycine, and stabilized by Ca2+. Precursor molecule contains a hemagglutinin domain. Misleadingly described in some literature as "trypsin-like", being a cysteine peptidase, type example of family C25. Group: Enzymes. Synonyms: Arg-gingipain; gingipain-1; argingipain; Arg-gingivain-55 proteinase; Arg-gingivain-70 proteinase; Arg-gingivain-75 proteinase; arginine-specific cysteine protease; arginine-specific gingipain; arginine-specific gingivain; RGP-1; RGP. Enzyme Commission Number: EC 3.4.22.37. CAS No. 159745-71-8. 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-4212; gingipain R; EC 3.4.22.37; 159745-71-8; Arg-gingipain; gingipain-1; argingipain; Arg-gingivain-55 proteinase; Arg-gingivain-70 proteinase; Arg-gingivain-75 proteinase; arginine-specific cysteine protease; arginine-specific gingipain; arginine-specific gingivain; RGP-1; RGP. Cat No: EXWM-4212. | |
| 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. | |
| 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. | |
| histolysain | From the protozoan, Entamoeba histolytica. In peptidase family C1 (papain family). Group: Enzymes. Synonyms: histolysin; histolysin; Entamoeba histolytica cysteine proteinase; amebapain; Entamoeba histolytica cysteine protease; Entamoeba histolytica neutral thiol proteinase. Enzyme Commission Number: EC 3.4.22.35. CAS No. 92228-52-9. 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-4210; histolysain; EC 3.4.22.35; 92228-52-9; histolysin; histolysin; Entamoeba histolytica cysteine proteinase; amebapain; Entamoeba histolytica cysteine protease; Entamoeba histolytica neutral thiol proteinase. Cat No: EXWM-4210. | |
| Immobilized Papain on G3m | Papain has wide specificity and degrades most protein substrates. Preferential cleavage: arg-, lys-, phe-X. Papain also has esterase activity. G3m: 25 ug (0.6 units) papain immobilized per CR-column on dextran. This CR-column digests at least 20 ug tubulin per application. Nr. 7 Storage buffer : 50 mM Tris/HCl, 4 mM EDTA, pH 7. 5Nr. 52 Reaction buffer: 50 mM phosphate, 4 mM EDTA, pH 6. 0Nr. 53 Washing buffer : 50 mM phosphate, 4 mM EDTA, 1 M NaCl, pH 6. 0The enzyme is more active in the presence of 3. 5 mM cysteine. Group: Enzymes. Synonyms: papayotin; summetrin; velardon; papaine; Papaya peptidase I; papain; EC 3. 4. 22. 2; 9001-73-4. Enzyme Commission Number: EC 3. 4. 22. 2. Storage: 4 °C. Source: Papaya latex. papayotin; summetrin; velardon; papaine; Papaya peptidase I; papain; EC 3. 4. 22. 2; 9001-73-4; Immobilized Papain. Cat No: NATE-1765. | |
| intermediate cleaving peptidase 55 | Icp55 removes the destabilizing N-terminal amino acid residues that are left after cleavage by the mitochondrial processing peptidase, leading to the stabilisation of the substrate. The enzyme can remove single amino acids or a short peptide, as in the case of cysteine desulfurase (EC 2.8.1.7), where three amino acids are removed. Group: Enzymes. Synonyms: Icp55; mitochondrial intermediate cleaving peptidase 55 kDa. Enzyme Commission Number: EC 3.4.11.26. 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-4023; intermediate cleaving peptidase 55; EC 3.4.11.26; Icp55; mitochondrial intermediate cleaving peptidase 55 kDa. Cat No: EXWM-4023. | |
| 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. | |
| Native Human Cathepsin H | Cathepsin H is a protein that in humans is encoded by the CTSH gene. The protein encoded by this gene is a lysosomal cysteine proteinase important in the overall degradation of lysosomal proteins. It is composed of a dimer of disulfide-linked heavy and light chains, both produced from a single protein precursor. The encoded protein, which belongs to the peptidase C1 protein family, can act both as an aminopeptidase and as an endopeptidase. Increased expression of this gene has been correlated with malignant progression of prostate tumors. Two transcript variants encoding different isoforms have been found for this gene. Group: Enzymes. Synonyms: CTSH; cathepsin H; CPSB; ACC-4; ACC-5; ACC4; ACC5; CPSB; minichain. Purity: > 95% (SDS-PAGE). CTSH. Mole weight: 28 kDa. Storage: -40°C. Form: Liquid. Source: Human Liver. Species: Human. CTSH; cathepsin H; CPSB; ACC-4; ACC-5; ACC4; ACC5; CPSB; minichain. Cat No: NATE-0176. | |
| Native Human Cathepsin L | Cathepsin L (EC 3.4.22.15, Aldrichina grahami cysteine proteinase) is an important lysosomal endopeptidase enzyme which is involved in the initiation of protein degradation. It is a member of the Peptidase C1 family, which play an important role in diverse processes including normal lysosome mediated protein turnover, antigen and proprotein processing, and apoptosis. Cathepsin L has been reported in many organisms including fish, birds and mammals. Applications: The most powerful of the lysosomal proteinases. it has a higher specific activity than cathepsin b and h in the degradation of a variety of physiological protein substrates. Group: Enzymes. Synonyms: cathepsin L; CTSL; EC 3.4.22.15; Aldrichina grahami cysteine proteinase; 60616-82-2. Enzyme Commission Number: EC 3.4.22.15. CAS No. 60616-82-2. CTSL. Activity: > 0.5 units/mg protein. Storage: -20°C. Form: Solution in in 20 mM malonate, pH 5.5, 1 mM EDTA, and 400 mM NaCl. Source: Human liver. Species: Human. cathepsin L; CTSL; EC 3.4.22.15; Aldrichina grahami cysteine proteinase; 60616-82-2. Cat No: NATE-0177. | |
| Native Papaya latex Papain | Papain papaya latex has antifungal activity against C. albicans. It is a cysteine protease that cleaves peptide bonds of basic amino acids, leucine, or glycine. Applications: Used to produce fab fragments of antibodies. also used for cell dissociation since it has been shown to be more effective and less damaging with certain tissues. papain from papaya latex, has been used to digest carotid artery smooth muscle cells. papain is used in dissecting solutions. it is used to produce fab fragments of antibodies. it is used for cell dissociation since it has been shown to be more effective and less damaging with certain tissues. Group: Enzymes. Synonyms: papayotin; summetrin; velardon; papaine; Papaya peptidase I; papain; EC 3.4.22.2; 9001-73-4. Enzyme Commission Number: EC 3.4.22.2. CAS No. 9001-73-4. Papain. Mole weight: 21 kDa. Activity: 0.5-2.0 units/mg solid; 1.5-10 units/mg solid; > 10 units/mg protein; 16-40 units/mg protein. Storage: -20°C. Form: lyophilized powder or buffered aqueous suspension, 2× Crystallized. Source: Papaya latex. papayotin; summetrin; velardon; papaine; Papaya peptidase I; papain; EC 3.4.22.2; 9001-73-4. Cat No: NATE-0506. | |
| Native Staphylococcus aureus Staphopain A | Staphopains A and B are part of the staphylococcal proteolytic cascade (SPC) and may contribute to tissue invasion and metastatic infections of Staphylococcus aureus. Staphopain A, along with Staphopain B, may contribute to septic shock through the release of bradykinin and S-kinin from human kininogens. This activity required proteolytically-active Staphopain A and was augmented by Staphopain B. Staphopain a is inhibited by staphostatin a, e-64, and heavy metal ions such as hg2+ and ag+. staphopain a is also inhibited by plasma α2-macroglobulin but not by human cystatin c. staphopain a and staphopain b, members of the peptidase c47 family, are the major cysteine proteases secreted by s. aureus. Applications: Staphopain a was used for cleaving the n terminus of atypical chemokine receptor (ackr2) to suppress its ligand internalization activity in a study on the pivotal role of ackr2 in ligand binding, internalization and scavenging of inflammatory responses. Group: Enzymes. Synonyms: Staphopain; EC 3.4.2. Enzyme Commission Number: EC 3.4.22.48. CAS No. 347841-89-8. Staphopain. Mole weight: mol wt ~20 kDa by SDS-PAGE. Storage: -20°C. Form: lyophilized powder. Source: Staphylococcus aureus. Staphopain; EC 3.4.22.48; staphylopain; 347841-89-8; ScpA; Staphopain A; Staphylococcal cysteine proteinase A; Staphylopain A. Cat No: NATE-0666. | |
| Native Staphylococcus aureus Staphopain B | Staphopains A and B are part of the staphylococcal proteolytic cascade (SPC) and may contribute to tissue invasion and metastatic infections of Staphylococcus aureus. Staphopain A, along with Staphopain B, may contribute to septic shock through the release of bradykinin and S-kinin from human kininogens. This activity required proteolytically-active Staphopain A and was augmented by Staphopain B. Staphopain activity is inhbited by staphostatin b (sspc) and e-64. staphopain activity is stimulated by edta. staphopain a and staphopain b, members of the peptidase c47 family, are the major cysteine proteases secreted by s. aureus. Group: Enzymes. Synonyms: Staphopain; EC 3.4.22.48; staphylopain; 347841-89-8; Staphopain B; Staphylococcal cysteine proteinase B; Staphylopain B; sspB. Enzyme Commission Number: EC 3.4.22.48. CAS No. 347841-89-8. Purity: > 95% (SDS-PAGE). Staphopain. Mole weight: mol wt ~20 kDa by SDS-PAGE. Storage: -20°C. Source: Staphylococcus aureus. Staphopain; EC 3.4.22.48; staphylopain; 347841-89-8; Staphopain B; Staphylococcal cysteine proteinase B; Staphylopain B; sspB. Cat No: NATE-0683. | |
| N-Ethylmaleimide | N-Ethylmaleimide (NEM) is a derivative of maleic acid and is used as a reagent for alkylation and covalent modification of nucleophilic thiol residues on proteins. It acts as an irreversible inhibitor of all cysteine peptidases that alkylates the active site thiol group of the enzymes. Uses: Used in cancer research; a sulfhydryl reagent that is widely used in experimental biochemical studies. Synonyms: NEM; 1-Ethyl-1H-pyrrole-2,5-dione; ethylmaleimide. Grades: >98.0%(HPLC)(N). CAS No. 128-53-0. Molecular formula: C6H7NO2. Mole weight: 125.13. | |
| oryzin | A peptidase of family S8 (subtilisin family), not containing cysteine, that is the predominant extracellular alkaline endopeptidase of the mold Aspergillus oryzae.Identical or closely related enzymes are produced by A. flavus and A. sojae. Group: Enzymes. Synonyms: Aspergillus alkaline proteinase; aspergillopeptidase B; API 21; aspergillopepsin B; aspergillopepsin F; Aspergillus candidus alkaline proteinase; Aspergillus flavus alkaline proteinase; Aspergillus melleus semi-alkaline proteinase;. Enzyme Commission Number: EC 3.4.21.63. CAS No. 9074-7-1. 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-4154; oryzin; EC 3.4.21.63; 9074-07-1; Aspergillus alkaline proteinase; aspergillopeptidase B; API 21; aspergillopepsin B; aspergillopepsin F; Aspergillus candidus alkaline proteinase; Aspergillus flavus alkaline proteinase; Aspergillus melleus semi-alkaline proteinase; Aspergillus oryzae alkaline proteinase; Aspergillus parasiticus alkaline proteinase; Aspergillus serine proteinase; Aspergillus sydowi alkaline proteinase; Aspergillus soya alkaline proteinase; Aspergillus melleus alkaline proteinase; Aspergillus sulphureus alkaline proteinase; prozyme; P 5380; kyorinase; seaprose S; semi-alkaline protease; sumizyme MP; prozyme 10; onoprose; onoprose SA; protease P; promelase. Cat No: EXWM-4154. | |
| Papain | Papain is a cysteine protease of the peptidase C1 family, which is used in food, pharmaceutical, textile, and cosmetic industries. Uses: Scientific research. Group: Natural products. CAS No. 9001-73-4. Pack Sizes: 100 mg. Product ID: HY-P1645. |  |
| picornain 3C | From entero-, rhino-, aphto- and cardioviruses. Larger than the homologous virus picornain 2A. Type example of peptidase family C3. Group: Enzymes. Synonyms: picornavirus endopeptidase 3C; poliovirus protease 3C; rhinovirus protease 3C; foot-and-mouth protease 3C; poliovirus proteinase 3C; rhinovirus proteinase 3C; coxsackievirus 3C proteinase; foot-and-mouth-disease virus proteinase 3C; 3C protease; 3C proteinase; cysteine proteinase 3C; hepatitis A virus 3C proteinase; protease 3C; tomato ringspot nepovirus 3C-related protease. Enzyme Commission Number: EC 3.4.22.28. CAS No. 97162-88-4. 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-4202; picornain 3C; EC 3.4.22.28; 97162-88-4; picornavirus endopeptidase 3C; poliovirus protease 3C; rhinovirus protease 3C; foot-and-mouth protease 3C; poliovirus proteinase 3C; rhinovirus proteinase 3C; coxsackievirus 3C proteinase; foot-and-mouth-disease virus proteinase 3C; 3C protease; 3C proteinase; cysteine proteinase 3C; hepatitis A virus 3C proteinase; protease 3C; tomato ringspot nepovirus 3C-related protease. Cat No: EXWM-4202. | |
| pyroglutamyl-peptidase I | A cysteine peptidase, known from bacteria, plants and animals. The enzyme from bacterial sources is used in protein sequencing, and is the type example of peptidase family C15. Group: Enzymes. Synonyms: 5-oxoprolyl-peptidase; pyrase; pyroglutamate aminopeptidase; pyroglutamyl aminopeptidase; L-pyroglutamyl peptide hydrolase; pyrrolidone-carboxyl peptidase; pyrrolidone-carboxylate peptidase; pyrrolidonyl peptidase; L-pyrrolidonecarboxylate peptidase; pyroglutamidase; pyrrolidonecarboxylyl peptidase. Enzyme Commission Number: EC 3.4.19.3. CAS No. 9075-21-2. Pyrase. 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-4088; pyroglutamyl-peptidase I; EC 3.4.19.3; 9075-21-2; 5-oxoprolyl-peptidase; pyrase; pyroglutamate aminopeptidase; pyroglutamyl aminopeptidase; L-pyroglutamyl peptide hydrolase; pyrrolidone-carboxyl peptidase; pyrrolidone-carboxylate peptidase; pyrrolidonyl peptidase; L-pyrrolidonecarboxylate peptidase; pyroglutamidase; pyrrolidonecarboxylyl peptidase. Cat No: EXWM-4088. | |
| saccharolysin | An 83 kDa cytoplasmic thiol-dependent metalloendopeptidase from Saccharomyces cerevisiae. In peptidase family M3 (thimet oligopeptidase family). Group: Enzymes. Synonyms: proteinase yscD; yeast cysteine proteinase D (Misleading); Saccharomyces cerevisiae proteinase yscD. Enzyme Commission Number: EC 3.4.24.37. CAS No. 96779-48-5. 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-4319; saccharolysin; EC 3.4.24.37; 96779-48-5; proteinase yscD; yeast cysteine proteinase D (Misleading); Saccharomyces cerevisiae proteinase yscD. Cat No: EXWM-4319. | |
| Ste24 endopeptidase | Type example of peptidase family M48. One of two enzymes that can catalyse this processing step for mating a-factor in yeast. Subsequently, the S-isoprenylated cysteine residue that forms the new C-terminus is methyl-esterified and forms a hydrophobic membrane-anchor. Group: Enzymes. Enzyme Commission Number: EC 3.4.24.84. CAS No. 148463-92-7. 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-4368; Ste24 endopeptidase; EC 3.4.24.84; 148463-92-7. Cat No: EXWM-4368. | |
| stem bromelain | The most abundant of the cysteine endopeptidases of the stem of the pineapple plant, Ananas comosus. Distinct from the bromelain found in the pineapple fruit (EC 3.4.22.33). Scarcely inhibited by chicken cystatin and also very slowly inactivated by E-64. In peptidase family C1 (papain family). Group: Enzymes. Synonyms: bromelain; pineapple stem bromelain. Enzyme Commission Number: EC 3.4.22.32. CAS No. 37189-34-7. Bromelain. 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-4207; stem bromelain; EC 3.4.22.32; 37189-34-7; bromelain; pineapple stem bromelain. Cat No: EXWM-4207. | |
| streptopain | From the bacterium, group A Streptococcus. Formed from the proenzyme by limited proteolysis. Type example of peptidase family C10. Group: Enzymes. Synonyms: Streptococcus peptidase A; streptococcal cysteine proteinase; Streptococcus protease. Enzyme Commission Number: EC 3.4.22.10. CAS No. 9025-51-8. 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-4193; streptopain; EC 3.4.22.10; 9025-51-8; Streptococcus peptidase A; streptococcal cysteine proteinase; Streptococcus protease. Cat No: EXWM-4193. | |
| subtilisin | Subtilisin is a serine endopeptidase, type example of peptidase family S8. It contains no cysteine residues (although these are found in homologous enzymes). Species variants include subtilisin BPN' (also subtilisin B, subtilopeptidase B, subtilopeptidase C, Nagarse, Nagarse proteinase, subtilisin Novo, bacterial proteinase Novo) and subtilisin Carlsberg (subtilisin A, subtilopeptidase A, alcalase Novo). Similar enzymes are produced by various Bacillus subtilis strains and other Bacillus species. Group: Enzymes. Synonyms: alcalase; alcala. Enzyme Commission Number: EC 3.4.21.62. CAS No. 9014-1-1. 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-4153; subtilisin; EC 3.4.21.62; 9014-01-1; alcalase; alcalase 0.6L; alcalase 2.5L; ALK-enzyme; bacillopeptidase A; bacillopeptidase B; Bacillus subtilis alkaline proteinase bioprase; bioprase AL 15; bioprase APL 30; colistinase; (see also comments); subtilisin J; subtilisin S41; subtilisin Sendai; subtilisin GX; subtilisin E; subtilisin BL; genenase I; esperase; maxatase; alcalase; thermoase PC 10; protease XXVII; thermoase; superase; subtilisin DY; subtilopeptidase; SP 266; savinase 8.0L; savinase 4.0T; kazusase; protease VIII; opticlean; Bacillus subtilis alkaline proteinase; protin A 3L; savinase; savinase 16.0L; savinase 32.0 L EX | |
| SUMO Protease 1 (GST-tagged) from Yeast, Recombinant | SUMO (Small Ubiquitin-like MOdifiers) Protease 1 (Ulp1, Ubl-specific protease 1 from Saccharomyces cerevisiae) is a highly active cysteine protease. It is highly specific as it recognizes the tertiary structure of the ubiquitin-like (UBL) protein, SUMO (Smt3), rather than its amino acid sequence. SUMO fusion tag, as an N-terminal fusion partner, has been shown to enhance functional protein production in prokaryotic and eukaryotic expression systems with significantly improved protein stability and solubility. The SUMO protease 1 can be used to cleave SUMO protein tag from recombinant SUMO-fusion proteins. The optimal temperature for cleavage is 30°C; however, the en...eaction by affinity chromatography using the Glutathione resin. Group: Enzymes. Synonyms: Ulp1 peptidase; SUMO Protease; SUMO Protease. Enzyme Commission Number: EC 3.4.22.68. Purity: > 90% by SDS-PAGE. Mole weight: 52.6 kDa (403-621 aa + N-terminal GST). Activity: >10,000 units/mg. Storage: Store at -80°C. Stable for at least 1 year as supplied. It may be further diluted to 0.1-0.5 mg/ml with 50 mM Tris-HCl, 100 mM NaCl, 5 mM DTT and 20% glycerol pH 8.0 and stored at -20°C in aliquots. Avoid repeated freezing and thawing cycles. Form: Liquid. Source: E. coli. Species: Yeast. Ulp1 peptidase; SUMO Protease; SUMO Protease; SUMO Protease 1; Protease. Cat No: NATE-1708. | |
| SUMO Protease 1 (His-tagged) from Yeast, Recombinant | SUMO (Small Ubiquitin-like MOdifiers) Protease 1 (Ulp1, Ubl-specific protease 1 from Saccharomyces cerevisiae) is a highly active cysteine protease. It is highly specific as it recognizes the tertiary structure of the ubiquitin-like (UBL) protein, SUMO (Smt3), rather than its amino acid sequence. SUMO fusion tag, as an N-terminal fusion partner, has been shown to enhance functional protein production in prokaryotic and eukaryotic expression systems with significantly improved protein stability and solubility. The SUMO Protease 1 can be used to cleave SUMO protein tag from recombinant SUMO-fusion proteins. The optimal temperature for cleavage is 30°C; however, the en...finity chromatography using the Ni chelating resin. Group: Enzymes. Synonyms: Ulp1 peptidase; SUMO Protease; SUMO Protease. Enzyme Commission Number: EC 3.4.22.68. Purity: > 90% by SDS-PAGE. Mole weight: 28.7 kDa (403-621 aa + N-terminal Poly-His tag). Activity: 1 X 10^6 units/mg. Storage: Store at -80°C. Stable for at least 1 year as supplied. It may be further diluted to 0.01-0.05 mg/ml with 50 mM Tris-HCl, 100 mM NaCl, 5 mM DTT and 20% glycerol pH 8.0 and stored at -20°C in aliquots. Avoid repeated freezing and thawing cycles. Form: Liquid. Source: E. coli. Species: Yeast. Ulp1 peptidase; SUMO Protease; SUMO Protease; SUMO Protease 1; Protease. Cat No: NATE-1709. | |
| Cilastatin sodium | Cilastatin sodium is the sodium salt of cilastatin, which is a dipeptidase inhibitor of renal enzyme dehydropeptidase-I and leukotriene D4 peptidase. It inhibits metabolism of LTD4 to LTE4 and the hydrolysis of β-lactam antibiotics. It reduces toxic accumulation of cyclosporin A in kidney proximal tubule epithelial cells. It can be combined intravenously with imipenem in order to protect it from dehydropeptidase. It suppresses both host and target metabolism of the broad-spectrum antibiotic imipenem, improving its efficacy. It usually confers antibiotic resistance to certain bacteria because itself does not have antibiotic activity. It has nephroprotective effects. Synonyms: L 642957; MK 791; L642957; MK791; L-642957; MK-791; [R-[R*,S*-(Z)]]-7-[(2-Amino-2-carboxyethyl)thio]-2-[[(2,2-dimethylcyclopropyl)carbonyl]amino]-2-heptenoic Acid Monosodium Salt; (2Z) ?-7- [ [ (2R) ?-2-Amino-2-carboxyethyl] ?thio] ?-2- [ [ [ (1S) ?-2, ?2-dimethylcyclopropyl] ?carbonyl] ?amino] ?-2-heptenoic Acid Sodium Salt; sodium S-((Z)-6-carboxy-6-((S)-2,2-dimethylcyclopropane-1-carboxamido)hex-5-en-1-yl)-L-cysteinate. Grades: ≥99% by HPLC. CAS No. 81129-83-1. Molecular formula: C16H25N2NaO5S. Mole weight: 380.43. | |
| membrane alanyl aminopeptidase | A zinc enzyme, not activated by heavy metal ions. Type example of peptidase family M1. Group: Enzymes. Synonyms: microsomal aminopeptidase; aminopeptidase M; aminopeptidase N; particle-bound aminopeptidase; amino-oligopeptidase; alanine aminopeptidase; membrane aminopeptidase I; pseudo leucine aminopeptidase; alanyl aminopeptidase; alanine-specific aminopeptidase; cysteinylglycine dipeptidase; cysteinylglycinase; L-alanine aminopeptidase; CD13. Enzyme Commission Number: EC 3.4.11.2. CAS No. 9054-63-1. 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-4016; membrane alanyl aminopeptidase; EC 3.4.11.2; 9054-63-1; microsomal aminopeptidase; aminopeptidase M; aminopeptidase N; particle-bound aminopeptidase; amino-oligopeptidase; alanine aminopeptidase; membrane aminopeptidase I; pseudo leucine aminopeptidase; alanyl aminopeptidase; alanine-specific aminopeptidase; cysteinylglycine dipeptidase; cysteinylglycinase; L-alanine aminopeptidase; CD13. Cat No: EXWM-4016. | |
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