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| Product | Description | |
|---|---|---|
| ?Aminocaproic acid | Aminocaproic acid is a derivative and analogue of the amino acid lysine, which makes it an effective inhibitor for enzymes that bind that particular residue. Such enzymes include proteolytic enzymes like plasmin, the enzyme responsible for fibrinolysis. Uses: Antifibrinolytic agents. Synonyms: Aminocaproic acid; NSC 400230; NSC-400230; NSC400230. Grades: >98%. CAS No. 60-32-2. Molecular formula: C6H13NO2. Mole weight: 131.17. |  |
| bacterial leucyl aminopeptidase | A zinc enzyme. Forms of the enzyme have been isolated from Aeromonas proteolytica, Escherichia coli and Streptococcus thermophilus. Examples are known from peptidase families M17 and M28 (of leucyl aminopeptidase and aminopeptidase Y, respectively). Group: Enzymes. Synonyms: Aeromonas proteolytica aminopeptidase. Enzyme Commission Number: EC 3.4.11.10. CAS No. 37288-67-8. Aminopeptidase. 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-4008; bacterial leucyl aminopeptidase; EC 3.4.11.10; 37288-67-8; Aeromonas proteolytica aminopeptidase. Cat No: EXWM-4008. |  |
| Beer blend enzyme | This product is superior stains by submerged fermentation and the advanced after the extraction process compound enzyme preparation of beer. It contain - dextranase ,xylanase ,cellulose α-amylase ,glycogen phosphorylase ,proteolytic enzyme Etc. A variety of enzyme integrated to improve saccharification , improve the filtration rate. Applications: 1?saccharification of raw material to improve the efficiency of utilization and production, increase the yield of saccharification , reduce costs. 2?reduce wort viscosity, improve wort and beer filtration the efficiency and quality. 3?enhance protein degr. Group: Enzymes. Synonyms: Beer blend enzyme; saccharification enzyme; saccharification; improve wort; beer filtration; beer filtration enzyme; protein degradation enzyme; protein degradation; Beer blend enzyme; BER-1513. Beer enzyme. Appearance: powder. Beer blend enzyme; saccharification enzyme; saccharification; improve wort; beer filtration; beer filtration enzyme; protein degradation enzyme; protein degradation; Beer blend enzyme; BER-1513. Pack: 25kg/barrel or subject to client requirement. Cat No: BER-1514. | |
| Bradykinin (1-5) | Bradykinin (1-5) is a major stable metabolite of Bradykinin, formed by the proteolytic action of angiotensin-converting enzyme (ACE). Uses: Scientific research. Group: Peptides. CAS No. 23815-89-6. Pack Sizes: 1 mg; 5 mg. Product ID: HY-P1488. |  |
| 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. | |
| Caspase-1 from Human, Recombinant | Caspase 1/Interleukin-1 converting enzyme is an enzyme that proteolytically cleaves other proteins, such as the precursor forms of the inflammatory cytokines interleukin 1β and interleukin 18, into active mature peptides. Caspase 1 has been shown to induce cell necrosis or pyroptosis and may function in various developmental stages. Studies of a similar protein in mouse suggest a role in the pathogenesis of Huntington's disease. Alternative splicing of the gene results in five transcript variants encoding distinct isoforms. Recent studies implicated caspase 1 in promoting CD4 T-cell death and inflammation by HIV, two signature events that fuel HIV disease progression to AIDS. Recombinant, human caspase-1 fused at the n-terminus to a hisotag sequence and expressed in e. coli useful for the study of enzyme regulation, cleavage of target substrates, and inhibitor screening. Group: Enzymes. Synonyms: CASP1; ICE; IL1BC; P45; Caspase 1; Interleukin-1; IL-1β Converting Enzyme. Purity: >90% by SDS-PAGE. Caspase-1. Mole weight: 10 kDa and 20 kDa. Activity: >25,000 units/mg protein. Storage: < -70°C; Avoid freeze/thaw. Form: Liquid. Source: E. coli. Species: Human. CASP1; ICE; IL1BC; P45; Caspase 1; Interleukin-1; IL-1β Converting Enzyme. Cat No: NATE-0813. | |
| Caspase-6 (Active) from Human, Recombinant | Caspase-6 is an enzyme that in humans is encoded by the CASP6 gene. This gene encodes a protein that is a member of the cysteine-aspartic acid protease (caspase) family. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes that undergo proteolytic processing at conserved aspartic residues to produce two subunits, large and small, that dimerize to form the active enzyme. This protein is processed by caspases 7, 8 and 10, and is thought to function as a downstream enzyme in the caspase activation cascade. Caspase 6 can also undergo self-processing without other members of the caspase family. Alternative splicing of this gene results in two transcript variants that encode different isoforms. Group: Enzymes. Synonyms: CASP6; MCH2; Caspase-6 (Active); Caspase-6. Caspase 6. Appearance: Liquid. Storage: -80°C. Form: Liquid. 5μg in 25μl of 50mM TRIS (pH 8.0) containing 100mM sodium chloride and 50mM imidazole. Source: E. coli. Species: Human. CASP6; MCH2; Caspase-6 (Active); Caspase-6. Cat No: NATE-0814. | |
| Caspase-7 from Human, Recombinant | Caspase-7 is a member of the caspase (cysteine aspartate protease) family of proteins, and has been shown to be an executioner protein of apoptosis. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes that undergo proteolytic processing by upstream caspases (caspase-8, -9) at conserved aspartic residues to produce two subunits, large and small, that dimerize to form the active enzyme in the form of a heterotetramer. The precursor of this caspase is cleaved by caspase 3, caspase 10, and caspase 9. It is activated upon cell death stimuli and induces apoptosis. Alternative splicing results in four transcript variants, encoding three distinct isoforms. Applications: Used to screen caspase inhibitors, study enzyme regulation, determine caspase substrate specificity, or as positive control in caspase activity assays. Group: Enzymes. Synonyms: CASP7; CASP-7; CMH-1; ICE-LAP3; LICE2; MCH3; Caspase-7. Enzyme Commission Number: EC 3.4.22.-. Purity: 90% (SDS-PAGE). Caspase 7. Activity: ~25,000U/mg protein. Appearance: Lyophilized. Storage: -80°C. Source: E. coli. Species: Human. CASP7; CASP-7; CMH-1; ICE-LAP3; LICE2; MCH3; Caspase-7. Cat No: NATE-0815. | |
| 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. | |
| Cathepsin F from Human, Recombinant | Cathepsin F, also known as CTSF, belongs to the cathepsin family. Cathepsins are papain familycysteine proteinases that represent a major component of the lysosomal proteolytic system. The CTSF gene isubiquitously expressed, and it maps to chromosome 11q13, close to the gene encoding cathepsin W. CTSF isthought to play a role in normal protein catabolism, and because it is highly expressed in some cancer cell lines, itmay be involved in degradative processes occurring during tumor progression. Recombinant human CTSF protein,fused to His-tag at N-terminus, was expressed in E.coli. Group: Enzymes. Enzyme Commission Number: EC 3.4.22.41. Mole weight: This protein is fused with a 6× His tag at N-terminus and has a calculated MW of 26 kDa. Form: Liquid. Source: E. coli. Species: Human. Cat No: NATE-1666. | |
| Cathepsin S from Human, recombinant | Cathepsin S (CTSS) is a lysosomal cysteine protease of the papain family and may participate in the degradation of antigenic proteins to peptides for presentation on MHC class II molecules. CTSS is synthesized as inactive precursor of 331 amino acids consisting of a 15-aa signal peptide, a propeptide of 99 aa, and a mature polypeptide of 217 aa. It is activated in the lysosomes by a proteolytic cleavage of the propeptide. The deduced amino acid sequence contains only one potential N-glycosylation site located in the propeptide. Compared with the abundant cathepsins B, L and H, cathepsin S shows a restricted tissue distribution, with highest levels in spleen, heart, and lung...l compartment, and is implicated in the pathogenesis of Alzheimers disease and Down Syndrome. Group: Enzymes. Synonyms: CTSS; cathepsin S; EC 3.4.22.27; FLJ50259; MGC3886. Enzyme Commission Number: EC 3.4.22.27. CAS No. 71965-46-3. Purity: > 90% by SDS-PAGE. CTSS. Mole weight: 23.9 kDa (115-331 aa). Activity: >2000 mU/mg. Storage: Stable for at least 1 year as supplied. Briefly spin down the vial and reconstitute in 50 mM sodium acetate, 100 mM NaCl (pH 5.5) to 0.1-1 mg/ml and store at -80°C. Avoid repeated freeze and thaw cycles. Form: Lyophilized from proprietary buffer. Source: E. coli. Species: Human. CTSS; cathepsin S; EC 3.4.22.27; FLJ50259; MGC3886. Cat No: NATE-1702. | |
| Cholesterol Esterase from Candida Rugosa | Cholesterol esterase (CE) is also known as cholesterol ester hydrolase. This enzyme catalyzes the following reaction: Sterol Ester --------> Sterol + Fatty Acid. Cholesterol esterase activity has been demonstrated in pancreas, intestine, liver and kidney. The enzyme is inactivated by proteolytic enzymes but stabilized by proteolytic enzyme inhibitors and by bile salts. Group: Enzymes. Synonyms: cholesterol esterase; cholesteryl ester synthase; triterpenol esterase; cholesteryl esterase; cholesteryl ester hydrolase; sterol ester hydrolase; cholesterol ester hydrolase; cholesterase; acylcholesterol lipase; sterol esterase; CE. Enzyme Commission Number: EC 3.1.1.13. CAS No. 9026-00-0. Purity: 0.9. Activity: 25-100 U/mg. Storage: Store at -20° C. Form: Freeze dried powder. Source: Candida Rugosa. cholesterol esterase; cholesteryl ester synthase; triterpenol esterase; cholesteryl esterase; cholesteryl ester hydrolase; sterol ester hydrolase; cholesterol ester hydrolase; cholesterase; acylcholesterol lipase; sterol esterase; CE. Cat No: NATE-1679. | |
| Cholesterol Esterase from Microorganism | Cholesterol esterase (CE) is also known as cholesterol ester hydrolase. This enzyme catalyzes the following reaction: Sterol Ester --------> Sterol + Fatty Acid. Cholesterol esterase activity has been demonstrated in pancreas, intestine, liver and kidney. The enzyme is inactivated by proteolytic enzymes but stabilized by proteolytic enzyme inhibitors and by bile salts. Group: Enzymes. Synonyms: cholesterol esterase; cholesteryl ester synthase; triterpenol esterase; cholesteryl esterase; cholesteryl ester hydrolase; sterol ester hydrolase; cholesterol ester hydrolase; cholesterase; acylcholesterol lipase; EC 3.1.1.13; Sterol esterase. Enzyme Commission Number: EC 3.1.1.13. CAS No. 9026-00-0. Activity: 5.0U/mg-solid or more. Form: Freeze dried powder. Source: Microorganism. cholesterol esterase; cholesteryl ester synthase; triterpenol esterase; cholesteryl esterase; cholesteryl ester hydrolase; sterol ester hydrolase; cholesterol ester hydrolase; cholesterase; acylcholesterol lipase; EC 3.1.1.13; Sterol esterase. Cat No: DIA-135. | |
| Cholesterol Esterase from Pseudomonas sp. | Cholesterol esterase (CE) is also known as cholesterol ester hydrolase. This enzyme catalyzes the following reaction: Sterol Ester --------> Sterol + Fatty Acid. Cholesterol esterase activity has been demonstrated in pancreas, intestine, liver and kidney. The enzyme is inactivated by proteolytic enzymes but stabilized by proteolytic enzyme inhibitors and by bile salts. Group: Enzymes. Synonyms: cholesterol esterase; cholesteryl ester synthase; triterpenol esterase; cholesteryl esterase; cholesteryl ester hydrolase; sterol ester hydrolase; cholesterol ester hydrolase; cholesterase; acylcholesterol lipase; EC 3.1.1.13; Sterol esterase. Enzyme Commission Number: EC 3.1.1.13. CAS No. 9026-00-0. Activity: 100U/mg-solid or more (containing approx. 40% of stabilizers). Form: Freeze dried powder. Source: Pseudomonas sp. cholesterol esterase; cholesteryl ester synthase; triterpenol esterase; cholesteryl esterase; cholesteryl ester hydrolase; sterol ester hydrolase; cholesterol ester hydrolase; cholesterase; acylcholesterol lipase; EC 3.1.1.13; Sterol esterase. Cat No: DIA-134. | |
| Cholesterol Esterase from Schizophyllum commune | Cholesterol esterase (CE) is also known as cholesterol ester hydrolase. This enzyme catalyzes the following reaction: Sterol Ester --------> Sterol + Fatty Acid. Cholesterol esterase activity has been demonstrated in pancreas, intestine, liver and kidney. The enzyme is inactivated by proteolytic enzymes but stabilized by proteolytic enzyme inhibitors and by bile salts. Group: Enzymes. Synonyms: cholesterol esterase; cholesteryl ester synthase; triterpenol esterase; cholesteryl esterase; cholesteryl ester hydrolase; sterol ester hydrolase; cholesterol ester hydrolase; cholesterase; acylcholesterol lipase; EC 3.1.1.13; Sterol esterase. Enzyme Commission Number: EC 3.1.1.13. CAS No. 9026-00-0. Activity: 2.0 U/mg-solid or more (containing approx. 20% of stabilizers). Form: Freeze dried powder. Source: Schizophyllum commune. cholesterol esterase; cholesteryl ester synthase; triterpenol esterase; cholesteryl esterase; cholesteryl ester hydrolase; sterol ester hydrolase; cholesterol ester hydrolase; cholesterase; acylcholesterol lipase; EC 3.1.1.13; Sterol esterase. Cat No: DIA-133. | |
| chymosin | Neonatal gastric enzyme with high milk clotting and weak general proteolytic activity, formed from prochymosin. Found among mammals with postnatal uptake of immunoglobulins. In peptidase family A1(pepsin A family). Group: Enzymes. Synonyms: rennin (but this should be avoided since it leads to confusion with renin). Enzyme Commission Number: EC 3.4.23.4. CAS No. 9001-98-3. Rennin. 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-4276; chymosin; EC 3.4.23.4; 9001-98-3; rennin (but this should be avoided since it leads to confusion with renin). Cat No: EXWM-4276. | |
| Chymotrypsin | Chymotrypsin is a proteolytic enzyme. It can priority hydrolyze tyrosine containing l-isomer, phenylalanine and the peptide bond of tryptophan, the best effective condition is pH 8.0. Its activity can be restrained by heavy metal or natural trypsin inhibitor in some degrees. Applications: Practically used to heal cicatrisation caused by injuries, inflammation and it is also used for avoiding part dropsy, blood-gathering, haematoma caused by wrick, breast dropsy after operation, tympanitis and rhinitis brief introduction of production: the high purity chymotrypsin is extracted from bovine or porcine pancreas and purified by affinity chromatography in order to avoid being polluted by other protease. Group: Enzymes. Synonyms: Chymotrypsin; Alpha-chymotrypsin; Chymotrypsin A; Chymotrypsin B. CAS No. 9004-7-3. Chymotrypsin. Appearance: inquire. Chymotrypsin; Alpha-chymotrypsin; Chymotrypsin A; Chymotrypsin B. Pack: inquire. Cat No: BIO-1012. | |
| Clostripain | Clostripain (Clostridiopeptidase B) is a proteolytic enzyme isolated from Clostridium histolyticum with esterase, amidase and protease activities and is a highly specific carboxypeptide targeting arginine key protease [1]. Uses: Scientific research. Group: Signaling pathways. Alternative Names: Clostridiopeptidase B. CAS No. 9028-00-6. Pack Sizes: 1 mg. Product ID: HY-P2895. | |
| Collagenase I, from Clostridium histolyticum | Collagenases are enzymes that break the peptide bonds in collagen. Collagenases are derived from the Clostridium histolyticum. Collagenases (Type I) are proteolytic enzymes that break peptide bonds in collagen and can be used for tissue digestion and dissociation. Uses: Scientific research. Group: Signaling pathways. CAS No. 9001-12-1. Pack Sizes: 25 mg; 50 mg; 100 mg. Product ID: HY-O0004. | |
| Collagenase NB 6 from Clostridium histolyticum (GMP Grade) | Collagenases from Clostridium histolyticum are proteolytic enzymes that cleave peptide bonds in the triple helical collagen molecule of human or animal tissue in situ. For this reason collagenases are widely used for isolation of various cell types by tissue dissociation. Applications: Collagenase nb 6 gmp grade is suitable for cell isolation from various tissue types intended for clinical applications. if a research or sterile product is required, collagenase nb 4 standard grade or collagenase nb 5 sterile grade, respectively, are recommended. both products have comparable enzymatic activities to collagenase nb 6 gmp grade. Group: Enzymes. Synonyms: Collagenase NB 6; Collagenase NB; Collagenase. Enzyme Commission Number: EC 3.4.24.3. CAS No. 9001-12-1. Collagenase. Mole weight: 70 000 - 120 000 (collagenases). Activity: ≥ 0.100 U/mg. Storage: 2 to 8 °C. Form: Lyophilized powder. Source: Clostridium histolyticum. Collagenase NB 6; Collagenase NB; Collagenase. Cat No: NATE-1918. | |
| C-terminal processing peptidase | Proteolytic processing of the D1 protein of photosystem II is necessary to allow the light-driven assembly of the tetranuclear manganese cluster, which is responsible for photosynthetic water oxidation. The recognition of the substrate is mediated by a PDZ domain, a small protein module that promotes protein-protein interactions by binding to internal or C-terminal sequences of their partner proteins. Type example of peptidase family S41. Group: Enzymes. Synonyms: CtpA gene product (Synechocystis sp.); photosystem II D1 protein processing peptidase; protease Re; tail-specific protease; Tsp protease. Enzyme Commission Number: EC 3.4.21.102. CAS No. 216484-75-2, 92480-11-0. 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-4097; C-terminal processing peptidase; EC 3.4.21.102; 216484-75-2, 92480-11-0; CtpA gene product (Synechocystis sp.); photosystem II D1 protein processing peptidase; protease Re; tail-specific protease; Tsp protease. Cat No: EXWM-4097. | |
| deuterolysin | Proteolytic activity found in Penicillium roqueforti, P. caseicolum, Aspergillus sojae and A. oryzae. Optimum pH of 5 for digesting various proteins. Strong action on protamine and histones. Insensitive to phosphoramidon. About 20 kDa. A distinct Aspergillus sojae endopeptidase is larger and has a neutral pH optimum. Type example of peptidase family M35. Formerly included in EC 3.4.24.4. Group: Enzymes. Synonyms: Penicillium roqueforti protease II; microbial neutral proteinase II; acid metalloproteinase; neutral proteinase II; Penicillium roqueforti metalloproteinase. Enzyme Commission Number: EC 3.4.24.39. CAS No. 247028-11-1. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4321; deuterolysin; EC 3.4.24.39; 247028-11-1; Penicillium roqueforti protease II; microbial neutral proteinase II; acid metalloproteinase; neutral proteinase II; Penicillium roqueforti metalloproteinase. Cat No: EXWM-4321. | |
| Dnp-Pro-Leu-Gly-Leu-Trp-Ala-DArg-NH2 | Dnp-Pro-Leu-Gly-Leu-Trp-Ala-DArg-NH2, a peptide utilized for biological research, is an exemplary agent for evaluating proteolytic activity and inhibitor effects. Notably, its potential in disease treatment, encompassing cancer and inflammation, has put it at the forefront of therapeutic development. In addition to its promising therapeutic properties, Dnp-Pro-Leu-Gly-Leu-Trp-Ala-DArg-NH2 may serve as a vital diagnostic tool for identifying pertinent enzymes within biological samples, providing otherwise unattainable insights for investigative purposes. Synonyms: N-(2,4-DINITROPHENYL)-PRO-LEU-GLY-LEU-TRP-ALA-D-ARG AMIDE; MMP SUBSTRATE, FLUOROGENIC; 360 MMP FRET SUBSTRATE I; DNP-PRO-LEU-GLY-LEU-TRP-ALA-D-ARG-NH2; DNP-PLGLWAR-NH2; N-(2,4-dinitrophenyl)-pro-leu-gly-leu-*trp-ala-D-. Grades: 98%. CAS No. 121282-17-5. Molecular formula: C45H64N14O11. Mole weight: 977.08. | |
| DUB Inhibitor IV, b-AP15 (NSC687852, 3, 5-bis ( (4-Nitrophenyl) methylidene) -1-prop-2-enoylpiperidin-4-one, (3E, 5E) -1-Acryloyl-3, 5-bis (4-nitrobenzylidene) piperidin-4-one, USP14 Inhibitor III, UCH-L5/UCH37 Inhibitor II) | A cell-permeable bis-nitrobenzylidene-piperidinone compound that acts as a potent, reversible and selective inhibitor of 19S regulatory-particle-associated deubiquitylating enzymes (DUBs) UCH-L5 and USP-14 (IC50=2.1uM against Ub-AMC substrate), with no effect on UCH-L1, UCH-L3, USP2, USP7, USP8 and BAP1 and on the proteasomal proteolytic activities. Shown to prevent proteasomal degradation (IC50=0.8uM in MelJuSo-UbG76V-YFP cells), and cause accumulation of higher molecular weights polyubiquitinated proteins in HCT-116 cells. Preferentially induces cell-cycle arrest and apoptosis in several colon cancer and in CNS cells, and effectively suppresses tumor growth in various mouse model (5mg/kg, i.p.). Group: Biochemicals. Grades: Highly Purified. CAS No. 1009817-63-4. Pack Sizes: 10mg. Molecular Formula: C??H??N?O?, Molecular Weight: 419.4. US Biological Life Sciences. |  Worldwide |
| Enterokinase from bovine intestine, Recombinant | Enteropeptidase (also called enterokinase) is an enzyme produced by cells of the duodenum and involved in human and animal digestion. It is secreted from intestinal glands (the crypts of Lieberkühn) following the entry of ingested food passing from the stomach. Enteropeptidase converts trypsinogen (a zymogen) into its active form trypsin, resulting in the subsequent activation of pancreatic digestive enzymes. Absence of enteropeptidase results in intestinal digestion impairment. Applications: Enterokinase is a member of the s1 peptidase family. in vivo, it is responsble for the proteolytic activation of trypsin from trypsinogen. enterokinase is used for site specific ...yme from creative enzymes has been used to compare the specific activity with that of purified, recombinant bovine enterokinase (light chain) overexpressed in escherichia coli. Group: Enzymes. Synonyms: enterokinase; enteropeptidase; EC 3.4.21.9; 9014-74-8. Enzyme Commission Number: EC 3.4.21.9. CAS No. 9014-74-8. Enterokinase. Mole weight: 28 kDa light chain form. Activity: Type I, > 20 units/mg protein. Storage: -20°C. Form: Type I, supplied as a solution in 20 mM Tris-HCl, 200 mM NaCl, and 50% glycerol; Type II, white powder. Source: E. coli. Species: Bovine intestine. enterokinase; enteropeptidase; EC 3.4.21.9; 9014-74-8. Pack: vial of ~0.2 unit. Cat No: NATE-0226. | |
| 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. | |
| Furin from Human, Recombinant | Furin is a dibasic endoprotease that is localized in the Golgi apparatus. It is responsible for the proteolytic maturation of many precursor proteins in the secretory and endocytic pathways of mammalian cells. Furin is a dibasic endoprotease that is localized in the Golgi apparatus. It has a molecular mass of 52.7 kDa. It is responsible for the proteolytic maturation of many precursor proteins in the secretory and endocytic pathways of mammalian cells. Furin cleaves precursor proteins at their paired basic amino acid processing sites. Some substrates of furin include von Willebrand factor, transforming growth factor beta 1 precursor, pro-beta-secretase and proparathyroid hormo...terial exotoxins, typically at sites marked by the consensus sequence arg-xaa-(lys/arg)-arg. Group: Enzymes. Synonyms: furin; prohormone convertase; dibasic processing enzyme; PACE; paired basic amino acid cleaving enzyme; paired basic amino acid converting enzyme; serine proteinase PACE; PC1; SPC3; proprotein convertase. Furin. Activity: > 2,000 unit/mL. Storage: -70°C. Form: buffered aqueous solution. Source: Baculovirus infected Sf9 cells. Species: Human. furin; prohormone convertase; dibasic processing enzyme; PACE; paired basic amino acid cleaving enzyme; paired basic amino acid converting enzyme; serine proteinase PACE; PC1; SPC3; proprotein convertase. Cat No: NATE-0268. | |
| γ-glutamyltransferase | The mammlian enzyme is part of the cell antioxidant defense mechanism. It initiates extracellular glutathione (GSH) breakdown, provides cells with a local cysteine supply and contributes to maintain intracelular GSH levels. The protein also has EC 3.4.19.13 (glutathione hydrolase) activity. The enzyme consists of two chains that are created by the proteolytic cleavage of a single precursor polypeptide. The N-terminal L-threonine of the C-terminal subunit functions as the active site for both the cleavage and the hydrolysis reactions. Group: Enzymes. Synonyms: glutamyl transpeptidase; α-glutamyl transpeptidase; γ-glutamyl peptidyltransferase; γ-glutamyl transpeptidase (ambiguous); γ-GPT; γ-GT; γ-GTP; L-γ-glutamyl. Enzyme Commission Number: EC 2.3.2.2. CAS No. 9046-27-9. γ-GT. 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-2293; γ-glutamyltransferase; EC 2.3.2.2; 9046-27-9; glutamyl transpeptidase; α-glutamyl transpeptidase; γ-glutamyl peptidyltransferase; γ-glutamyl transpeptidase (ambiguous); γ-GPT; γ-GT; γ-GTP; L-γ-glutamyl transpeptidase; L-γ-glutamyltransferase; L-glutamyltransferase; GGT (ambiguous); γ-glutamyltranspeptidase (ambiguous). Cat No: EXWM-2293. | |
| Glutaryl-glycyl-L-arginine 7-amido-4-methylcoumarin hydrochloride | Glutaryl-glycyl-L-arginine 7-amido-4-methylcoumarin hydrochloride is an innovative biomedical compound, used for ground-breaking proteolytic enzyme research and development. Fortified by its hydrochloride configuration, it manifests enhanced solubility and unprecedented stability. Synonyms: Glutaryl-Gly-Arg-AMC.HCl. CAS No. 103213-40-7. Molecular formula: C23H31ClN6O7. Mole weight: 538.98. | |
| glutathione hydrolase | This protein also has EC 2.3.2.2 (γ-glutamyltransferase) activity. The enzyme consists of two chains that are created by the proteolytic cleavage of a single precursor polypeptide. The N-terminal L-threonine of the C-terminal subunit functions as the active site for both the cleavage and the hydrolysis reactions. The human enzyme also hydrolyses oxidized glutathione and leukotriene C4 with similar efficiency, while the mouse enzyme does not. Group: Enzymes. Synonyms: glutathionase; GGT (ambiguous); γ-glutamyltranspeptidase (ambiguous). Enzyme Commission Number: EC 3.4.19.13. 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-4085; glutathione hydrolase; EC 3.4.19.13; glutathionase; GGT (ambiguous); γ-glutamyltranspeptidase (ambiguous). Cat No: EXWM-4085. | |
| Heparanase 1 from Human, Recombinant | Heparanase is an endo β-D-glucuronidase, which degrades heparan sulfate side chains of heparan sulfate proteoglycans (HSPGs) in the extracellular matrix. Heparanase plays an important role in ECM degradation, facilitating the migration and extravasation of tumor cells and inflammatory leukocytes. Upon degradation, heparanase releases growth factors and cytokines that stimulate cell proliferation and chemotaxis. Heparanase is a heterodimer comprised of a 50 kDa subunit harboring the active site and a 8 kDa subunit. It is produced as a latent 65 kDa precursor and proteolytically processed to its active form. Heparanase is highly expressed in myeloid leukocytes (i.e. neutrophils) in platelets and in human placenta. Human heparanase was found to be upregulated in various types of primary tumors, correlating in some cases with increased tumor invasiveness and vascularity and with poor prospective survival. Recombinant heparanase protein hpa1 is produced in cho cells. the protein is purified by several orthogonal chromatography steps. Applications: Positive control for western blot analysis. Group: Enzymes. Synonyms: Heparanase; Hpa1 heparan. HPA1. Storage: Store at -20°C, avoid repeated freeze-thaw cycles. Source: CHO. Species: Human. Heparanase; Hpa1 heparanase; Hpa1; heparanase 1; heparanase-1; C1A heparanase; HPSE; HPA1. Cat No: NATE-0843. | |
| Immobilized Proteinase K on G3m | Proteinase K is an unspecific serine protease with strong proteolytic activity on denatured (in SDS) and high molecular weight native proteins. It cleaves peptide bonds mostly after the carboxyl group of N-substituted hydrophobic, aliphatic and aromatic amino acids. G3m: 25 ug proteinase K immobilized on matrix G3m per CR-column. 0.7 mAnson units immobilized per CR-column. This CR-column cuts at least 370 ug BSA per application. Nr. 5 Storage buffer: 50 mM Tris/HCl, pH 7. 5Nr. 16 Reaction buffer: 50 mM Tris/HCl, 5 mM NaCl, pH 8. 0Nr. 17 Washing buffer: 50 mM Tris/HCl, 1. 0 M NaCl, pH 8. 0The columns are more active in 0.1% SDS and at 40°C. Also active in PBS buffer (20 mM Na-phosphate, 150 mM NaCl at pH 7. 6). Group: Enzymes. Synonyms: Tritirachium alkaline proteinase; Tritirachium album serine proteinase; proteinase K; Tritirachium album proteinase K; endopeptidase K; EC 3. 4. 21. 64; 39450-01-6. Enzyme Commission Number: EC 3. 4. 21. 64. Purity: Chromatographically purified, free of ribo- and deoxyribonucleases. Storage: 4 °C. Source: Tritirachium album. Tritirachium alkaline proteinase; Tritirachium album serine proteinase; proteinase K; Tritirachium album proteinase K; endopeptidase K; EC 3. 4. 21. 64; 39450-01-6; Immobilized Proteinase K. Cat No: NATE-1768. | |
| infectious pancreatic necrosis birnavirus Vp4 peptidase | Infectious pancreatic necrosis virus (IPNV) is a birnavirus that causes an acute, contagious disease in young salmonid fish. As with most viruses that infect eukaryotic cells, the proteolytic processing of viral precursor proteins is a crucial step in the life cycle of this virus. pVP2 is converted into VP2 by cleavage near the carboxy end of pVP2. This cleavage is most likely due to host-cell proteases rather than VP4. Differs from most serine peptidases in not having the catalytic triad Ser-His-Asp. Belongs in peptidase family S50. Group: Enzymes. Synonyms: infectious pancreatic necrosis virus protease; IPNV Vp4 protease; IPNV Vp4 peptidase; NS protease; NS-associated protease; Vp4 protease. Enzyme Commission Number: EC 3.4.21.115. 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-4110; infectious pancreatic necrosis birnavirus Vp4 peptidase; EC 3.4.21.115; infectious pancreatic necrosis virus protease; IPNV Vp4 protease; IPNV Vp4 peptidase; NS protease; NS-associated protease; Vp4 protease. Cat No: EXWM-4110. | |
| Insulin Degrading Enzyme (HisoTag) from Rat, Recombinant | Insulin Degrading Enzyme (IDE) is a large zinc-binding protease of the M16A metalloprotease subfamily known to cleave multiple short polypeptides that vary considerably in sequence. IDE was first identified by its ability to degrade the B chain of the hormone insulin. This activity was observed over sixty years ago, though the enzyme specifically responsible for B chain cleavage was identified more recently. This discovery revealed considerable amino acid sequence similarity between IDE and the previously characterized bacterial protease pitrilysin, suggesting a common proteolytic mechanism. Recombinant, rat insulin degrading enzyme fused to a hisotag sequence and expressed in s. frugiperda insect cells. a metalloprotease that degrades insulin and a variety of other peptides including amyloid peptides. Group: Enzymes. Synonyms: IDE; Insulin-degrading enzyme; insulysin; insulin protease. Enzyme Commission Number: EC 3.4.24.56. Purity: >90% by SDS-PAGE. IDE. Mole weight: 110 kDa. Activity: >3 U/mg protein. Storage: < -70°C. Form: Liquid. Source: S. frugiperda. Species: Rat. IDE; Insulin-degrading enzyme; insulysin; insulin protease. Cat No: NATE-0849. | |
| Keratinase, Recombinant | Keratinase is a particular class of extracellular proteolytic inducible enzyme with the capability of degrading insoluble keratin substrates. It is important for hydrolyzing hair, feather, and collagen in sewage system during waste water treatment. It is also useful in food industry, animal feed preparation etc. Insoluble feather keratin from poultry industry may be converted by enzymatic hydrolysis to glues, feedstuffs, fertilizers, films or used for the production of rare amino acids serine, cysteine and proline. Applications: Keratinase was used for enzymatic treatment of elementary body (eb), gag molecules, and cells in the study of the role glycosaminoglycans (gags) in the invasion of host cells by chlamydia pneumoniae strains. Group: Enzymes. Synonyms: Keratinase; KerA; Keratinase from Bacillus licheniformis; Keratinolytic protease; EC 3.4.21. Enzyme Commission Number: EC 3.4.21. Keratinase. Mole weight: ~39 kDa. Activity: 300 - 1000 units/mg. Storage: Store at -20°C. Form: Lyophilized powder. Source: E. coli BL21. Keratinase; KerA; Keratinase from Bacillus licheniformis; Keratinolytic protease; EC 3.4.21. Cat No: NATE-0853. | |
| Kiwifruit concentrate powder | Kiwifruit concentrate powder contains a naturally potent proteolytic enzyme, actinidin, which enhances protein digestion. In-vitro studies have shown that actinidin enhances the digestion of a number of different food proteins, including soy, red meat, milk, gluten and gliaden. Kiwifruit concentrate powder may also help to improve gut motility, which is an important contributor to improved bowel function. The active enzyme content of Kiwifruit concentrate powder is protected by specialised pre-processing and freeze drying techniques which maintain optimal temperature and pH conditions. Group: Others. Activity: >20,000 u/g. Appearance: green to brown powder. Form: Freeze dried powder. Source: green kiwifruit. Actinidin; Kiwifruit concentrate powder; Kiwifruit powder. Cat No: KCP-001. | |
| Matrix Metalloproteinase-13 (HisoTag) from Human, Recombinant | Matrix metalloproteinases are members of a unique family of proteolytic enzymes that have a zinc ion at their active sites and can degrade collagens, elastin and other components of the extracellular matrix (ECM). These enzymes are present in normal healthy individuals and have been shown to have an important role in processes such as wound healing, pregnancy, and bone resorption. However, overexpression and activation of MMPs have been linked with a range of pathological processes and disease states involved in the breakdown and remodeling of the ECM. Such diseases include tumor invasion and metastasis, rheumatoid arthritis, periodontal disease and vascular pr..., a ca2+- and zn2+- binding catalytic domain, a hinge region, and a c-terminal hemopexin domain. hydrolyzes collagen type ii 5-6 times faster than collagens type i and iii. exhibits high activity towards gelatin and degrades α1-antichymotrypsin and plasminogen activator inhibitor-2. Group: Enzymes. Synonyms: Collagenase-3; Matrix metallopeptidase 13; MMP13; CLG3; MANDP1; MMP-13. Purity: >90% by SDS-PAGE. Matrix Metalloproteinase. Mole weight: 60 kDa. Activity: >50 mU/mg protein. Storage: < -70°C; Avoid freeze/thaw. Form: Liquid. Source: S. frugiperda. Species: Human. Collagenase-3; Matrix metallopeptidase 13; MMP13; CLG3; MANDP1; MMP-13. Cat No: NATE-0859. | |
| Matrix Metalloproteinase-1 from Human, Recombinant | Matrix metalloproteinases are members of a unique family of proteolytic enzymes that have a zinc ion at their active sites and can degrade collagens, elastin and other components of the extracellular matrix (ECM). These enzymes are present in normal healthy individuals and have been shown to have an important role in processes such as wound healing, pregnancy, and bone resorption. However, overexpression and activation of MMPs have been linked with a range of pathological processes and disease states involved in the breakdown and remodeling of the ECM. Such diseases include tumor invasion and metastasis, rheumatoid arthritis, periodontal disease and vascular processe...may also undergo autocatalysis to yield a 27 kda/22 kda active enzyme. expressed by a large number of cell types. cleaves fibrillar type i collagen. must be activated just prior to use. Group: Enzymes. Synonyms: Matrix Metalloproteinase 1; Human Interstitial Collagenase; Collagenase-1; EC 3.4.24.7; vertebrate collagenase. Enzyme Commission Number: EC 3.4.24.7. CAS No. 9001-12-1. Purity: >90% by SDS-PAGE. Matrix Metalloproteinase. Mole weight: 56 kDa/52 kDa. Activity: >15 mU/mg protein. Storage: < -70°C; Avoid freeze/thaw. Form: Liquid. Source: Human Rheumatoid Synovial Fibroblast. Species: Human. Matrix Metalloproteinase 1; Human Interstitial Collagenase; Collagenase | |
| Matrix Metalloproteinase-2 from Human, Recombinant | Matrix metalloproteinases are members of a unique family of proteolytic enzymes that have a zinc ion at their active sites and can degrade collagens, elastin and other components of the extracellular matrix (ECM). These enzymes are present in normal healthy individuals and have been shown to have an important role in processes such as wound healing, pregnancy, and bone resorption. However, overexpression and activation of MMPs have been linked with a range of pathological processes and disease states involved in the breakdown and remodeling of the ECM. Such diseases include tumor invasion and metastasis, rheumatoid arthritis, periodontal disease and vascular processe... does not interfere with activation. may contain up to 10% timp proteins. during storage, a small portion (less than 10%) of the enzyme may also become activated. Group: Enzymes. Synonyms: 72 kDa Gelatinase; Matrix Metalloproteinase 2; Gelatinase A; EC 3.4.24.24; type IV collagenase; 3/4 collagenase; matrix metalloproteinase 5; 72 kDa gelatinase type A; collagenase IV; collagenase type IV; MMP 2; type IV collagen metalloproteinase; type IV collagenase/gelatinase. Enzyme Commission Number: EC 3.4.24.24. CAS No. 146480-35-5. Purity: >90% by SDS-PAGE. Matrix Metalloproteinase. Mole weight: 72 kDa. Storage: < -70°C; Avoid freeze/thaw. Form: Liquid. Source: CHO Cells. Spe | |
| Matrix Metalloproteinase-8 from Human, Recombinant | Full-length recombinant human neutrophil pro-collagenase (MMP-8), latent form. Matrix metalloproteinase 8 (MMP-8), or neutrophil collagenase, degrades interstitial collagens, acting preferentially on collagen type I. Increased full-length MMP-8 protein was associated with infiltration into the skin of neutrophils, which are the major cell type that expresses MMP-8. MMP-8 is synthesized and stored in specific granules in neutrophil leukocytes. MMP-8 activity is therefore regulated by factors such as surface-bound ligands (IgG or complement components) that release it through degranulation.Once released and activated through proteolytic or oxidative mechanisms, MMP-8 p...ollagenase activity. Group: Enzymes. Synonyms: Neutrophil collagenase; EC 3.4.24.34; Matrix metalloproteinase-8; MMP-8; PMNL collagenase; PMNL-CL; HNC; CLG1. Enzyme Commission Number: EC 3.4.24.34. CAS No. 9001-12-1. Purity: Greater than 90% as determined by SDS-PAGE. Matrix Metalloproteinase. Mole weight: 75 kDa. Activity: 100 units/ml. Stability: MMP-8 although stable at 4°C for 1 week, should be stored desiccated below -18°C. Please prevent freeze-thaw cycles. Appearance: Sterile Filtered clear solution. Source: E. coli. Species: Human. Neutrophil collagenase; EC 3.4.24.34; Matrix metalloproteinase-8; MMP-8; PMNL collagenase; PMNL-CL; HNC; CLG1. Cat No: NATE-0862. | |
| Matrix Metalloproteinase-9 from Human, Recombinant | Matrix metalloproteinases are members of a unique family of proteolytic enzymes that have a zinc ion at their active sites and can degrade collagens, elastin and other components of the extracellular matrix (ECM). These enzymes are present in normal healthy individuals and have been shown to have an important role in processes such as wound healing, pregnancy, and bone resorption. However, overexpression and activation of MMPs have been linked with a range of pathological processes and disease states involved in the breakdown and remodeling of the ECM. Such diseases include tumor invasion and metastasis, rheumatoid arthritis, periodontal disease and vascular processe...(less than 10%) of the enzyme may also become activated. requires activation prior to use. a simple activation protocol is included. Applications: Immunoblotting (1 ug protein/lane) substrate cleavage assay (1 ug protein/lane) zymography (1 ug protein/lane). Group: Enzymes. Synonyms: Gelatinase B; EC 3.4.24.35; 92-kDa gelatinase; matrix metalloproteinase 9; type V collagenase; 92-kDa type IV collagenase; macrophage gelatinase; 95 kDa type IV collagenase/gelatinase; collagenase IV; collagenase type IV; gelatinase MMP 9; MMP 9; type IV collagen metalloproteinase. Enzyme Commission Number: EC 3.4.24.35. CAS No. 146480-36-6. Purity: >90% by SDS-PAGE. Matrix Metalloprotei | |
| Methylation modified Trypsin from Porcine, Recombinant | Trypsin specifically hydrolyzes peptide bonds at the carboxyl side of lysine and arginine residues. Recombinant trypsin is free of any other proteases activities, and TPCK is unnecessary and not contained. Unmodified trypsin is subject to auto-proteolysis, generating fragments that can interfere with protein sequencing or HPLC/MS peptides analysis. Sequencing grade modified trypsin is recombinant porcine trypsin modified by reductive methylation, rendering it resistant to proteolytic digestion. Applications: Protein digests for peptide mapping applications or protein identification by peptide mass fingerprinting or ms/ms spectral matching. it is suitable for digest...under -70°C, It is stable within 24 months.2. Above 95% activity is remained after 5 times repeated freezing and thawing.3. Above 90% activity is remained after kept under 4°C or 25°C for 24h.4. A 0.05 mg/ml solution of sequencing grade modified recombinant trypsin in 50mM NH4HCO3 is retained above 95% after a 3 hours incubation at 37 °C. For long-term such as 20hours incubation, 1mM CaCl2 is recommended to be contained. Form: Lyophilized. Source: E. coli. Species: Porcine. α-trypsin; β-trypsin; cocoonase; parenzyme; parenzymol; tryptar; trypure; pseudotrypsin; tryptase; tripcellim; sperm receptor hydrolase; Alpha-trypsin; Beta-trypsin; EC 3.4.21.4; Tryp | |
| Nα-Benzoyl-L-arginine 4-nitroanilide hydrochloride | A chromogenic substrate for trypsin, papain & other proteolytic enzymes. Synonyms: Bz-L-Arg-pNA HCl; N-[(2S)-5-(diaminomethylideneamino)-1-(4-nitroanilino)-1-oxopentan-2-yl]benzamide hydrochloride; L-BAPA,L-BAPNA,BANI; Nalpha-Benzoyl-L-arginine 4-nitroanilide hydrochloride; BANI; L-BAPNA. Grades: ≥ 98% (HPLC). CAS No. 21653-40-7. Molecular formula: C19H22N6O4·HCl. Mole weight: 434.90. | |
| Native Aeromonas proteolytica Aminopeptidase | Aminopeptidase from Aeromonas proteolytica is a metalloenzyme, which contains 2 atoms of Zn2+ in a single polypeptide with an approximate molecular weight of 29.5 kDa as determined by sedimentation. This enzyme has a high degree of stability, being stable even at tempeRatures of 70°C for several hours. Partial inactivation occurs in 8 M urea. Maximum stability and activity are between pH 8.0-8.5. Aminopeptidase from Aeromonas proteolytica can function as an esterase. Applications: Aminopeptidases are a family of widely distributed proteases, which may be used to study many significant biological processes such as protein maturation, hormone production, and peptide digestion. the enzyme has been used to measure the kinetic rate constant for the binding of bestatin, a general protease inhibitor, to aminopeptidase. Group: Enzymes. Synonyms: Aminopeptidase; 37288-67-8; EC 3.4.11.10; Aeromonas proteolytica aminopeptidase. Enzyme Commission Number: EC 3.4.11.10. CAS No. 37288-67-8. Aminopeptidase. Storage: -20°C. Form: lyophilized powder, 50-150 units/mg protein. Source: Aeromonas proteolytica. Aminopeptidase; 37288-67-8; EC 3.4.11.10; Aeromonas proteolytica aminopeptidase. Cat No: NATE-0071. | |
| Native Bacillus licheniformis Keratinase (feed grade) | Keratinase is a particular class of extracellular proteolytic inducible enzyme with the capability of degrading insoluble keratin substrates. It is important for hydrolyzing hair, feather, and collagen in sewage system during waste water treatment. It is also useful in food industry, animal feed preparation etc. Insoluble feather keratin from poultry industry may be converted by enzymatic hydrolysis to glues, feedstuffs, fertilizers, films or used for the production of rare amino acids serine, cysteine and proline. Group: Enzymes. Synonyms: KerA; Keratinolytic protease; EC 3.4.21. Enzyme Commission Number: EC 3.4.21. Keratinase. Form: Powder. Source: Bacillus licheniformis. Keratinase; KerA; Keratinase from Bacillus licheniformis; Keratinolytic protease; EC 3.4.21. Cat No: FEED-0001. | |
| 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 Bacillus polymyxa Neutral Protease (Dispase) | Neutral protease (Dispase) is a non-mammalian animal origin free (AOF) metallo, neutral protease. Its mild proteolytic action makes the enzyme especially suitable for the preparation of primary cells and secondary (subcultivation) cell culture, since it is gentle on cell membranes. This protease is also used as a secondary enzyme in cell isolation and tissue dissociation applications, commonly used with collagense. Chromatographically purified. a lyophilized powder. Applications: Tissue disaggregation and subcultivation; prevention of unwanted cell clumping; preparation of cells for culture; separation of intact epidermis from dermis and intact epithelial sheet in c...se; Neutral Protease (Dispase). Enzyme Commission Number: EC 3.4.24.28. CAS No. 9001-92-7. Purity: Chromatographically purified. Neutral Protease. Mole weight: 32.5 kDa. Activity: > 4 units per mg dry weight. Stability: Stable at 2-8°C for 12 months. Aliquot and Store at -20°C after reconstitution with water or commonly used balanced salt solutions or media. Storage: Store at 2-8°C. Form: lyophilized powder. Source: Bacillus polymyxa. Bacillolysin; EC 3.4.24.28; Bacillus metalloendopeptidase; Bacillus subtilis neutral proteinase; anilozyme P 10; Bacillus metalloproteinase; Bacillus neutral proteinase; megateriopeptidase; Neutral Protease (Dispase). Cat No: NATE-0482. | |
| Native Bacillus Subtilis Sutilains (industry grade) | Sutilain, a proteolytic enzyme isolated from Bacillus subtilis, has been used for the treatment of burns. Group: Enzymes. Synonyms: Proteinase; Bacillus subtilis; sutilain. CAS No. 12211-28-8. Purity: > 90%. Source: Bacillus subtilis. Proteinase; Bacillus subtilis; sutilain. Cat No: NATE-1631. | |
| Native Bovine α-Chymotrypsinogen A | Chymotrypsinogen is a proteolytic enzyme and a precursor (zymogen) of the digestive enzyme chymotrypsin. It is a single polypetide chain consisting of 245 amino acid residues. It is synthesized in the acinar cells of the pancreas and stored inside membrane-bounded granules at the apex of the acinar cell. The cell is then stimulated by either a hormonal signal or a nerve impulse and the contents of the granules spill into a duct leading into the duodenum. Applications: The enzyme has been used in the non-invasive determination of solid-state protein conformation using near infrared (nir) spectroscopy. it has been used to study the partitioning of protein in polymer/polymer aqueous two-phase systems. the enzyme has also been used for self-interaction chromatography applications, to test the rapid measurement of protein osmotic second virial coefficients. in this technique, the protein is immobilized on chromatographic particles and its retention is measured using isocratic elution. Group: Zymogens. Synonyms: 9035-75-0; Chymotrypsinogen; α-Chymotrypsino. CAS No. 9035-75-0. Chymotrypsinogen A. Activity: > 40 units/mg solid. Storage: -20°C. Form: essentially salt-free, lyophilized powder. Source: Bovine Pancreas. Species: Bovine. 9035-75-0; Chymotrypsinogen; α-Chymotrypsinogen A; Chymotrypsinogen A; Chymotrypsin. Cat No: NATE-0748. | |
| Native Bovine Chymotrypsinogen A | Chymotrypsinogen is a proteolytic enzyme and a precursor (zymogen) of the digestive enzyme chymotrypsin. It is a single polypetide chain consisting of 245 amino acid residues. It is synthesized in the acinar cells of the pancreas and stored inside membrane-bounded granules at the apex of the acinar cell. The cell is then stimulated by either a hormonal signal or a nerve impulse and the contents of the granules spill into a duct leading into the duodenum. Group: Zymogens. Synonyms: chymotrypsinogen A; Chymotrypsinogen; Chymotrypsin. CAS No. 9035-75-0. Purity: Purified, Five times crystallized, electrophoretically homogeneous. Chymotrypsinogen A. Activity: Activates to at least 45 units per mg protein. Stability: The enzyme is stable for days in solution at pH 3.0 and for years as a dry powder when stored refrigerated. Storage: Store at 2-8°C. Form: lyophilized powder. Source: Bovine Pancreas. Species: Bovine. chymotrypsinogen A; Chymotrypsinogen; Chymotrypsin. Cat No: NATE-0134. | |
| Native Bovine Factor X Activated (Xa) | Factor Xa catalyzes the hydrolysis of the Arg-Thr and then Arg-Ile bonds in prothrombin to yield active thrombin. The fairly strict recognition sequence is Ile-Glu (or Asp)-Gly-Arg-↓-X. It may sometimes cleave at other basic residues, depending on the conformation of the target protein. Factor Xa will not cleave if a proline residue follows the arginine of the recognition sequence. Factor xa is a serine endoproteinase and a member of the s1 peptidase family. factor xa plays a critical role in the coagulation cascade by catalyzing the proteolytic conversion of prothrombin to active thrombin. factor xa?s prothrombin conversion activity is greatly enhanced in vivo when c...d with 10 μg of factor xa for 2.5 hours at 37 oc. Group: Enzymes. Synonyms: EC 3.4.21.6; 9002-05-5; thrombokinase; prothrombase; prothrombinase; activated blood-coagulation factor X; autoprothrombin C; thromboplastin; plasma thromboplastin; factor Xa; activated Stuart-Prower factor; activated factor X; coagulation factor Xa. Enzyme Commission Number: EC 3.4.21.6. CAS No. 9002-5-5. Factor Xa. Storage: -20°C. Form: aqueous glycerol solution. Source: Bovine plasma. Species: Bovine. EC 3.4.21.6; 9002-05-5; thrombokinase; prothrombase; prothrombinase; activated blood-coagulation factor X; autoprothrombin C; thromboplastin; plasma thromboplastin; factor Xa; activated Stuart-Pr | |
| Native Bovine Thrombin | Thrombin is a serine protease that in humans is encoded by the F2 gene. Prothrombin (coagulation factor II) is proteolytically cleaved to form thrombin in the coagulation cascade, which ultimately results in the reduction of blood loss. Thrombin in turn acts as a serine protease that converts soluble fibrinogen into insoluble strands of fibrin, as well as catalyzing many other coagulation-related reactions. Thrombin is the final coagulation protease in regard to hemostasis, promoting both procoagulant and anticoagulant effects. Applications: Thrombin is used for site specific cleavage of recombinant fusion proteins containing an accessible thrombin recognition site for removal of ...Ia; E thrombin; β-thrombin; γ-thrombin. Enzyme Commission Number: EC 3.4.21.5. CAS No. 9002-4-4. Thrombin. Activity: 600-2,000 NIH units/mg protein (biuret) or > 2,000 NIH units/mg protein (E1%/280 = 19.5); > 125 NIH units/mg protein (biuret). Form: Type I, Lyophilized from saline sodium Citrate buffer, pH 6.5; Type II, buffered aqueous solution, In 0.05 M phosphate buffer, pH 7.0. Source: Bovine plasma. Species: Bovine. thrombin; 9002-04-4; EC 3.4.21.5; 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: NATE-0698. | |
| Native Candida Rugosa Cholesterol Esterase | Cholesterol esterase (CE) is also known as cholesterol ester hydrolase. This enzyme catalyzes the following reaction: Sterol Ester --------> Sterol + Fatty Acid.Cholesterol esterase activity has been demonstrated in pancreas, intestine, liver and kidney. The enzyme is inactivated by proteolytic enzymes but stabilized by proteolytic enzyme inhibitors and by bile salts. CE from rat pancreas has a molecular weight of 65,000-69,000. In the presence of bile salts, it aggregates to a hexamer which is possibly the active form of the enzyme. Group: Enzymes. Synonyms: cholesterol esterase; cholesteryl ester synthase; triterpenol esterase; cholesteryl esterase; cholesteryl ester hydrolase; sterol ester hydrolase; cholesterol ester hydrolase; cholesterase; acylcholesterol lipase; sterol esterase; CE. Enzyme Commission Number: EC 3.1.1.13. CAS No. 9026-00-0. Purity: 0.9. Cholesterol Esterase. Activity: 25-100 U/mg. Storage: Store at -20° C. Form: Freeze-dried powder. Source: Candida Rugosa. cholesterol esterase; cholesteryl ester synthase; triterpenol esterase; cholesteryl esterase; cholesteryl ester hydrolase; sterol ester hydrolase; cholesterol ester hydrolase; cholesterase; acylcholesterol lipase; sterol esterase; CE. Cat No: NATE-1679. | |
| Native Flavobacterium menigosepticum Endoproteinase AspN | Endopeptidase or endoproteinase are proteolytic peptidases that break peptide bonds of nonterminal amino acids (i.e. within the molecule), in contrast to exopeptidases, which break peptide bonds from end-pieces of terminal amino acids. For this reason, endopeptidases cannot break down peptides into monomers, while exopeptidases can break down proteins into monomers. A particular case of endopeptidase is the oligopeptidase, whose substrates are oligopeptides instead of proteins. Endoproteinase aspn (flavastacin) is a zinc metalloendopeptidase which selectively cleaves peptide bonds n-terminal to aspartic acid residues. this enzyme is recommended to digest peptides with molecular weights of 5 kda or less. Applications: O digestion of proteins for proteomic analysis by mass spectrometry o protein and peptide identification. Group: Enzymes. Synonyms: Endopeptidase; endoproteinase. CAS No. 9001-92-7. Endoproteinase Asp-N. Mole weight: 40089.9 daltons. Activity: 25 μmol/min/mg. Storage: at -20°C. Form: Supplied in lyophilized form. Source: Flavobacterium menigosepticum. Endopeptidase; endoproteinase; Endoproteinase AspN; Endoproteinase Asp-N. Cat No: NATE-1274. | |
| Native Human Factor XIa | Prepared from Human Factor XI using Human Factor Xlla. This Xlla was removed using a corn trypsin inhibitor column. Complete activation is observed by SDS-PAGE. Factor XI, through the contact factor pathway cascade, is activated to Factor XIa via Factor Xlla and High Molecular Weight Kininogen. During activation by Factor Xlla and HK, FXI undergoes proteolytic cleavage in which the Mr=80,000 chain reportedly is cleaved to a heavy and light chain with Mr of about 48,000 and 33,000. This Factor XIa is responsible for the activation of Factor IX to Factor IXa. Unlike other examples of activation of Vitamin K-dependent blood-clotting proteins, Factor XIa proteolysis of Factor IX does not require membrane surfaces. Group: Enzymes. Synonyms: Human Factor XIa; Factor XIa. Factor XIa. Mole weight: 160 kDa. Storage: < -60°C. Source: Human. Species: Human. Human Factor XIa; Factor XIa. Cat No: NATE-0886. | |
| Native Human Proteinase 3 | Proteinase 3 also known as PRTN3 is an enzyme that in humans is encoded by the PRTN3 gene. PRTN3 is a serine protease enzyme expressed mainly in neutrophil granulocytes. Its exact role in the function of the neutrophil is unknown, but, in human neutrophils, proteinase 3 contributes to the proteolytic generation of antimicrobial peptides. It is also the epitope of anti-neutrophil cytoplasmic antibodies (ANCAs) of the c-ANCA (cytoplasmic subtype) class, a type of antibody frequently found in the disease granulomatosis with polyangiitis (formerly known as "Wegener's granulomatosis"). Group: Enzymes. Synonyms: PRTN3; proteinase 3; ACPA; AGP7; C-ANCA; CANCA; MBN; MBT; NP-4; NP4; P29; PR-3; PR3; EC 3.4.21.76. Enzyme Commission Number: EC 3.4.21.76. CAS No. 128028-50-2. Purity: > 96% (SDS-PAGE). PRTN3. Activity: Typically > 0.1 U/mg protein. Storage: -20°C. Form: Liquid. Source: Human Neutrophils. Species: Human. PRTN3; proteinase 3; ACPA; AGP7; C-ANCA; CANCA; MBN; MBT; NP-4; NP4; P29; PR-3; PR3; EC 3.4.21.76. Cat No: NATE-0620. | |
| Native Human Thrombin | Thrombin is a serine protease that in humans is encoded by the F2 gene. Prothrombin (coagulation factor II) is proteolytically cleaved to form thrombin in the coagulation cascade, which ultimately results in the reduction of blood loss. Thrombin in turn acts as a serine protease that converts soluble fibrinogen into insoluble strands of fibrin, as well as catalyzing many other coagulation-related reactions. Lyophilized powder containing sucrose, sodium chloride and tris. thrombin is the final coagulation protease in regard to hemostasis, promoting both procoagulant and anticoagulant effects. Group: Enzymes. Synonyms: thrombin; 9002-04-4; EC 3.4.21.5; fibrinogenase; thrombase; thrombofort; topical; thrombin-C; tropostasin; activated blood-coagulation factor II; blood-coagulation factor IIa; factor IIa; E thrombin; β-thrombin; γ-thromb. Enzyme Commission Number: EC 3.4.21.5. CAS No. 9002-4-4. Thrombin. Activity: 600-2,000 NIH units/mg protein (biuret) or > 2,000 NIH units/mg protein (E1%/280 = 19.5); > 125 NIH units/mg protein (biuret). Form: lyophilized powder. Source: Human plasma. Species: Human. thrombin; 9002-04-4; EC 3.4.21.5; 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: NATE-0699. | |
| Native Papaya latex Chymopapain | Chymopapain is a proteolytic enzyme isolated from the latex of papaya (Carica papaya). It is a medication used to treat herniated lower lumbar discs in the spine. Chymopapain injections are normally given under local, Rather than general, anaesthesia. The dose for a single intervertebral disc is 2 to 4 nanokatals, with a maximum dose per patient of 8 nanokatals. The procedure is referred to as chemonucleolysis. Applications: Chymopapain from papaya latex has been used in a study to assess the anthelmintic effect of natural plant cysteine proteinases against the gastrointestinal nematode, heligmosomoides. chymopapain from papaya latex has also been used in a study to investiga...enzyme has been used along with pronase, collagenase, elastase, dnase, and catalase for rabbit lung cells digestion at a concentration of 0.05% in calcium-magnesium-free kreb?s serum substitute. it has also been used for the release of neuroblastoma cells from marrow bound to antibody-coated microspheres. Group: Enzymes. Synonyms: chymopapain A; chymopapain B; chymopapain S; EC 3.4.22.6; 9001-09-6; Chymodiactin. Enzyme Commission Number: EC 3.4.22.6. CAS No. 9001-9-6. Chymopapain. Activity: > 2.0 units/mg protein. Storage: -20°C. Form: lyophilized powder. Source: Papaya latex. chymopapain A; chymopapain B; chymopapain S; EC 3.4.22.6; 9001-09-6; Chymodiactin. Cat No: NATE-0133. | |
| Native Pineapple Bromelain | Bromelain is a cysteine endopeptidase with broad specificity for cleavage of proteins. Bromelain may be from a stem or piece of fruit. Stem bromelain (SBM) (EC 3.4.22.32), a proteolytic enzyme, is a widely accepted phytotherapeutical drug member of the bromelain family of proteolytic enzymes obtained from Ananas comosus. Some of the therapeutic benefits of SBM are reversible inhibition of platelet aggregation, angina pectoris, bronchitis, sinusitis, surgical traumas, thrombophlebitis, pyelonephritis and enhanced absorption of drugs, particularly of antibiotics. Its anti-metastasis and anti-inflammatory activities are apparently independent of its proteolytic activity. Applications: Bromelain may be used to inhibit the biosysnthesis of proinflammatory prostaglandins. it may be used to reduce clotting efficiency. bromelain, from pineapple stem, has been used to make enzymatic hydrolysates of honeybee-collected pollen. Group: Enzymes. Synonyms: stem bromelain; EC 3.4.22.32; 37189-34-7; bromelain; pineappl. Enzyme Commission Number: EC 3.4.22.32. CAS No. 37189-34-7. Bromelain. Activity: > 3 units/mg protein; 5-15 units/mg protein. Form: Lyophilized powder containing mannitol and potassium phosphate buffer salts. Source: Pineapple stem. Species: Pineapple. stem bromelain; EC 3.4.22.32; 37189-34-7; bromelain; pineapple stem bromelain; SBM. Cat No: NATE-0665. | |
| Native Porcine Cholesterol Esterase | The enzyme is found primarily in pancreas and pancreatic secretions, but in other tissues as well. Bile salts, such as cholate and its conjugates, act as stabilizers of the native polymeric form of the enzyme and can protect it from proteolytic degradation in the intestine. Applications: Determination of cholesterol in serum and plasma, with cholesterol oxidase or peroxidase synthesis of optically active alcohols and carboxylic acids (via ester hydrolysis, esterification, or transesterification). Group: Enzymes. Synonyms: cholesterol esterase; cholesteryl ester synthase; triterpenol esterase; cholesteryl esterase; cholesteryl ester hydrolase; sterol ester hydrolase; cholesterol ester hydrolase; cholesterase; acylcholesterol lipase; EC 3.1.1.13; 9026-00-0; sterol esterase; CE. Enzyme Commission Number: EC 3.1.1.13. CAS No. 9026-00-0. Cholesterol Esterase. Activity: > 300 units per gram dry weight. Storage: Store at -20°C. Form: Lyophilized powder. Source: Porcine pancreas. Species: Porcine. cholesterol esterase; cholesteryl ester synthase; triterpenol esterase; cholesteryl esterase; cholesteryl ester hydrolase; sterol ester hydrolase; cholesterol ester hydrolase; cholesterase; acylcholesterol lipase; EC 3.1.1.13; 9026-00-0; sterol esterase; CE. Cat No: NATE-0115. | |
| Native Porcine Leucine Aminopeptidase | Leucine aminopeptidase (LAP) is a proteolytic enzyme which hydrolyzes the peptide bond adjacent to a free amino group. It is called leucine aminopeptidase because it rapidly catalyzes the hydrolysis of leucine containing peptides. However, it also catalyzes the hydrolytic release of other amino acids located at the N-terminal end of various peptides and proteins. The enzyme from porcine kidney has been extensively studied. It has a molecular weight of 255,000 and it consists of four subunits each having one atom of zinc. Group: Enzymes. Synonyms: Leucine Aminopeptidase; 9054-63-1; leucyl peptidase; peptidase S; cytosol aminopeptidase; cathepsin III; L-leucine aminopeptidase; leucinaminopeptidase; leucinamide aminopeptidase; FTBL proteins; proteinates FTBL; aminopeptidase II; aminopeptidase III; aminopeptidas. Enzyme Commission Number: EC 3.4.11.1. Purity: 90% (biuret). LAP. Activity: >100 U/mg protein. Storage: Stable when stored at 4°C. Do not freeze. Form: Ammonium Sulfate. Source: Porcine Kidney. Species: Porcine. Leucine Aminopeptidase; 9054-63-1; leucyl peptidase; peptidase S; cytosol aminopeptidase; cathepsin III; L-leucine aminopeptidase; leucinaminopeptidase; leucinamide aminopeptidase; FTBL proteins; proteinates FTBL; aminopeptidase II; aminopeptidase III; aminopeptidase I; EC 3.4.11.1; leucyl aminopeptidase; LAP. Cat No: NATE-1879. | |
| Native Porcine Pepsin | Pepsin is one of the principal protein degrading or proteolytic enzymes in the digestive system. During the process of digestion, Pepsin acts on the complex dietary protein and breaks up into peptides and amino acids which can be readily absorbed by the intestinal lining. It helps in digestive disturbance in general and as a result of impaired production of gastric juice. It acts as an adjunct in the treatment of anemic conditions, especially during slimming diet when protein intake increases. It is used as research tool in protein analysis and as digestive syrup in heart burn, acid indigestion and sour stomach. It is also used in tablets for increasing appetite and in the preparation of cheese and other protein-containing foods. Group: Enzymes. Synonyms: EC 3.4.23.1; pepsin; lactated pepsin; pepsin fortior; fundus-pepsin; elixir lactate of pepsin; P I; lactated pepsin elixir; P II; pepsin R; pepsin D; Pepsin A. Enzyme Commission Number: EC 3.4.23.1. CAS No. 9001-75-6. Pepsin. Activity: 10000U/g. Source: Porcine Stomach. Species: Porcine. EC 3.4.23.1; pepsin; lactated pepsin; pepsin fortior; fundus-pepsin; elixir lactate of pepsin; P I; lactated pepsin elixir; P II; pepsin R; pepsin D; Pepsin A. Cat No: PHAM-242. | |
| Native Porcine Thrombin | Thrombin is a serine protease that in humans is encoded by the F2 gene. Prothrombin (coagulation factor II) is proteolytically cleaved to form thrombin in the coagulation cascade, which ultimately results in the reduction of blood loss. Thrombin in turn acts as a serine protease that converts soluble fibrinogen into insoluble strands of fibrin, as well as catalyzing many other coagulation-related reactions. Applications: Diagnostic controls, calibrators & standards; immunoassays; testing/assay validation; life science; manufacturing; coagulation/anemia. Group: Enzymes. Synonyms: thrombin; alpha Subunit Thrombin. Thrombin. Mole weight: 362 kDa. Activity: > 1,000 NIH U/mg. Stability: 2 years. Storage: Store at -20°C. Form: Liquid in 0.05 M sodium Citrate, 0.2 M NaCl, 0.1% PEG-8,000, pH 6.5. Source: Porcine Plasma. Species: Porcine. thrombin; EC 3.4.21.5; fibrinogenase; thrombase; thrombofort; topical; thrombin-C; tropostasin; activated blood-coagulation factor II; blood-coagulation factor IIa; factor IIa; E thrombin; β-thrombin; γ-thrombin; alpha Subunit Thrombin. Cat No: NATE-0970. | |
| Native Rabbit Thrombin | Thrombin is a serine protease that in humans is encoded by the F2 gene. Prothrombin (coagulation factor II) is proteolytically cleaved to form thrombin in the coagulation cascade, which ultimately results in the reduction of blood loss. Thrombin in turn acts as a serine protease that converts soluble fibrinogen into insoluble strands of fibrin, as well as catalyzing many other coagulation-related reactions. The nih assay procedure uses 0.2 ml diluted plasma (1:1 with saline) as a substrate and 0.1 ml of thrombin sample (stabilized in a 1% buffered albumin solution) based on a modification of the method of biggs. only clotting times in the range of 15-25 seconds are used for determining thrombin concentrations. activity is expressed in nih units obtained by direct comparison to a nih thrombin reference standard. Group: Enzymes. Synonyms: thrombin; 9002-04-4; EC 3.4.21. Enzyme Commission Number: EC 3.4.21.5. CAS No. 9002-4-4. Thrombin. Activity: 600-2,000 NIH units/mg protein (biuret) or > 2,000 NIH units/mg protein (E1%/280 = 19.5); > 125 NIH units/mg protein (biuret). Source: Rabbit plasma. Species: Rabbit. thrombin; 9002-04-4; EC 3.4.21.5; 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: NATE-0700. | |
| Native Rat Thrombin | Thrombin is a serine protease that in humans is encoded by the F2 gene. Prothrombin (coagulation factor II) is proteolytically cleaved to form thrombin in the coagulation cascade, which ultimately results in the reduction of blood loss. Thrombin in turn acts as a serine protease that converts soluble fibrinogen into insoluble strands of fibrin, as well as catalyzing many other coagulation-related reactions. Thrombin is the final coagulation protease in regard to hemostasis, promoting both procoagulant and anticoagulant effects. Applications: Thrombin is used for site specific cleavage of recombinant fusion proteins containing an accessible thrombin recognition site for removal of affinity tags. thrombin has been used in a study to investigate activation of equine platelet-rich plasma. Group: Enzymes. Synonyms: thrombin; 9002-04-4; EC 3.4.21.5; fibrin. Enzyme Commission Number: EC 3.4.21.5. CAS No. 9002-4-4. Thrombin. Activity: 600-2,000 NIH units/mg protein (biuret) or > 2,000 NIH units/mg protein (E1%/280 = 19.5); > 125 NIH units/mg protein (biuret). Form: lyophilized powder. Source: Rat plasma. Species: Rat. thrombin; 9002-04-4; EC 3.4.21.5; 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: NATE-0701. | |
| Native Rhizopus sp. Protease | 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. Acidic protease exhibits both proteolytic and lipolytic activities. stable in the acid range of ph 3-5. ph optimum is 3.0. Applications: Protease from rhizopus spp. has been used in a study to assess the amino acid sequences near the amino termini using automated edman degradation. it has also been used in a study to investigate inactivation of the enzyme by reaction with diazoacetyl-dl-norleucine methyl ester in the presence of cupric acetate. Group: Enzymes. Synonyms: Protease; peptidase; proteinase; 9001-92-7. CAS No. 9001-92-7. Protease. Activity: > 0.2 unit/mg solid. Storage: 2-8°C. Form: Supplied as a powder containing dextrin as a stabilizer. Source: Rhizopus sp. Protease; peptidase; proteinase; 9001-92-7. Cat No: NATE-0629. | |
| 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. | |
| Native Streptomyces griseus Aminopeptidase I | Aminopeptidase I from S. griseus has a fairly broad specificity, being able to remove the N-terminal residue of most proteins, except where the penultimate residue is an imino acid. It contains two Zn2+ binding sites. Aminopeptidase I from S. griseus is inhibited by 1,10-phenanthroline and is activated six-fold by Ca2+, which also stabilizes it against heat inactivation. This monomeric zinc metalloprotein has an isoelectric point (pI) of 5.4. Applications: Aminopeptidase i from streptomyces griseus may be used as a reagent for the analysis of protein structure and as a model for studies of proteolytic enzyme activation by calcium ions. it may be used as a reagent in the assay of endoprotease activities with a synthetic substrate in a two-stage assay. the lyophilized powder also contains calcium acetate. Group: Enzymes. Synonyms: aminopeptidase III; aminopeptidase yscI; leucine aminopeptidase IV; yeast aminopeptidase I; EC 3.4.11.22; 9031-94-1; Aminopeptidase I. Enzyme Commission Number: EC 3.4.11.22. CAS No. 9031-94-1. Aminopeptidase I. Activity: > 200 units/mg protein. Storage: -20°C. Form: lyophilized powder. Contains calcium acetate. Source: Streptomyces griseus. aminopeptidase III; aminopeptidase yscI; leucine aminopeptidase IV; yeast aminopeptidase I; EC 3.4.11.22; 9031-94-1; Aminopeptidase I. Cat No: NATE-0070. | |
| Native Streptomyces griseus Protease | Protease from Streptomyces griseus is a mixture of at least three proteolytic activities including an extracellular serine protease. In general, serine proteases display a wide range of substrate specificities, which are believed to be mediated by an active site composed of one Asp, one His, and a Ser residue in the molecule. This enzyme prefers to hydrolyze peptide bonds on the carboxyl side of glutamic or aspartic acid. Collected from culture broth of s. griseus and purified by successive column procedures. a mixture of at least three proteolytic activities including an extracellular serine protease. in general, serine proteases display a wide range of substrate specifici...de aldehydes and serine proteases. protease is typically used in nucleic acid isolation procedures in incubations of 0.5-3.0 hours supplemented with 0.2% sodium dodecyl sulfate and 10 mm edta. the enzyme from creative enzymes has been used for the digestion and analysis of antithrombin-heparin complexes. it has also been used for the isolation of enzyme-resistant starch. this enzyme is more active at a higher ph range than the known alkaline protease, showing the proteolytic activity even in 0.2n naoh solution. this enzyme is useful for proteolysis of insoluble protein and for structure investigation of protein. Group: Enzymes. Synonyms: Protease; 9036-06-0; Actinase E, Pro | |
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