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| Product | Description | |
|---|---|---|
| 6-Aminohexanoic acid (EACA) | 6-Aminohexanoic Acid is a reagent commonly used for the extraction of aldehydes from reaction mixtures. 6-Aminohexanoic Acid has also been shown to improve solubilization of membrane proteins in electrophoresis. Studies suggest that 6-Aminohexanoic Acid inhibits the activation of the first component of the complement system.EACA is reported to inhibit chymotrypsin, Factor VIIa, lysine carboxypeptidase, plasmin, and plasminogen activator. Lysine analog. Promotes rapid dissociation of plasmin, thereby inhibiting the activation of plasminogen and subsequent fibrinolysis. Reported to inhibit plasminogen binding to activated platelets. An early report indicated that it inhibits the activation of the first component of the complement system. Binds and inactivates Carboxypeptidase B. Group: Biochemicals. Alternative Names: 6-Amino-n-hexanoic Acid; 6-Aminocaproic Acid; 6-Aminohexanoic Acid; A 14719; ACS; Acepramin; Acepramine; Acikaprin; Afibrin; Amicar; Amikar; Aminokapron; CL 10304; CY 116; Caplamin; Capramol; Caprocid; Caprolisin; EACA; EACS; Epsamon; Epsicapron; Epsikapron; Epsilcapramin; Epsilon S; Hemocaprol; Hemopar; Hepin; Ipsilon; NSC 212532; NSC 26154; NSC 400230; Respramin; ε-Amino-n-caproic. Grades: Highly Purified. CAS No. 60-32-2. Pack Sizes: 500g, 1Kg. Molecular Formula: C6H13NO2, Molecular Weight: 131.17. US Biological Life Sciences. |  Worldwide |
| aminopeptidase S | Aminopeptidases are associated with many biological functions, including protein maturation, protein degradation, cell-cycle control and hormone-level regulation. This enzyme contains two zinc molecules in its active site and is activated by Ca2+. In the presence of Ca2+, the best substrates are Leu-Phe, Leu-Ser, Leu-pNA (aminoacyl-p-nitroanilide), Phe-Phe-Phe and Phe-Phe. Peptides with proline in the P1' position are not substrates. Belongs in peptidase family M28. Group: Enzymes. Synonyms: Mername-AA022 peptidase; SGAP; aminopeptidase (Streptomyces griseus); Streptomyces griseus aminopeptidase; S. griseus AP; double-zinc aminopeptidase. Enzyme Commission Number: EC 3.4.11.24. 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-4021; aminopeptidase S; EC 3.4.11.24; Mername-AA022 peptidase; SGAP; aminopeptidase (Streptomyces griseus); Streptomyces griseus aminopeptidase; S. griseus AP; double-zinc aminopeptidase. Cat No: EXWM-4021. |  |
| aminopeptidase Y | Requires Co2+; inhibited by Zn2+ and Mn2+. An enzyme best known from Saccharomyces cerevisiae that hydrolyses Lys-NHPhNO2 and, more slowly, Arg-NHPhNO2. Type example of peptidase family M28. Group: Enzymes. Synonyms: aminopeptidase Co; aminopeptidase (cobalt-activated); lysyl aminopeptidase. Enzyme Commission Number: EC 3.4.11.15. CAS No. 114796-97-3. 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-4011; aminopeptidase Y; EC 3.4.11.15; 114796-97-3; aminopeptidase Co; aminopeptidase (cobalt-activated); lysyl aminopeptidase. Cat No: EXWM-4011. | |
| anthrax lethal factor endopeptidase | From the bacterium Bacilus anthracis that causes anthrax. One of three proteins that are collectively termed anthrax toxin. Cleaves several MAP kinase kinases near their N-termini, preventing them from phosphorylating the downstream mitogen-activated protein kinases. In peptidase family M34. Group: Enzymes. Synonyms: lethal toxin. Enzyme Commission Number: EC 3.4.24.83. CAS No. 477950-41-7. 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-4367; anthrax lethal factor endopeptidase; EC 3.4.24.83; 477950-41-7; lethal toxin. Cat No: EXWM-4367. | |
| β-Ala-His dipeptidase | Present in the serum of humans and higher primates, but not in the serum of other mammals. Activated by Cd2+ and citrate. Belongs in peptidase family M20. Group: Enzymes. Synonyms: serum carnosinase. Enzyme Commission Number: EC 3.4.13.20. CAS No. 525589-43-9. 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-4034; β-Ala-His dipeptidase; EC 3.4.13.20; 525589-43-9; serum carnosinase. Cat No: EXWM-4034. | |
| calpain-1 | In peptidase family C2. Requires Ca2+ at micromolar concentrations for activity. Cytosolic in animal cells. The active enzyme molecule is a heterodimer in which the large subunit contains the peptidase unit, and the small subunit is also a component of EC 3.4.22.53, calpain-2. Group: Enzymes. Synonyms: μ-calpain; calcium-activated neutral protease I. Enzyme Commission Number: EC 3.4.22.52. CAS No. 78990-62-2. Calpain 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-4227; calpain-1; EC 3.4.22.52; 78990-62-2; μ-calpain; calcium-activated neutral protease I. Cat No: EXWM-4227. | |
| calpain-2 | Type example of peptidase family C2. Requires Ca2+ at millimolar concentrations for activity. Cytosolic in animal cells. The active enzyme molecule is a heterodimer in which the large subunit contains the peptidase unit, and the small subunit is also a component of EC 3.4.22.52, calpain-1. Group: Enzymes. Synonyms: calcium-activated neutral protease II; m-calpain; milli-calpain. Enzyme Commission Number: EC 3.4.22.53. CAS No. 702693-80-9. 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-4228; calpain-2; EC 3.4.22.53; 702693-80-9; calcium-activated neutral protease II; m-calpain; milli-calpain. Cat No: EXWM-4228. | |
| calpain-3 | This Ca2+-dependent enzyme is found in skeletal muscle and is genetically linked to limb girdle muscular dystrophy type 2A. The enzyme is activated by autoproteolytic cleavage of insertion sequence 1 (IS1),which allows substrates and inhibitors gain access to the active site. Substrates include the protein itself and connectin/titin. Belongs in peptidase family C2. Group: Enzymes. Synonyms: p94; calpain p94; CAPN3; muscle calpain;calpain 3; calcium-activated neutral proteinase 3; muscle-specific calcium-activated neutral protease 3; CANP 3; calpain L3. Enzyme Commission Number: EC 3.4.22.54. 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-4229; calpain-3; EC 3.4.22.54; p94; calpain p94; CAPN3; muscle calpain;calpain 3; calcium-activated neutral proteinase 3; muscle-specific calcium-activated neutral protease 3; CANP 3; calpain L3. Cat No: EXWM-4229. | |
| carboxypeptidase E | A zinc enzyme, activated by Co2+. Inhibited by 1,10-phenanthroline and other chelating agents. pH optimum 5.6. Located in storage granules of secretory cells, and active in processing of protein hormones and bioactive peptides. In peptidase family M14 (carboxypeptidase A family). Group: Enzymes. Synonyms: carboxypeptidase H; enkephalin convertase; cobalt-stimulated chromaffin granule carboxypeptidase; insulin granule-associated carboxypeptidase; enkephalin convertase; membrane-bound carboxypeptidase; carboxypeptidase E; enkephalin-precursor endopeptidase; enkephalin precursor carboxypeptidase; peptidyl-L-lysine(-L-arginine) hydrolase. Enzyme Commission Number: EC 3.4.17.10. CAS No. 81876-95-1. 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-4062; carboxypeptidase E; EC 3.4.17.10; 81876-95-1; carboxypeptidase H; enkephalin convertase; cobalt-stimulated chromaffin granule carboxypeptidase; insulin granule-associated carboxypeptidase; enkephalin convertase; membrane-bound carboxypeptidase; carboxypeptidase E; enkephalin-precursor endopeptidase; enkephalin precursor carboxypeptidase; peptidyl-L-lysine(-L-arginine) hydrolase. Cat No: EXWM-4062. | |
| carboxypeptidase U | Pro-carboxypeptidase U in (human) plasma is activated by thrombin or plasmin during clotting to form the unstable carboxypeptidase U, with activity similar to that of the more stable lysine carboxypeptidase, except that no preference is shown for Lys over Arg. A zinc enzyme, in peptidase family M14 (carboxypeptidase A family). Group: Enzymes. Synonyms: arginine carboxypeptidase; carboxypeptidase R; plasma carboxypeptidase B (misleading, since the term carboxypeptidase B is used for other enzymes); thrombin-activatable fibrinolysis inhibitor. Enzyme Commission Number: EC 3.4.17.20. CAS No. 156621-18-0. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4073; carboxypeptidase U; EC 3.4.17.20; 156621-18-0; arginine carboxypeptidase; carboxypeptidase R; plasma carboxypeptidase B (misleading, since the term carboxypeptidase B is used for other enzymes); thrombin-activatable fibrinolysis inhibitor. Cat No: EXWM-4073. | |
| caspase-2 | Caspase-2 is an initiator caspase, as are caspase-8 (EC 3.4.22.61), caspase-9 (EC 3.4.22.62) and caspase-10 (EC 3.4.22.63). Contains a caspase-recruitment domain (CARD) in its N-terminal prodomain, which plays a role in procaspase activation. Two forms of caspase-2 with antagonistic effects exist: caspase-2L induces programmed cell death and caspase-2S suppresses cell death. Caspase-2 is activated by caspase-3 (EC 3.4.22.56), or by a caspase-3-like protease. Activation involves cleavage of the N-terminal prodomain, followed by self-proteolysis between the large and small subunits of pro-caspase-2 and further proteolysis into smaller fragments. Proteolysis occurs at Asp residues and the ...s a substrate of the large isoform of pro-caspase-2 (caspase-2L) but not of the short isoform (caspase-2S). Belongs in peptidase family C14. Group: Enzymes. Synonyms: ICH-1; NEDD-2; caspase-2L; caspase-2S; neural precursor cell expressed developmentally down-regulated protein 2; CASP-2; NEDD2 protein. Enzyme Commission Number: EC 3.4.22.55. CAS No. 182372-14-1. 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-4230; caspase-2; EC 3.4.22.55; 182372-14-1; ICH-1; NEDD-2; caspase-2L; caspase-2S; neural precursor cell expressed developmentally down-regulated protein 2; CASP-2; NEDD2 protein. Cat No: EXWM-4230. | |
| caspase-3 | Caspase-3 is an effector/executioner caspase, as are caspase-6 (EC 3.4.22.59) and caspase-7 (EC 3.4.22.60). These caspases are responsible for the proteolysis of the majority of cellular polypeptides [e.g. poly(ADP-ribose) polymerase (PARP)], which leads to the apoptotic phenotype. Procaspase-3 can be activated by caspase-1 (EC 3.4.22.36), caspase-8 (EC 3.4.22.61), caspase-9 (EC 3.4.22.62) and caspase-10 (EC 3.4.22.63) as well as by the serine protease granzyme B. Caspase-3 can activate procaspase-2 (EC 3.4.22.55). Activation occurs by inter-domain cleavage followed by removal of the N-terminal prodomain. Although Asp-Glu-(Val/Ile)-Asp is thought to be the preferred cleavage sequence, the enzyme can accommodate different residues at P2 and P3 of the substrate. Like caspase-2, a hydrophobic residue at P5 of caspase-3 leads to more efficient hydrolysis, e.g. (Val/Leu)-Asp-Val-Ala-Asp? is a better substrate than Asp-Val-Ala-Asp?. This is not the case for caspase-7. Belongs in peptidase family C14. Group: Enzymes. Synonyms: CPP32; apopain; yama protein. Enzyme Commission Number: EC 3.4.22.56. CAS No. 169592-56-7. 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-4231; caspase-3; EC 3.4.22.56; 169592-56-7; CPP32; apopain; yama protein. Cat No: EXWM-4231. | |
| caspase-7 | Caspase-7 is an effector/executioner caspase, as are caspase-3 (EC 3.4.22.56) and caspase-6 (EC 3.4.22.59). These caspases are responsible for the proteolysis of the majority of cellular polypeptides [e.g. poly(ADP-ribose) polymerase (PARP)], which leads to the apoptotic phenotype. Although a hydrophobic residue at P5 of caspase-2 (EC 3.4.22.55) and caspase-3 leads to more efficient hydrolysis, the amino-acid residue at this location in caspase-7 has no effect. Caspase-7 is activated by the initiator caspases [caspase-8 (EC 3.4.22.61), caspase-9 (EC 3.4.22.62) and caspase-10 (EC 3.4.22.63)]. Removal of the N-terminal prodomain occurs before cleavage in the linker region between the large and small subunits. Belongs in peptidase family C14. Group: Enzymes. Synonyms: CASP-7; ICE-like apoptotic protease 3; ICE-LAP3; apoptotic protease Mch-3; Mch3; CMH-1. Enzyme Commission Number: EC 3.4.22.60. CAS No. 189258-14-8. 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-4236; caspase-7; EC 3.4.22.60; 189258-14-8; CASP-7; ICE-like apoptotic protease 3; ICE-LAP3; apoptotic protease Mch-3; Mch3; CMH-1. Cat No: EXWM-4236. | |
| caspase-9 | Caspase-9 is an initiator caspase, as are caspase -2 (EC 3.4.22.55), caspase-8 (EC 3.4.22.61) and caspase-10 (EC 3.4.22.63). Caspase-9 contains a caspase-recruitment domain (CARD) in its N-terminal prodomain, which plays a role in procaspase activation. An alternatively spliced version of caspase-9 also exists, caspase-9S, that inhibits apoptosis, similar to the situation found with caspase-2. Phosphorylation of caspase-9 from some species by Akt, a serine-threonine protein kinase, inhibits caspase activity in vitro and caspase activation in vivo. The activity of caspase-9 is increased dramatically upon association with the apoptosome but the enzyme can be activated without proteolytic cleavage. Procaspase-3 is the enzyme's physiological substrate. Belongs in peptidase family C14. Group: Enzymes. Synonyms: CASP-9; ICE-like apoptotic protease 6; ICE-LAP6; apoptotic protease Mch-6; apoptotic protease-activating factor 3; APAF-3. Enzyme Commission Number: EC 3.4.22.62. CAS No. 180189-96-2. 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-4238; caspase-9; EC 3.4.22.62; 180189-96-2; CASP-9; ICE-like apoptotic protease 6; ICE-LAP6; apoptotic protease Mch-6; apoptotic protease-activating factor 3; APAF-3. Cat No: EXWM-4238. | |
| coagulation factor IXa | A chymotrypsin homologue, and one of the γ-carboxyglutamic acid-containing blood coagulation factors. The proenzyme factor IX is activated by factor XIa. In peptidase family S1 (trypsin family). Group: Enzymes. Synonyms: activated Christmas factor; blood-coagulation factor IXa; activated blood-coagulation factor IX; autoprothrombin II; blood platelet cofactor II; activated blood coagulation factor XI. Enzyme Commission Number: EC 3.4.21.22. CAS No. 37316-87-3. 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-4122; coagulation factor IXa; EC 3.4.21.22; 37316-87-3; activated Christmas factor; blood-coagulation factor IXa; activated blood-coagulation factor IX; autoprothrombin II; blood platelet cofactor II; activated blood coagulation factor XI. Cat No: EXWM-4122. | |
| coagulation factor VIIa | Formed from the precursor factor VII. The cattle enzyme is more readily inhibited by diisopropyl fluorophosphate than the human. In peptidase family S1 (trypsin family). Group: Enzymes. Synonyms: blood-coagulation factor VIIa; activated blood coagulation factor VII. Enzyme Commission Number: EC 3.4.21.21. CAS No. 65312-43-8. 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-4121; coagulation factor VIIa; EC 3.4.21.21; 65312-43-8; blood-coagulation factor VIIa; activated blood coagulation factor VII. Cat No: EXWM-4121. | |
| coagulation factor XIa | In peptidase family S1 (trypsin family), and one of the γ-carboxyglutamic acid-containing blood coagulation factors. The proenzyme factor XI is activated by factor XIIa. Group: Enzymes. Synonyms: blood-coagulation factor XIa; activated blood-coagulation factor XI; activated plasma thromboplastin antecedent. Enzyme Commission Number: EC 3.4.21.27. CAS No. 37203-61-5. 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-4125; coagulation factor XIa; EC 3.4.21.27; 37203-61-5; blood-coagulation factor XIa; activated blood-coagulation factor XI; activated plasma thromboplastin antecedent. Cat No: EXWM-4125. | |
| coagulation factor XIIa | Also activates plasminogen and plasma prokallikrein. Formed from the proenzyme, factor XII, by plasma kallikrein or factor XIIa. In peptidase family S1 (trypsin family). Group: Enzymes. Synonyms: Hageman factor (activated); blood-coagulation factor XIIf; activated β blood-coagulation factor XII; prealbumin activator; Hageman factor β-fragment; Hageman factor fragment HFf; blood-coagulation factor XIIaβ; prekallikrein activator; kallikreinogen activator. Enzyme Commission Number: EC 3.4.21.38. CAS No. 75216-42-1. 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-4132; coagulation factor XIIa; EC 3.4.21.38; 75216-42-1; Hageman factor (activated); blood-coagulation factor XIIf; activated β blood-coagulation factor XII; prealbumin activator; Hageman factor β-fragment; Hageman factor fragment HFf; blood-coagulation factor XIIaβ; prekallikrein activator; kallikreinogen activator. Cat No: EXWM-4132. | |
| complement subcomponent C1r | Activated from proenzyme C1r in plasma during activation of the complement system by the "classical" route. In peptidase family S1 (trypsin family). Group: Enzymes. Synonyms: activated complement C1r; C1r esterase; activated complement C1r. Enzyme Commission Number: EC 3.4.21.41. CAS No. 80295-69-8. 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-4135; complement subcomponent C1r; EC 3.4.21.41; 80295-69-8; activated complement C1r; C1r esterase; activated complement C1r. Cat No: EXWM-4135. | |
| complement subcomponent C1s | Activated from proenzyme C1s in plasma by complement subcomponent C1r. In peptidase family S1 (trypsin family). Group: Enzymes. Synonyms: C1 esterase; activated complement C1s; complement C1r. Enzyme Commission Number: EC 3.4.21.42. CAS No. 80295-70-1. 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-4136; complement subcomponent C1s; EC 3.4.21.42; 80295-70-1; C1 esterase; activated complement C1s; complement C1r. Cat No: EXWM-4136. | |
| cytosol alanyl aminopeptidase | A puromycin-sensitive, Co2+-activated zinc-sialoglycoprotein that is generally cytosolic. Multiple forms are widely distributed in mammalian tissues and body fluids. In peptidase family M1 (membrane alanyl aminopeptidase family). Group: Enzymes. Synonyms: arylamidase; aminopolypeptidase; thiol-activated aminopeptidase; human liver aminopeptidase; puromycin-sensitive aminopeptidase; soluble alanyl aminopeptidase; cytosol aminopeptidase III; alanine aminopeptidase. Enzyme Commission Number: EC 3.4.11.14. CAS No. 243859-94-1. 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-4010; cytosol alanyl aminopeptidase; EC 3.4.11.14; 243859-94-1; arylamidase; aminopolypeptidase; thiol-activated aminopeptidase; human liver aminopeptidase; puromycin-sensitive aminopeptidase; soluble alanyl aminopeptidase; cytosol aminopeptidase III; alanine aminopeptidase. Cat No: EXWM-4010. | |
| cytosol nonspecific dipeptidase | A zinc enzyme with broad specificity, varying somewhat with source species. Activated and stabilized by dithiothreitol and Mn2+. Inhibited by bestatin and leucine. Group: Enzymes. Synonyms: N2-β-alanylarginine dipeptidase; glycyl-glycine dipeptidase; glycyl-leucine dipeptidase; iminodipeptidase; peptidase A; Pro-X dipeptidase; prolinase; prolyl dipeptidase; prolylglycine dipeptidase; iminodipeptidase; prolinase; L-prolylglycine dipe. Enzyme Commission Number: EC 3.4.13.18. CAS No. 9025-31-4. 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-4032; cytosol nonspecific dipeptidase; EC 3.4.13.18; 9025-31-4; N2-β-alanylarginine dipeptidase; glycyl-glycine dipeptidase; glycyl-leucine dipeptidase; iminodipeptidase; peptidase A; Pro-X dipeptidase; prolinase; prolyl dipeptidase; prolylglycine dipeptidase; iminodipeptidase; prolinase; L-prolylglycine dipeptidase; prolylglycine dipeptidase; diglycinase; Gly-Leu hydrolase; glycyl-L-leucine dipeptidase; glycyl-L-leucine hydrolase; glycyl-L-leucine peptidase; L-amino-acyl-L-amino-acid hydrolase; glycylleucine peptidase; glycylleucine hydrolase; glycylleucine dipeptide hydrolase; non-specific dipeptidase; human cytosolic non-specific dipeptidase; glycyl-L-leucine hydrolase; glycyl-glycine dipeptidase. Cat No: EXWM-4032. | |
| dipeptidyl-dipeptidase | A thiol-activated peptidase from cabbage (Brassica oleracea). Tetrapeptides are formed from Ala-Ala, Gly-Gly, Ala-Gly and Gly-Ala. Group: Enzymes. Synonyms: dipeptidyl tetrapeptide hydrolase; dipeptidyl ligase; tetrapeptide dipeptidase. Enzyme Commission Number: EC 3.4.14.6. CAS No. 91608-92-3. 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-4051; dipeptidyl-dipeptidase; EC 3.4.14.6; 91608-92-3; dipeptidyl tetrapeptide hydrolase; dipeptidyl ligase; tetrapeptide dipeptidase. Cat No: EXWM-4051. | |
| 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. | |
| gametolysin | A glycoprotein found in the periplasmic space of Chlamydomonas reinhardtii gametes in a 62 kDa inactive form; decreased to 60 kDa upon activation. A zinc enzyme, inhibited by phosphoramidon, but also thiol activated. Type example of peptidase family M11. Group: Enzymes. Synonyms: autolysin, Chlamydomonas cell wall degrading protease; lysin; Chlamydomonas reinhardtii metalloproteinase; gamete lytic enzyme; gamete autolysin. Enzyme Commission Number: EC 3.4.24.38. CAS No. 97089-74-2. 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-4320; gametolysin; EC 3.4.24.38; 97089-74-2; autolysin, Chlamydomonas cell wall degrading protease; lysin; Chlamydomonas reinhardtii metalloproteinase; gamete lytic enzyme; gamete autolysin. Cat No: EXWM-4320. | |
| 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. | |
| glutamyl aminopeptidase | Ca2+-activated and generally membrane-bound. A zinc-metallopeptidase in family M1 (membrane alanyl aminopeptidase family). Group: Enzymes. Synonyms: aminopeptidase A; aspartate aminopeptidase; angiotensinase A; glutamyl peptidase; Ca2+-activated glutamate aminopeptidase; membrane aminopeptidase II; antigen BP-1/6C3 of mouse B lymphocytes; L-aspartate aminopeptidase; angiotensinase A2. Enzyme Commission Number: EC 3.4.11.7. CAS No. 9074-83-3. 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-4028; glutamyl aminopeptidase; EC 3.4.11.7; 9074-83-3; aminopeptidase A; aspartate aminopeptidase; angiotensinase A; glutamyl peptidase; Ca2+-activated glutamate aminopeptidase; membrane aminopeptidase II; antigen BP-1/6C3 of mouse B lymphocytes; L-aspartate aminopeptidase; angiotensinase A2. Cat No: EXWM-4028. | |
| hepacivirin | Encoded by the genome of the viruses of the hepatitis C group, and contributes to the maturation of the precursor polyproteins. The enzyme is greatly activated by binding of the 54-residue NS4A 'cofactor' protein also derived from the viral polyprotein. Type example of peptidase family S29. The crystallographic structure shows a chymotrypsin-like fold. Group: Enzymes. Synonyms: Cpro-2; hepatitis C virus NS3 serine proteinase; NS3-4A serine proteinase complex. Enzyme Commission Number: EC 3.4.21.98. CAS No. 149885-80-3. 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-4190; hepacivirin; EC 3.4.21.98; 149885-80-3; Cpro-2; hepatitis C virus NS3 serine proteinase; NS3-4A serine proteinase complex. Cat No: EXWM-4190. | |
| kallikrein 8 | The enzyme is activated by removal of an N-terminal prepropeptide. The highest amidolytic activity is observed using Boc-Val-Pro-Arg?7-amido-4-methylcoumarin, which is a substrate of α-thrombin. Substrates lacking basic amino acids in the P1 position are not cleaved. The enzyme degrades casein, fibronectin, gelatin, collagen type IV, fibrinogen, and high-molecular-mass kininogen and is associated with diseases such as ovarian cancer and Alzheimer's disease. Belongs in peptidase family S1A. Group: Enzymes. Synonyms: KLK8; PRSS19; human kallikrein 8; hK8; mK8; ovasin; tumor-associated differentially expressed gene 14; TADG-14; NP; neuropsin. Enzyme Commission Number: EC 3.4.21.118. CAS No. 171715-15-4. 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-4113; kallikrein 8; EC 3.4.21.118; 171715-15-4; KLK8; PRSS19; human kallikrein 8; hK8; mK8; ovasin; tumor-associated differentially expressed gene 14; TADG-14; NP; neuropsin. Cat No: EXWM-4113. | |
| 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. | |
| leucyl aminopeptidase | A zinc enzyme isolated from pig kidney and cattle lens; activated by heavy metal ions. Type example of peptidase family M17. Group: Enzymes. Synonyms: leucine aminopeptidase; leucyl peptidase; peptidase S; cytosol aminopeptidase; cathepsin III; L-leucine aminopeptidase; leucinaminopeptidase; leucinamide aminopeptidase; FTBL proteins; proteinates FTBL; aminopeptidase II; aminopeptidase III; aminopeptidase I. Enzyme Commission Number: EC 3.4.11.1. CAS No. 9001-61-0. LAP. 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-4007; leucyl aminopeptidase; EC 3.4.11.1; 9001-61-0; leucine aminopeptidase; leucyl peptidase; peptidase S; cytosol aminopeptidase; cathepsin III; L-leucine aminopeptidase; leucinaminopeptidase; leucinamide aminopeptidase; FTBL proteins; proteinates FTBL; aminopeptidase II; aminopeptidase III; aminopeptidase I. Cat No: EXWM-4007. | |
| limulus clotting enzyme | From the hemocyte granules of horseshoe crabs Limulus and Tachypleus. Proclotting enzyme is activated by limulus clotting factor. In peptidase family S1 (trypsin family). Group: Enzymes. Synonyms: clotting enzyme. Enzyme Commission Number: EC 3.4.21.86. 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-4178; limulus clotting enzyme; EC 3.4.21.86; clotting enzyme. Cat No: EXWM-4178. | |
| limulus clotting factor B | From the hemocyte granules of the horseshoe crabs Limulus and Tachypleus. Factor B is activated by limulus clotting factor C. In peptidase family S1 (trypsin family). Group: Enzymes. Enzyme Commission Number: EC 3.4.21.85. CAS No. 848851-53-6. 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-4177; limulus clotting factor B; EC 3.4.21.85; 848851-53-6. Cat No: EXWM-4177. | |
| limulus clotting factor C | From the hemocyte granules of the horseshoe crabs Limulus and Tachypleus. Factor C is activated by Gram-negative bacterial lipopolysaccharides and chymotrypsin. Inhibited by antithrombin III. In peptidase family S1 (trypsin family). Group: Enzymes. Synonyms: factor C; limulus factor C. Enzyme Commission Number: EC 3.4.21.84. CAS No. 115743-27-6. 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-4176; limulus clotting factor C; EC 3.4.21.84; 115743-27-6; factor C; limulus factor C. Cat No: EXWM-4176. | |
| 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. | |
| meprin B | A brush border membrane-bound metalloendopeptidase known from the intestine of all mouse strains that have been tested, and the kidney of certain inbred strains. A tetramer of meprin β subunits (in contrast to meprin A, which contains both α and β subunits). Occurs in the kidney as a proenzyme that can be activated by trypsin. Meprin B is inhibited by both EDTA and 1,10-phenanthroline, but not by phosphoramidon, captopril or thiorphan. In peptidase family M12 (astacin family). Group: Enzymes. Synonyms: meprin-b. Enzyme Commission Number: EC 3.4.24.63. CAS No. 150679-52-0. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4346; meprin B; EC 3.4.24.63; 150679-52-0; meprin-b. Cat No: EXWM-4346. | |
| metallocarboxypeptidase D | Activated by Co2+; inhibited by guanidinoethylmercaptosuccinic acid. Large molecule (180 kDa) because of presence of three copies of metallopeptidase domain. The product of the silver gene (Drosophila) is similar. A zinc metallopeptidase in peptidase family M14 (carboxypeptidase A family). Group: Enzymes. Synonyms: carboxypeptidase D (cattle, human, mouse, rat); gp180 (duck). Enzyme Commission Number: EC 3.4.17.22. CAS No. 153967-26-1. 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-4075; metallocarboxypeptidase D; EC 3.4.17.22; 153967-26-1; carboxypeptidase D (cattle, human, mouse, rat); gp180 (duck). Cat No: EXWM-4075. | |
| 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 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. | |
| Native Bovine Factor X Activated (Xa) | Factor Xa catalyzes the hydrolysis of the Arg-Thr and then Arg-Ile bonds in prothrombin to yield active thrombin. The fairly strict recognition sequence is Ile-Glu (or Asp)-Gly-Arg-↓-X. It may sometimes cleave at other basic residues, depending on the conformation of the target protein. Factor Xa will not cleave if a proline residue follows the arginine of the recognition sequence. Factor xa is a serine endoproteinase and a member of the s1 peptidase family. factor xa plays a critical role in the coagulation cascade by catalyzing the proteolytic conversion of prothrombin to active thrombin. factor xa?s prothrombin conversion activity is greatly enhanced in vivo when c...d with 10 μg of factor xa for 2.5 hours at 37 oc. Group: Enzymes. Synonyms: EC 3.4.21.6; 9002-05-5; thrombokinase; prothrombase; prothrombinase; activated blood-coagulation factor X; autoprothrombin C; thromboplastin; plasma thromboplastin; factor Xa; activated Stuart-Prower factor; activated factor X; coagulation factor Xa. Enzyme Commission Number: EC 3.4.21.6. CAS No. 9002-5-5. Factor Xa. Storage: -20°C. Form: aqueous glycerol solution. Source: Bovine plasma. Species: Bovine. EC 3.4.21.6; 9002-05-5; thrombokinase; prothrombase; prothrombinase; activated blood-coagulation factor X; autoprothrombin C; thromboplastin; plasma thromboplastin; factor Xa; activated Stuart-Pr | |
| N-formylmethionyl-peptidase | Highly specific for N-formylmethionyl peptides. Will not cleave methionyl peptides or N-formyl derivatives of amino acids other than methionine. Isolated from rat liver. Inhibited by heavy metals and activated by Cl-. Group: Enzymes. Synonyms: (fMet)-releasing enzyme; formylmethionine aminopeptidase. Enzyme Commission Number: EC 3.4.19.7. CAS No. 76106-80-4. 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-4091; N-formylmethionyl-peptidase; EC 3.4.19.7; 76106-80-4; (fMet)-releasing enzyme; formylmethionine aminopeptidase. Cat No: EXWM-4091. | |
| prolyl oligopeptidase | Found in vertebrates, plants and Flavobacterium. Generally cytosolic, commonly activated by thiol compounds. Type example of peptidase family S9. Group: Enzymes. Synonyms: post-proline cleaving enzyme; proline-specific endopeptidase; post-proline endopeptidase; proline endopeptidase; endoprolylpeptidase; prolyl endopeptidase. Enzyme Commission Number: EC 3.4.21.26. CAS No. 72162-84-6. PE. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4124; prolyl oligopeptidase; EC 3.4.21.26; 72162-84-6; post-proline cleaving enzyme; proline-specific endopeptidase; post-proline endopeptidase; proline endopeptidase; endoprolylpeptidase; prolyl endopeptidase. Cat No: EXWM-4124. | |
| protein C (activated) | A peptidase of family S1 (trypsin family), one of the γ-carboxyglutamic acid-containing coagulation factors. Formed from protein C, the proenzyme that circulates in plasma, by the action of a complex of thrombin with thrombomodulin, or by serine endopeptidases present in several snake venoms. Group: Enzymes. Synonyms: blood-coagulation factor XIVa; activated blood coagulation factor XIV; activated protein C; autoprothrombin II-A; protein Ca; APC; GSAPC. Enzyme Commission Number: EC 3.4.21.69. CAS No. 42617-41-4. Protein C. 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-4160; protein C (activated); EC 3.4.21.69; 42617-41-4; blood-coagulation factor XIVa; activated blood coagulation factor XIV; activated protein C; autoprothrombin II-A; protein Ca; APC; GSAPC. Cat No: EXWM-4160. | |
| thrombin | Formed from prothrombin. More selective than trypsin and plasmin. In peptidase family S1 (trypsin family). Group: Enzymes. Synonyms: fibrinogenase; thrombase; thrombofort; topical; thrombin-C; tropostasin; activated blood-coagulation factor II; blood-coagulation factor IIa; factor IIa; E thrombin; β-thrombin; γ-thrombin. Enzyme Commission Number: EC 3.4.21.5. CAS No. 9002-4-4. Thrombin. 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-4143; thrombin; EC 3.4.21.5; 9002-04-4; fibrinogenase; thrombase; thrombofort; topical; thrombin-C; tropostasin; activated blood-coagulation factor II; blood-coagulation factor IIa; factor IIa; E thrombin; β-thrombin; γ-thrombin. Cat No: EXWM-4143. | |
| Xaa-Pro dipeptidase | A Mn2+-activated enzyme, in peptidase family M24 (methionyl aminopeptidase family); cytosolic from most animal tissues. Group: Enzymes. Synonyms: prolidase; imidodipeptidase; proline dipeptidase; peptidase D; γ-peptidase; X-Pro dipeptidase. Enzyme Commission Number: EC 3.4.13.9. CAS No. 9025-32-5. Prolidase. 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-4042; Xaa-Pro dipeptidase; EC 3.4.13.9; 9025-32-5; prolidase; imidodipeptidase; proline dipeptidase; peptidase D; γ-peptidase; X-Pro dipeptidase. Cat No: EXWM-4042. | |
| 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. |  |
| 1-Bromo-3-methyl-2-butene (90%) | 1-Bromo-3-methyl-2-butene is used to prepare xanthine dipeptidyl peptidase inhibitors for treatment of type 2 diabetes. It can also be used to synthesize natural and non-natural prenylated chalcones with antitumor, antioxidant activities. Group: Biochemicals. Grades: Highly Purified. CAS No. 870-63-3. Pack Sizes: 1g, 5g. Molecular Formula: C5H9Br, Molecular Weight: 149.03. US Biological Life Sciences. | Worldwide |
| acylaminoacyl-peptidase | Active at neutral pH. Several variants of this enzyme exist; the human erythrocyte enzyme is relatively specific for removal of N-acetylalanine from peptides. Displays dipeptidyl-peptidase activity on glycyl-peptides, perhaps as a result of mis-recognition of the glycyl residue as an uncharged N-acyl group. Inhibited by diisopropyl fluorophosphate. In peptidase family S9 (prolyl oligopeptidase family). Group: Enzymes. Synonyms: acylamino-acid-releasing enzyme; N-acylpeptide hydrolase; N-formylmethionine (fMet) aminopeptidase; α-N-acylpeptide hydrolase. Enzyme Commission Number: EC 3.4.19.1. CAS No. 73562-30-8. 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-4082; acylaminoacyl-peptidase; EC 3.4.19.1; 73562-30-8; acylamino-acid-releasing enzyme; N-acylpeptide hydrolase; N-formylmethionine (fMet) aminopeptidase; α-N-acylpeptide hydrolase. Cat No: EXWM-4082. | |
| ADAM10 endopeptidase | In peptidase family M12. Partially responsible for the "α-secretase" activity in brain that degrades the potentially harmful β-amyloid peptide. Work with ADAM10-deficient mice supports a role in Notch signalling. Group: Enzymes. Synonyms: Kuzbanian protein; myelin-associated disintegrin metalloproteinase. Enzyme Commission Number: EC 3.4.24.81. CAS No. 193099-09-1. 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-4365; ADAM10 endopeptidase; EC 3.4.24.81; 193099-09-1; Kuzbanian protein; myelin-associated disintegrin metalloproteinase. Cat No: EXWM-4365. | |
| 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. | |
| alternative-complement-pathway C3/C5 convertase | A bimolecular complex of complement fragment Bb with either C3b or cobra venom factor; Bb contains the active site. Bb is formed by cleavage of proenzyme factor B by factor D. Cleavage of complement component C5 requires additional C3b which binds C5 and renders it susceptible to cleavage by C3b,Bb complex. C3b,Bb is stabilized in plasma by factor P. Complement factor B is in peptidase family S1 (trypsin family). Group: Enzymes. Synonyms: complement component C3/C5 convertase (alternative); proenzyme factor B; properdin factor B; C3 proactivator; glycine-rich β-glycoprotein; heat-labile factor; C3 convertase; C3. Enzyme Commission Number: EC 3.4.21.47. CAS No. 80295-67-6. 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-4140; alternative-complement-pathway C3/C5 convertase; EC 3.4.21.47; 80295-67-6; complement component C3/C5 convertase (alternative); proenzyme factor B; properdin factor B; C3 proactivator; glycine-rich β-glycoprotein; heat-labile factor; C3 convertase; C3b,Bb,CVF,Bb,C5 convertase; (C3b)n,Bb; complement C 3(C 5) convertase (amplification); alternative complement pathway C3(C5) convertase; C5 convertase; CVF,Bb; (CVF)-dependent glycine-rich-β-glucoprotein; cobra venom factor-dependent C3 convertase. Cat No: EXWM-4140. | |
| aminopeptidase I | A 640-kDa, dodecameric enzyme best known as the major vacuolar aminopeptidase of yeast, Saccharomyces cervisiae, in which species it was first given the name aminopeptidase I (one), amongst others. Activity is stimulated by both Zn2+ and Cl- ions. Type example of peptidase family M18. Group: Enzymes. Synonyms: aminopeptidase III; aminopeptidase yscI; leucine aminopeptidase IV; yeast aminopeptidase I. Enzyme Commission Number: EC 3.4.11.22. CAS No. 9031-94-1. Aminopeptidase I. 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-4019; aminopeptidase I; EC 3.4.11.22; 9031-94-1; aminopeptidase III; aminopeptidase yscI; leucine aminopeptidase IV; yeast aminopeptidase I. Cat No: EXWM-4019. | |
| Antagonist G | Antagonist G is a substance P analog, which is a broad spectrum neuropeptide growth factor antagonist and antiproliferative agent. It was developed for the treatment of small cell lung cancer. It could inhibit neuropeptide-dependent and -independent proliferation of small cell lung cancer in vitro. It also inhibits growth of SCLC xenografts in mice in vivo. It blocks Swiss 3T3 cell growth induced by vasopressin, gastrin-releasing peptide and bradykinin. It activates JNK and stimulates apoptosis. It is an anticancer agent and is resistant to degradation by peptidases. Synonyms: [Arg6,D-Trp7,9,N-MePhe8]-Substance P(6-11). Grades: 98%. CAS No. 115150-59-9. Molecular formula: C49H66N12O6S. Mole weight: 951.20. | |
| ASP-4000 | ASP-4000 is a dipeptidyl peptidase 4 (DPP) inhibitor with antihyperglycemic activity. Uses: Hyperlipidaemia; hyperlipoproteinaemia type iia;primary biliary cirrhosis. Synonyms: ASP4000; ASP-4000 free base; 2-Pyrrolidinecarbonitrile, 1-(((1R,3S,4S,6R)-6-hydroxy-2-azabicyclo(2.2.1)hept-3-yl)carbonyl)-, (2S)-. Grades: 98%. CAS No. 851510-67-3. Molecular formula: C12H17N3O2. Mole weight: 235.28. | |
| ASP-4000 hydrochoride | ASP-4000 is a dipeptidyl peptidase 4 (DPP) inhibitor. It has antihyperglycemic activity. Uses: Antihyperglycemic agent. Synonyms: ASP-4000 hydrochoride; ASP 4000 hydrochoride; ASP4000 hydrochoride; UNII-7393JFE67B;(2S)-1-(((1R,3S,4S,6R)-6-Hydroxy-2-azabicyclo(2.2.1)hept-3-yl)carbonyl)-2-pyrrolidinecarbonitrile hydrochloride. Grades: 98%. CAS No. 851389-35-0. Molecular formula: C12H18ClN3O2. Mole weight: 271.74. | |
| bleomycin hydrolase | The molecule is a homohexamer in which the monomers have a papain-like tertiary structure (in peptidase family C1). The active sites are on the walls of a central channel through the molecule, and access of substrate molecules to them is obstructed by this and by the C-terminus of each polypeptide chain. Bleomycin can scarcely be the natural substrate, and there are reports of limited endopeptidase activity. Known from bacteria as well as eukaryotic organisms. Hydrolase H from chicken muscle has many similarities to bleomycin hydrolase, but hydrolyses Ph-CO-Arg-2-naphthylamine as well as aminopeptidase substrates. Group: Enzymes. Synonyms: aminopeptidase C (Lactococcus lactis). Enzyme Commission Number: EC 3.4.22.40. CAS No. 53096-17-6. 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-4215; bleomycin hydrolase; EC 3.4.22.40; 53096-17-6; aminopeptidase C (Lactococcus lactis). Cat No: EXWM-4215. | |
| Boc-3,4-dichloro-D-phenylalanine | Boc-3,4-dichloro-D-phenylalanine is used to prepare fluorinated β-aminoacyl 1,2,4-triazolo[4,3-a]piperazine amides as dipeptidyl peptidase IV inhibitors and antidiabetic agents. It is also used in the synthesis of N-[(R,R)-(E)-1-(3,4-dichlorobenzyl)-3-(2-oxoazepan-3-yl)carbamoyl]allyl-N-methyl-3,5-bis(trifluoromethyl)benzamide as a potent and orally active dual neurokinin NK1/NK2 receptor antagonist. Synonyms: Boc-D-Phe(3,4-DiCl)-OH; Boc-D-Phe(3,4-Cl2)-OH; (R)-Boc-2-amino-3-(3,4-dichlorophenyl)propionic acid; Boc-D-Phe(3,4-Cl2)-OH; (R)-2-((tert-Butoxycarbonyl)amino)-3-(3,4-dichlorophenyl)propanoic acid; D-Phenylalanine, 3,4-dichloro-N-[(1,1-dimethylethoxy)carbonyl]-; Boc-D-3,4-Dichlorophenylalanine; AK162594; N-BOC-3,4-DICHLORO-D-PHENYLALANINE. Grades: ≥ 98% (HPLC). CAS No. 114873-13-1. Molecular formula: C14H17Cl2NO4. Mole weight: 334.20. | |
| bontoxilysin | This zinc enzyme, produced by Clostridium botulinum, occurs as forms A-G that differ in specificity of action on the proteins of the neuroexocytosis apparatus. The 150-kDa proenzymes of bontoxilysin are processed to disulfide-linked subunits of 100 and 50 kDa, the latter being responsible for the endopeptidase activities. Weakly inhibited by captopril, and phosphoramidon. Toxicity is due to action at the neuromuscular junctions that blocks release of acetylcholine, causing flaccid paralysis, in contrast to the spastic paralysis caused by tentoxilysin. In peptidase family M27 (tentoxilysin family). Group: Enzymes. Synonyms: botulinum neurotoxin; BoNT. Enzyme Commission Number: EC 3.4.24.69. CAS No. 107231-12-9. 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-4352; bontoxilysin; EC 3.4.24.69; 107231-12-9; botulinum neurotoxin; BoNT. Cat No: EXWM-4352. | |
| Carboxypeptidase B from Porcine, Recombinant | Carboxypeptidase B (or peptidyl-L-lysine (-L-arginine) hydrolase) catalyzes the hydrolysis of the basic amino acids, lysine, arginine, and ornithine from the C-terminal position of polypeptides. It has been shown to be a single polypeptide of 34 kDa Da. Trypsin is capable of converting native enzyme to the active enzyme, carboxypeptidase B II in vitro. The optimum pH is found to be 9.0. The enzyme may be used for sequence analysis by successive cleavage of C-terminal basic amino acids. It can also be used as a serum marker for the diagnosis of acute pancreatitis. Carboxypeptidase b (ec 3.4.17.2), also well known as protaminase, pancreatic procarboxy-peptidase b (pcpb), ... mature chain. the secreted cpb zymogen is converted to enzymatically active cpb by limited proteolysis by trypsin. Group: Enzymes. Synonyms: carboxypeptidase B; protaminase; CPB1; pancreatic carboxypeptidase B; tissue carboxypeptidase B; peptidyl-L-lysine [L-arginine]hydrolase; EC 3.4.17.2; 9025-24-5. Enzyme Commission Number: EC 3.4.17.2. Purity: >90% (SDS-PAGE test). Mole weight: About 35kDa (SDS-PAGE detection). Activity: >180U/mg. Appearance: White powder, lyophilized. Storage: Redissolved in 20% glycerol, 4°C, store at -20°C for long-term preservation, Avoid multiple freeze-thaw cycles. Form: Freeze dried powder. Source: Porcine. carboxypeptidase B; protaminase; C | |
| carboxypeptidase M | A membrane-bound enzyme optimally active at neutral pH. In peptidase family M14 (carboxypeptidase A family). Group: Enzymes. Synonyms: CPM. Enzyme Commission Number: EC 3.4.17.12. CAS No. 120038-28-0. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4064; carboxypeptidase M; EC 3.4.17.12; 120038-28-0; CPM. Cat No: EXWM-4064. | |
| carboxypeptidase Taq | A 56-kDa enzyme from Thermus aquaticus. Most active at 80° C. Type example of peptidase family M32. Group: Enzymes. Enzyme Commission Number: EC 3.4.17.19. CAS No. 9031-98-5. 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-4071; carboxypeptidase Taq; EC 3.4.17.19; 9031-98-5. Cat No: EXWM-4071. | |
| caspase-10 | Caspase-10 is an initiator caspase, as are caspase-2 (EC 3.4.22.55), caspase-8 (EC 3.4.22.61) and caspase-9 (EC 3.4.22.62). Like caspase-8, caspase-10 contains two tandem death effector domains (DEDs) in its N-terminal prodomain, and these play a role in procaspase activation. The enzyme has many overlapping substrates in common with caspase-8, such as RIP (the cleavage of which impairs NF-κB survival signalling and starts the cell-death process) and PAK2 (associated with some of the morphological features of apoptosis, such as cell rounding and apoptotic body formation). Bid, a Bcl2 protein, can be cleaved by caspase-3 (EC 3.4.22.56), caspase-8 and caspase-10 at Lys-Gln-Thr-Asp? ...u-Thr-Asp? to yield a p13 fragment that is not N-myristoylated. Belongs in peptidase family C14. Group: Enzymes. Synonyms: FLICE2, Mch4; CASP-10; ICE-like apoptotic protease 4; apoptotic protease Mch-4; FAS-associated death domain protein interleukin-1β-converting enzyme 2. Enzyme Commission Number: EC 3.4.22.63. CAS No. 189088-85-5. 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-4239; caspase-10; EC 3.4.22.63; 189088-85-5; FLICE2, Mch4; CASP-10; ICE-like apoptotic protease 4; apoptotic protease Mch-4; FAS-associated death domain protein interleukin-1β-converting enzyme 2. Cat No: EXWM-4239. | |
| caspase-11 | This murine enzyme is part of the family of inflammatory caspases, which also includes caspase-1 (EC 3.4.22.36), caspase-4 (EC 3.4.22.57) and caspase-5 (EC 3.4.22.58) in humans and 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. Like caspase-5, but unlike caspase-4, this enzyme can be induced by lipopolysaccharide. This enzyme not only activates caspase-1, which is required for the maturation of proinflammatory cytokines such as interleukin-1β (IL-1β) and IL-18, but it also activates caspase-3 (EC 3.4.22.56), which leads to cellular apoptosis under pathological conditions. Belongs in peptidase family C14. Group: Enzymes. Synonyms: CASP-11. Enzyme Commission Number: EC 3.4.22.64. 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-4240; caspase-11; EC 3.4.22.64; CASP-11. Cat No: EXWM-4240. | |
| caspase-4 | This enzyme is part of the family of inflammatory caspases, which also includes caspase-1 (EC 3.4.22.36) 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. The enzyme is able to cleave itself and the p30 caspase-1 precursor, but, unlike caspase-1, it is very inefficient at generating mature interleukin-1β (IL-1β) from pro-IL-1&beta. Both this enzyme and caspase-5 can cleave pro-caspase-3 to release the small subunit (p12) but not the large subunit (p17). The caspase-1 inhibitor Ac-Tyr-Val-Ala-Asp-CHO can also inhibit this enzyme, but more slowly. Belongs in peptidase family C14. Group: Enzymes. Synonyms: ICErelII; ICErel-II; Ich-2; transcript X; TX; TX protease; caspase 4; CASP-4. Enzyme Commission Number: EC 3.4.22.57. CAS No. 182762-08-9. 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-4232; caspase-4; EC 3.4.22.57; 182762-08-9; ICErelII; ICErel-II; Ich-2; transcript X; TX; TX protease; caspase 4; CASP-4. Cat No: EXWM-4232. | |
| caspase-5 | This enzyme is part of the family of inflammatory caspases, which also includes caspase-1 (EC 3.4.22.36) and caspase-4 (EC 3.4.22.57) 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. The enzyme is able to cleave itself and the p30 caspase-1 precursor, but is very inefficient at generating mature interleukin-1β (IL-1β) from pro-IL-1&beta. Both this enzyme and caspase-4 can cleave pro-caspase-3 to release the small subunit (p12) but not the large subunit (p17). Unlike caspase-4, this enzyme can be induced by lipopolysaccharide. Belongs in peptidase family C14. Group: Enzymes. Synonyms: ICErel-III; Ich-3; ICH-3 protease; transcript Y; TY; CASP-5. Enzyme Commission Number: EC 3.4.22.58. CAS No. 192465-11-5. 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-4233; caspase-5; EC 3.4.22.58; 192465-11-5; ICErel-III; Ich-3; ICH-3 protease; transcript Y; TY; CASP-5. Cat No: EXWM-4233. | |
| caspase-6 | Caspase-6 is an effector/executioner caspase, as are caspase-3 (EC 3.4.22.56) and caspase-7 (EC 3.4.22.60). These caspases are responsible for the proteolysis of the majority of cellular polypeptides [e.g. poly(ADP-ribose) polymerase (PARP)], which leads to the apoptotic phenotype. Caspase-6 can cleave its prodomain to produce mature caspase-6, which directly activates caspase-8 (EC 3.4.22.61) and leads to the release of cytochrome c from the mitochondria. The release of cytochrome c is an essential component of the intrinsic apoptosis pathway. The enzyme can also cleave and inactivate lamins, the intermediate filament scaffold proteins of the nuclear envelope, leading to nuclear fragmentation in the final phases of apoptosis. Belongs in peptidase family C14. Group: Enzymes. Synonyms: CASP-6; apoptotic protease Mch-2; Mch2. Enzyme Commission Number: EC 3.4.22.59. CAS No. 182372-15-2. 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-4234; caspase-6; EC 3.4.22.59; 182372-15-2; CASP-6; apoptotic protease Mch-2; Mch2. Cat No: EXWM-4234. | |
| 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 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 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. | |
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