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| Product | Description | |
|---|---|---|
| Endo-protease | A protease enzyme used to hydrolyze protein to produce free-form amino acids for use as Free-Amino-Nitrogen (FAN).To increase the free amino-nitrogen content when brewing with high levels of raw wheat. Applications: Adding in the beginning of the mash, increasingremarkably the wort extract yield and the free amino-nitrogen content. Group: Enzymes. Synonyms: Endo-protease;protease enzyme; hydrolyze protein enzyme; as Free-Amino-Nitrogen; as FAN; Brewing; Endo-protease; BRE-1615. Endo-protease. Appearance: powder or liquid. Endo-protease;protease enzyme; hydrolyze protein enzyme; as Free-Amino-Nitrogen; as FAN; Brewing; Endo-protease; BRE-1615. Pack: 25kg/paper barrel (powder form), 30kg/polyster barrel (liquid form) or subject to client requirement. Cat No: BRE-1615. |  |
| Native Staph aureus V8 Protease (Endoproteinase Glu-C) | Protease S. aureus V8 (Endoproteinase-Glu-C) specifically cleaves peptide bonds on the COOH-terminal side of either aspartic or glutamic acids. In the presence of ammonium, the enzyme specificity is limited to glutamic sites. It has a molecular weight of 27 kDa daltons and optimum pH's of 4.0 and 7.8 with hemoglobin as the substrate. Protease S. aureus V8 is inhibited by diisopropylfluorophosphate and monovalent anions such as F-, Cl-, CH3COO-and NO3. Enzyme activity is determined by the casein digestion assay described by Drapeau. Protease s. aureus v8 (endoproteinase-glu-c) specifically cleaves peptide bonds on the cooh-terminal side of either aspartic or glutamic acids. Group: Enzymes. Synonyms: EC 3.4.21.19; Staph aureus V8 Protease; Prot. Enzyme Commission Number: EC 3.4.21.19. CAS No. 137010-42-5. Purity: Chromatographically purified. V8 Protease. Mole weight: 27 kDa (Drapeau 1978). Activity: > 500 units per mg dry weight. Stability: Autolysis occurs at temperatures > 40°C. The enzyme is fully active in USP 0.2% SDS. Stable for 12 months at 2-8°C. Storage: Store at 2-8°C. Form: Lyophilized powder. Source: Staph aureus V8. EC 3.4.21.19; Staph aureus V8 Protease; Protease, Staph aureus (Endoproteinase Glu-C); Glutamyl endopeptidase; V8 proteinase, endoproteinase Glu-C; staphylococcal serine proteinase. Cat No: NATE-0730. | |
| ADAMTS13 endopeptidase | In peptidase family M12. Group: Enzymes. Synonyms: ADAMTS VWF cleaving metalloprotease; ADAMTS-13; ADAMTS13;vWF-cleaving protease; VWF-CP; vWF-degrading protease; Upshaw factor; von Willebrand factor cleaving protease; ADAMTS13 peptidase. Enzyme Commission Number: EC 3.4.24.87. 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-4371; ADAMTS13 endopeptidase; EC 3.4.24.87; ADAMTS VWF cleaving metalloprotease; ADAMTS-13; ADAMTS13;vWF-cleaving protease; VWF-CP; vWF-degrading protease; Upshaw factor; von Willebrand factor cleaving protease; ADAMTS13 peptidase. Cat No: EXWM-4371. | |
| α-lytic endopeptidase | From the myxobacterium Lysobacter enzymogenes. In peptidase family S1 (trypsin family). Group: Enzymes. Synonyms: myxobacter α-lytic proteinase; α-lytic proteinase; α-lytic protease; Mycobacterium sorangium α-lytic proteinase; Myxobacter 495 α-lytic proteinase; α-lytic proteinase; Myxobacter α-lytic proteinase; Mycobacterium sorangium α-lytic proteinase. Enzyme Commission Number: EC 3.4.21.12. CAS No. 37288-76-9. 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-4115; α-lytic endopeptidase; EC 3.4.21.12; 37288-76-9; myxobacter α-lytic proteinase; α-lytic proteinase; α-lytic protease; Mycobacterium sorangium α-lytic proteinase; Myxobacter 495 α-lytic proteinase; α-lytic proteinase; Myxobacter α-lytic proteinase; Mycobacterium sorangium α-lytic proteinase. Cat No: EXWM-4115. | |
| Aminopeptidase N Inhibitor | Membrane alanyl aminopeptidase is also known as alanyl aminopeptidase (AAP) or aminopeptidase N (AP-N), which is an enzyme that in humans is encoded by the ANPEP gene. Aminopeptidase N (AP-N) inhibitor is a reversible inhibitor of AP-N/CD13 (IC50 = 25 μM). It is selective for AP-N/CD13 over matrix metalloproteinase-9 (MMP-9), angiotensin converting enzyme (ACE), neutral endopeptidase (NEP), γ-glutamyl transpeptidase, and the serine proteases dipeptidyl peptidase 4 (DPP-4) and cathepsin G at a concentration of 1 mM. AP-N inhibitor is non-cytotoxic to U937 cells at a concentration of 100 μM. Human aminopeptidase N is a receptor for one strain of human coronavirus that is an important cause of upper respiratory tract infections. Defects in this gene appear to be a cause of various types of leukemia or lymphoma. Synonyms: AP-N Inhibitor. Grades: ≥95%. CAS No. 596108-59-7. Molecular formula: C17H10N2O8. Mole weight: 370.27. |  |
| Aspergillopepsin I | Aspergillopepsin I (Aspergillus acid protease) is an aspartic endopeptidase that catalyses the hydrolysis of peptide bonds in proteins, with broad specificity [1]. Uses: Scientific research. Group: Signaling pathways. Alternative Names: Aspergillus acid protease. CAS No. 9025-49-4. Pack Sizes: 5 g. Product ID: HY-P2973. |  |
| bothrolysin | A 22.5 kDa endopeptidase from the venom of the jararaca snake (Bothrops jararaca), insensitive to phosphoramidon at 0.5 mM. In peptidase family M12 (astacin family). Group: Enzymes. Synonyms: Bothrops metalloendopeptidase J; J protease. Enzyme Commission Number: EC 3.4.24.50. CAS No. 443890-65-1. 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-4332; bothrolysin; EC 3.4.24.50; 443890-65-1; Bothrops metalloendopeptidase J; J protease. Cat No: EXWM-4332. | |
| brachyurin | From hepatopancreas of the fiddler crab, Uca pugilator. In peptidase family S1 (trypsin family). Other serine endopeptidases that degrade collagen, but are not listed separately here, include a second endopeptidase from Uca pugilator, digestive enzymes from other decapod crustacea, and an enzyme from the fungus Entomophthora coronata. Group: Enzymes. Synonyms: Uca pugilator collagenolytic proteinase; crab protease I; crab protease II. Enzyme Commission Number: EC 3.4.21.32. CAS No. 848900-32-3. 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-4127; brachyurin; EC 3.4.21.32; 848900-32-3; Uca pugilator collagenolytic proteinase; crab protease I; crab protease II. Cat No: EXWM-4127. | |
| 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 mammalian monocytes. This enzyme is part of the family of inflammatory caspases, which also includes caspase-4 (EC 3.4.22.57) and caspase-5 (EC 3.4.22.58) in humans and caspase-11 (EC 3.4.22.64), caspase-12, caspase-13 and caspase-14 in mice. Contains a caspase-recruitment domain (CARD) in its N-terminal prodomain, which plays a role in procaspase activation. Cleaves pro-interleukin-1β (pro-IL-1β) to form mature IL-1β, a potent mediator of inflammation. Also activates the proinflammatory cytokine, IL-18, which is also known as interferon-γ-inducing factor. Inhibited by Ac-Tyr-Val-Ala-Asp-CHO. Caspase-11 plays a critical role in the activation of caspase-1 in mi...proteinase; ICE. Enzyme Commission Number: EC 3.4.22.36. CAS No. 122191-40-6. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4211; caspase-1; EC 3.4.22.36; 122191-40-6; interleukin 1β-converting enzyme; protease VII; protease A; interleukin 1β precursor proteinase; interleukin 1 converting enzyme; interleukin 1β-converting endopeptidase; interleukin-1β convertase; interleukin-1β converting enzyme; interleukin-1β precursor proteinase; prointerleukin 1β protease; precursor interleukin-1β converting enzyme; pro-interleukin 1β proteinase; ICE. Cat No: EXWM-4211. | |
| Cathepsin D from Human, recombinant | Cathepsin D is a lysosomal aspartyl protease composed of a protein dimer of disulfide-linked heavy and light chains, both produced from a single protein precursor. It is an estrogen-regulated protein associated with tissue breakdown. Levels of cathepsin D have been positively correlated with recurring breast cancers of both node negative and node positive types. Additionally cathepsin D has been associated with amyloid formation in Alzheimer's plaques. Cathepsin D is produced initially as a pre-pro-enzyme which gets transported to lysosomes via endosomes in most cell types. In endosomes, it gets proteolyzed by unidentified proteases by removal of the pro-peptide to generate...e cathepsins B and L generates mature, active double-chain Cathepsin D. Group: Enzymes. Synonyms: CTSD; 9025-26-7; EC 3.4.23.5; CLN10; CPSD; HEL-S-130P; Procathepsin D. Enzyme Commission Number: EC 3.4.23.5. CAS No. 9025-26-7. Purity: > 80% by SDS-PAGE. CTSD. Mole weight: 45.1 kDa. Activity: >100 pmol/min/mg. Storage: Store at -20°C. Stable for at least 6 months as supplied. Reconstitute to 1 mg/ml in sterile water, store at -80°C in aliquots and use within 6 months after reconstitution. Avoid repeated freeze-thaw cycles. Form: Freeze-Dried. Source: E. coli. Species: Human. CTSD; cathepsin D; 9025-26-7; EC 3.4.23.5; CLN10; CPSD; HEL-S-130P; Procathepsin D. Cat No: NATE-1707. | |
| Cathepsin S, human | Cathepsin S, human, is a potent cysteine protease that promotes the degradation of damaged or harmful proteins in the endolysosomal pathway. Cathepsin S, human, is involved in multiple pathological processes, including arthritis, cancer, and cardiovascular disease [1] [2]. Uses: Scientific research. Group: Signaling pathways. Alternative Names: CTSS. CAS No. 71965-46-3. Pack Sizes: 50 μg. Product ID: HY-E70226. | |
| Chicking biddy feed enzymes | It is developed according to the digestive physiology of chicks and typical diets. The results of experiments showed that the products could not only effectively supplement the digestive enzyme of chicks, but also inhibited the proliferation of pathogen, improved the health condition of chick, and then enhanced feed utilization ratio. Thus the growth rate was increased uniformly. Ingredients: Protease, amylase, lipase, xylanase, β-mannanase, α-galactosidase. Applications: 1. make up inadequate secretion of endogenous enzyme of chicks to improve animal feed intake and feed efficiency; 2. through inhibiting the proliferation of harmful microorganisms, to improve chick growth rate and colony homogeneity; 3. increase their survival rate by enhancing disease resistance of chicks; 4. by means of breaking down anti-nutritional factors in feed, to improve digestion and absorption of the dietary energy and protein; 5. it can reduce excretion of nitrogen and phosphorus, to reduce environmental pollution. Group: Enzymes. Synonyms: Chicking biddy feed enzymes; digestive enzymes; enhanced feed utilization ratio; impro. Chicking biddy feed enzymes. Appearance: pellet. Chicking biddy feed enzymes; digestive enzymes; enhanced feed utilization ratio; improve chick growth rate; FEED-2329. Pack: 25kg/barrel or subject to client requirement. Cat No: FEED-2329. | |
| Chondroitinase AC from Flavobacterium heparinum, Recombinant | Chondroitinase AC from Flavobacteriun heparinum is an eliminase that degrades chondroitin sulfates A and C, but not chondroitin sulfate B. The enzyme cleaves, via an elimination mechanism, both sulfated and non-sulfated polysaccharide chains that contain (1?4)-linkages between hexosamines and glucuronic acid residues. The reaction yields oligosaccharide products, mainly disaccharides, with unsaturated uronic acids that can be detected by UV spectroscopy at 232 nm. Applications: Chondroitinase ac was shown to inhibit melanoma invasion and proliferation, endothelial proliferation, and angiogenesis. chondroitinase ac, but not chondroitinase b, has also been shown t..., and protease activities. ChnAC. Activity: >200 units/mg protein. Appearance: Powder. Storage: Store the product at -20?C. When stored properly and unopened at -20?C, the enzyme has a recommended retest date of 2 years. After reconstitution, the product may be kept at 4?C for 4 days, but it is recommended to store the solution in working aliquots at -20 ?C. Form: The enzyme is supplied as a lyophilized powder containing potassium phosphate, NaCl, and a stabilizer. Source: E. coli. Species: Flavobacterium heparinum. chondroitinase (ambiguous); chondroitin sulfate lyase; chondroitin AC eliminase; chondroitinase AC; ChnAC; 9047-57-8; EC 4.2.2.5. Cat No: NATE-1738. | |
| Chymotrypsin from Human, Recombinant | Chymotrypsin is a recombinant serine endopeptidase expressed in E.coli, purified with HPLC, the gene sequence is the same as human chymotrypsin. Recombinant chymotrypsin hydrolyzes at the carboxyl side of aromatic amino acids residues: Tyr, Phe and Trp. Cleavage may also be observed, but at a lower rate, at Leu and Met. Chymotrypsin activity is optimal in pH 7.0-9.0. Applications: Hydrolysis of proteins by chymotrypsin alone or in combination with other proteases. suitable for peptide mapping, fingerprinting, and sequence analysis. Group: Enzymes. Synonyms: EC 3.4.21.1; chymotrypsins A and B; alpha-chymar ophth; avazyme; chymar; chymotest; enzeon; quimar; quimotrase; alpha-chymar; alpha-chymotrypsin A; alpha-chymotrypsin; Chymotrypsin; &alpha. Enzyme Commission Number: EC 3.4.21.1. CAS No. 9004-7-3. Purity: > 95% by HPLC. Chymotrypsin. Mole weight: 26,950 Da. Activity: >1000 unit/mg protein. Storage: Recombinant Chymotrypsin lyophilized should be stored under 2°C-8°C in sealed container. It is stable within 24 months. After dissolved, it should be stored under -20°C. Form: White lyophilized. Source: E. coli. Species: Human. EC 3.4.21.1; chymotrypsins A and B; alpha-chymar ophth; avazyme; chymar; chymotest; enzeon; quimar; quimotrase; alpha-chymar; alpha-chymotrypsin A; alpha-chymotrypsin; Chymotrypsin; α-Chymotrypsin. Cat No: NATE-1890. | |
| Collagenase (food grade) | Collagenase is an enzyme complex to hydrolyzed gelatin and collagen, mainly composed by endo-proteases, exo-protease and flavor enzymes. Group: Enzymes. Synonyms: Endo-protease; Exo-protease; flavor enzyme; Collagenase. Collagenase. Activity: >100,000 u/g. Appearance: White or yellowish, odorless, powder. Endo-protease; Exo-protease; flavor enzyme; Collagenase. Cat No: NATE-1594. | |
| Cytochalasin A | It is produced by the strain of Helminthosporium dematioideum, Coriolus vernicipes. It has many biological activities, such as inhibiting cytokinesis reversibly, inhibiting megasophil endocytosis and exocytosis. Cytochalasin A is an HIV protease inhibitor. Synonyms: NSC174119; Dehydrophomin; 5-Dehydrophomin; 5,5-Didehydrophomin; 2H-Oxacyclotetradecino(2,3-d)isoindole-2,5,18-trione, 6,7,8,9,10,12a,13,14,15,15a,16,17-dodecahydro-13-hydroxy-9,15-dimethyl-14-methylene-16-(phenylmethyl)-, (3E, 9R, 11E, 12aS, 13S, 15S, 15aS, 16S, 18aS)-; (7S,13E,16R,21E)-7-Hydroxy-16-methyl-10-phenyl-24-Oxa[14]cytochalasa-6(12),13,21-triene-1,20,23-trione; 16-Benzyl-6,7,8,9,10,12a,13,14,15,15a,16,17-dodecahydro-13-hydroxy-9,15-dimethyl-14-methylene-2H-Oxacyclotetradecino[2,3-d]isoindole-2,5,18-trione. Grades: >98% by HPLC. CAS No. 14110-64-6. Molecular formula: C29H35NO5. Mole weight: 477.59. | |
| 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. | |
| endopeptidase Clp | An enzyme from bacteria that contains subunits of two types, ClpP, with peptidase activity, and ClpA, with ATPase activity. The ClpAP complex, which displays ATP-dependent endopeptidase activity, has the composition (ClpP14ClpA6)2. ClpP is the type example of peptidase family S14. Group: Enzymes. Synonyms: endopeptidase Ti; caseinolytic protease; protease Ti; ATP-dependent Clp protease; endopeptidase Ti; caseinolytic protease; ClpP; Clp protease. Enzyme Commission Number: EC 3.4.21.92. CAS No. 110910-59-3. 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-4184; endopeptidase Clp; EC 3.4.21.92; 110910-59-3; endopeptidase Ti; caseinolytic protease; protease Ti; ATP-dependent Clp protease; endopeptidase Ti; caseinolytic protease; ClpP; Clp protease. Cat No: EXWM-4184. | |
| endopeptidase La | Product of the lon gene in Escherichia coli. ATP hydrolysis is linked with peptide bond hydrolysis; vanadate inhibits both reactions. Type example of peptidase family S16. A similar enzyme occurs in animal mitochondria. Group: Enzymes. Synonyms: ATP-dependent serine proteinase; lon proteinase; protease La; proteinase La; ATP-dependent lon proteinase; ATP-dependent protease La; Escherichia coli proteinase La; Escherichia coli serine proteinase La; gene lon protease; gene lon proteins; PIM1 protease; PIM1 proteinase; serine protease La. Enzyme Commission Number: EC 3.4.21.53. CAS No. 79818-35-2. 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-4145; endopeptidase La; EC 3.4.21.53; 79818-35-2; ATP-dependent serine proteinase; lon proteinase; protease La; proteinase La; ATP-dependent lon proteinase; ATP-dependent protease La; Escherichia coli proteinase La; Escherichia coli serine proteinase La; gene lon protease; gene lon proteins; PIM1 protease; PIM1 proteinase; serine protease La. Cat No: EXWM-4145. | |
| Endoproteinase Glu-C | Endoproteinase GluC (V8 protease) is a serine proteinase. Endoproteinase GluC is able to hydrolyze some serpins and all classes of mammalian immunoglobulins [1]. Uses: Scientific research. Group: Signaling pathways. Alternative Names: V8 protease; Glu-C. CAS No. 137010-42-5. Pack Sizes: 100 μg. Product ID: HY-E70194. | |
| Endoproteinase GluC from Staphylococcus aureus, Recombinant | Protease S. aureus V8 (Endoproteinase-Glu-C) specifically cleaves peptide bonds on the COOH-terminal side of either aspartic or glutamic acids. In the presence of ammonium, the enzyme specificity is limited to glutamic sites. It has a molecular weight of 27 kDa daltons and optimum pH's of 4.0 and 7.8 with hemoglobin as the substrate. Protease S. aureus V8 is inhibited by diisopropylfluorophosphate and monovalent anions such as F-, Cl-, CH3COO-and NO3. Enzyme activity is determined by the casein digestion assay described by Drapeau. Endoproteinase gluc (staphylococcus aureus protease v8) is a serine proteinase which selectively cleaves peptide bonds c-terminal to...tide identification. Group: Enzymes. Synonyms: EC 3.4.21.19; Staph aureus V8 Protease; Protease, Staph aureus (Endoproteinase Glu-C); Glutamyl endopeptidase; V8 proteinase, endoproteinase Glu-C; staphylococcal serine proteinase. CAS No. 66676-43-5. V8 Protease. Mole weight: 29849 daltons. Activity: 38.3 μmol/min/mg. Storage: at -20°C. Form: Supplied freeze-dried from a Tris-HCl and sodium chloride buffer. Source: Bacillus subtilis. Species: Staphylococcus aureus. EC 3.4.21.19; Staph aureus V8 Protease; Protease, Staph aureus (Endoproteinase Glu-C); Glutamyl endopeptidase; V8 proteinase, endoproteinase Glu-C; staphylococcal serine proteinase. Cat No: NATE-1270. | |
| Endoproteinase Lys-C | Endoproteinase Lys-C is a protease that cleaves proteins on the C-terminal side of lysine residues and is commonly used for protein sequencing [1]. Uses: Scientific research. Group: Signaling pathways. CAS No. 72561-05-8. Pack Sizes: 50 mg; 100 mg; 250 mg; 1 mg; 5 mg; 10 mg. Product ID: HY-P3208. | |
| Enzyme blend for cattle and sheep | Complex enzyme for cattle and sheep is one of complex enzyme, which is designed according to Fattening cattle and sheep physiological characteristics and feed raw materials. This Complex enzyme is mainly the amylase, celluse, BETA-dextranase, Xylanase, protease with other endogenous enzymes which can well suit for character of the poultry digestive tract. The product through many optimization experiment, which can well digest non-starch polysaccharide, improve the use rate of feed. Applications: 1. this complex enzyme can digest starch polysaccharide, and effectively digest the cellulase, xylanase, beta-dextranase and so on in the feed, which can reduce the viscosity of chym...ality of milk. 3.restrain intestinal harmful organisms to grow, increase the quantity of beneficial microorganisms, maintain the dynamic balance of animal gut microbes, reduce diarrhea, and enhance immunity and disease resistance of animal. Group: Enzymes. Synonyms: for cattle; sheep; Fattening cattle; Fattening sheep; make full use of grains mixed meal; feed enzyme; Enzyme blend for cattle and sheep; FEED-2325. Enzyme for cattle and sheep. Appearance: powder. for cattle; sheep; Fattening cattle; Fattening sheep; make full use of grains mixed meal; feed enzyme; Enzyme blend for cattle and sheep; FEED-2325. Pack: 25kg/barrel or subject to client requirement. Cat No: FEED-2325. | |
| Enzyme blend for egg birds | Complex enzyme for egg birds is one of complex enzyme, which is designed according to poultry physiological characteristics and feed raw materials. This Complex enzyme is mainly the non-starch polysaccharide enzymes, with other enzymes including the protease and amylase, which can well suit for character of the poultry digestive tract. The products through much optimization experiment, which can well digest non-starch polysaccharide, improve the use rate of feed. Applications: 1.this complex enzyme can digest starch polysaccharide, and effectively digest the cellulase, xylanase, beta-dextranase and so on in the feed,which can reduce the viscosity of chymus, mach with the endogen...in intestinal harmful organisms to grow efficient, increase the quantity of beneficial microorganisms, maintain the dynamic balance of animal gut microbes, reduce diarrhea, and enhance immunity and disease resistance of animal, increase the cycle of the laying. egg. Group: Enzymes. Synonyms: egg birds; digest non-starch polysaccharide; improve the use rate of feed; feed enzyme; rate of feed; Enzyme blend for egg birds; FEED-2326. Enzyme for egg birds. Appearance: powder. egg birds; digest non-starch polysaccharide; improve the use rate of feed; feed enzyme; rate of feed; Enzyme blend for egg birds; FEED-2326. Pack: 25kg/barrel or subject to client requirement. Cat No: FEED-2326. | |
| Enzyme blend for milk cows | Complex enzyme for milk cows is one of complex enzyme, which is designed according to milk cows physiological characteristics and feed raw materials. This Complex enzyme is mainly the amylase, celluse, BETA-dextranase, Xylanase, protease with other endogenous enzymes which can well suit for character of the poultry digestive tract. The product through many optimization experiment, which can well digest non-starch polysaccharide, improve the use rate of feed. Applications: 1.this complex enzyme can digest starch polysaccharide, and effectively digest the cellulase, xylanase, beta-dextranase and so on in the feed, which can reduce the viscosity of chymus, this complex enzyme can w...grow, increase the quantity of beneficial microorganisms, maintain the dynamic balance of animal gut microbes, reduce diarrhea, and enhance immunity and disease resistance of animal. Group: Enzymes. Synonyms: milk cows; feed enzyme; milk cows; digest non-starch polysaccharide; improve the use rate of feed; use rate of feed; non-starch polysaccharide; Enzyme blend for milk cows; FEED-2327. Enzyme for milk cows. Appearance: powder. milk cows; feed enzyme; milk cows; digest non-starch polysaccharide; improve the use rate of feed; use rate of feed; non-starch polysaccharide; Enzyme blend for milk cows; FEED-2327. Pack: 25kg/barrel or subject to client requirement. Cat No: FEED-2327. | |
| Feed enzyme complex for aquaculture | This complex is made in the way of Solid State Fermentation (SSF), not like pure enzymes which are made in the way of Liquid State Fermentation (LSF). Feed enzyme complex for livestock is designed according to fattening livestock's physiological characteristics and feed raw materials. Feed enzyme complex includes mainly the celluse (endocellulase, exocellulase, glucosidase), Xylanase (endoxylanase, exoxylanase,xylosidase),β-glucanase , mannose, acid protease, amylase, glucoamylase, pectinase with other endogenous enzymes which can well suit for character of the poultry digestive tract. The product through many optimization experiment, which can well digest non-starch polysaccharide, improve the use rate of feed. Applications: Feed enzyme complex for aquaculture. Group: Enzymes. Enzyme blend for aquaculture. Feed enzyme complex for aquaculture. Pack: 25 kgs/barrel or at customer's request. Cat No: Feed-2112. | |
| Feed enzyme complex for conventional diet | This complex is made in the way of Solid State Fermentation (SSF), not like pure enzymes which are made in the way of Liquid State Fermentation (LSF). Feed enzyme complex for livestock is designed according to fattening livestock's physiological characteristics and feed raw materials. Feed enzyme complex includes mainly the celluse (endocellulase, exocellulase, glucosidase), Xylanase (endoxylanase, exoxylanase,xylosidase),β-glucanase , mannose, acid protease, amylase, glucoamylase, pectinase with other endogenous enzymes which can well suit for character of the poultry digestive tract. The product through many optimization experiment, which can well digest non-starch polysaccharide, improve the use rate of feed. Applications: Feed enzyme complex for conventional diet. Group: Enzymes. Enzyme blend for conventional diet. Feed enzyme complex for conventional diet. Pack: 25 kgs/barrel or at customer's request. Cat No: Feed-2114. | |
| Feed enzyme complex for miscellaneous meals | This complex is made in the way of Solid State Fermentation (SSF), not like pure enzymes which are made in the way of Liquid State Fermentation (LSF). Feed enzyme complex for livestock is designed according to fattening livestock's physiological characteristics and feed raw materials. Feed enzyme complex includes mainly the celluse (endocellulase, exocellulase, glucosidase), Xylanase (endoxylanase, exoxylanase,xylosidase),β-glucanase , mannose, acid protease, amylase, glucoamylase, pectinase with other endogenous enzymes which can well suit for character of the poultry digestive tract. The product through many optimization experiment, which can well digest non-starch polysaccharide, improve the use rate of feed. Applications: Feed enzyme complex for miscellaneous meals. Group: Enzymes. Enzyme blend for miscellaneous meals. Feed enzyme complex for miscellaneous meals. Pack: 25 kgs/barrel or at customer's request. Cat No: Feed-2116. | |
| Feed enzyme complex for piglets & hogs | This complex is made in the way of Solid State Fermentation (SSF), not like pure enzymes which are made in the way of Liquid State Fermentation (LSF). Feed enzyme complex for livestock is designed according to fattening livestock's physiological characteristics and feed raw materials. Feed enzyme complex includes mainly the celluse (endocellulase, exocellulase, glucosidase), Xylanase (endoxylanase, exoxylanase,xylosidase),β-glucanase , mannose, acid protease, amylase, glucoamylase, pectinase with other endogenous enzymes which can well suit for character of the poultry digestive tract. The product through many optimization experiment, which can well digest non-starch polysaccharide, improve the use rate of feed. Applications: Feed enzyme complex for piglets & hogs. Group: Enzymes. Enzyme blend for piglets & hogs. Feed enzyme complex for piglets & hogs. Pack: 25 kgs/barrel or at customer's request. Cat No: Feed-2110. | |
| Feed enzyme complex for poultry | This complex is made in the way of Solid State Fermentation (SSF), not like pure enzymes which are made in the way of Liquid State Fermentation (LSF). Feed enzyme complex for livestock is designed according to fattening livestock's physiological characteristics and feed raw materials. Feed enzyme complex includes mainly the celluse (endocellulase, exocellulase, glucosidase), Xylanase (endoxylanase, exoxylanase,xylosidase),β-glucanase , mannose, acid protease, amylase, glucoamylase, pectinase with other endogenous enzymes which can well suit for character of the poultry digestive tract. The product through many optimization experiment, which can well digest non-starch polysaccharide, improve the use rate of feed. Applications: Feed enzyme complex for poultry. Group: Enzymes. Enzyme blend for poultry. Feed enzyme complex for poultry. Pack: 25 kgs/barrel or at customer's request. Cat No: Feed-2111. | |
| Feed enzyme complex for ruminants | This complex is made in the way of Solid State Fermentation (SSF), not like pure enzymes which are made in the way of Liquid State Fermentation (LSF). Feed enzyme complex for livestock is designed according to fattening livestock's physiological characteristics and feed raw materials. Feed enzyme complex includes mainly the celluse (endocellulase, exocellulase, glucosidase), Xylanase (endoxylanase, exoxylanase,xylosidase),β-glucanase , mannose, acid protease, amylase, glucoamylase, pectinase with other endogenous enzymes which can well suit for character of the poultry digestive tract. The product through many optimization experiment, which can well digest non-starch polysaccharide, improve the use rate of feed. Applications: Feed enzyme complex for ruminants. Group: Enzymes. Enzyme blend for ruminants. Feed enzyme complex for ruminants. Pack: 25 kgs/barrel or at customer's request. Cat No: Feed-2113. | |
| Feed enzyme complex for wheat-based diet | This complex is made in the way of Solid State Fermentation (SSF), not like pure enzymes which are made in the way of Liquid State Fermentation (LSF). Feed enzyme complex for livestock is designed according to fattening livestock's physiological characteristics and feed raw materials. Feed enzyme complex includes mainly the celluse (endocellulase, exocellulase, glucosidase), Xylanase (endoxylanase, exoxylanase,xylosidase),β-glucanase , mannose, acid protease, amylase, glucoamylase, pectinase with other endogenous enzymes which can well suit for character of the poultry digestive tract. The product through many optimization experiment, which can well digest non-starch polysaccharide, improve the use rate of feed. Applications: Feed enzyme complex for wheat-based diet. Group: Enzymes. Enzyme blend for wheat-based diet. Feed enzyme complex for wheat-based diet. Pack: 25 kgs/barrel or at customer's request. Cat No: Feed-2115. | |
| Fmoc-ACA-OH | Fmoc-ACA-OH is a useful tool for the SPPS of AMC fluorogenic protease substrates by Fmoc SPPS. Fmoc-ACA-OH must be first loaded onto a Wang-type resin. Any unreacted linker hydroxyls must be capped using acetic anhydride. Following Fmoc removal, the first amino acid should be coupled with HATU/collidine. Insertion of ACA into the middle of a peptide provides fluorogenic substrates for endopeptidases. Treatment of the ACC peptide obtained after TFA cleavage with an aqueous base causes facile decarboxylation and formation of the AMC peptide. Uses: Peptide synthesis. Group: Amino acids. Alternative Names: Fmoc-ACA-OH, 7-N-Fmoc-aminocoumarin-4-acetic acid. CAS No. 378247-75-7. Mole weight: 441.43. Catalog: ACM378247757. |  |
| 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 endopeptidase | From Staphylococcus aureus strain V8. In appropriate buffer the specificity is restricted to Glu?. In peptidase family S1 (trypsin family). Group: Enzymes. Synonyms: V8 proteinase; endoproteinase Glu-C; staphylococcal serine proteinase. Enzyme Commission Number: EC 3.4.21.19. CAS No. 137010-42-5. V8 Protease. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4118; glutamyl endopeptidase; EC 3.4.21.19; 137010-42-5; V8 proteinase; endoproteinase Glu-C; staphylococcal serine proteinase. Cat No: EXWM-4118. | |
| HtrA2 peptidase | This enzyme is upregulated in mammalian cells in response to stress induced by both heat shock and tunicamycin treatment. It can induce apoptosis in a caspase-independent manner through its peptidase activity and in a caspase-dependent manner by disrupting the interaction between caspase and the inhibitor of apoptosis (IAP). Belongs in peptidase family S1C. Group: Enzymes. Synonyms: high temperature requirement protein A2; HtrA2; Omi stress-regulated endoprotease; serine proteinase OMI; HtrA2 protease; OMI/HtrA2 protease; HtrA2/Omi; Omi/HtrA2. Enzyme Commission Number: EC 3.4.21.108. 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-4103; HtrA2 peptidase; EC 3.4.21.108; high temperature requirement protein A2; HtrA2; Omi stress-regulated endoprotease; serine proteinase OMI; HtrA2 protease; OMI/HtrA2 protease; HtrA2/Omi; Omi/HtrA2. Cat No: EXWM-4103. | |
| human endogenous retrovirus K endopeptidase | In peptidase family A2. Group: Enzymes. Synonyms: human endogenous retrovirus K10 endopeptidase; endogenous retrovirus HERV-K10 putative protease; human endogenous retrovirus K retropepsin; HERV K10 endopeptidase; HERV K10 retropepsin; HERV-K PR; HERV-K protease; HERV-K113 protease; human endogenous retrovirus K113 protease; human retrovirus K10 retropepsin. Enzyme Commission Number: EC 3.4.23.50. 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-4288; human endogenous retrovirus K endopeptidase; EC 3.4.23.50; human endogenous retrovirus K10 endopeptidase; endogenous retrovirus HERV-K10 putative protease; human endogenous retrovirus K retropepsin; HERV K10 endopeptidase; HERV K10 retropepsin; HERV-K PR; HERV-K protease; HERV-K113 protease; human endogenous retrovirus K113 protease; human retrovirus K10 retropepsin. Cat No: EXWM-4288. | |
| IgA-specific metalloendopeptidase | A 190 kDa enzyme found in several pathogenic species of Streptococcus such as sanguis and pneumoniae. Type example of peptidase family M26. There is also an IgA-specific prolyl endopeptidase of the serine-type (see EC 3.4.21.72, IgA-specific serine endopeptidase). Group: Enzymes. Synonyms: immunoglobulin A1 proteinase; IgA protease; IgA1-specific proteinase; IgA1 protease; IgA1 proteinase. Enzyme Commission Number: EC 3.4.24.13. CAS No. 72231-73-3. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4294; IgA-specific metalloendopeptidase; EC 3.4.24.13; 72231-73-3; immunoglobulin A1 proteinase; IgA protease; IgA1-specific proteinase; IgA1 protease; IgA1 proteinase. Cat No: EXWM-4294. | |
| IgA-specific serine endopeptidase | Species variants differing slightly in specificity are secreted by Gram-negative bacteria Neisseria gonorrhoeae and Haemophilus influenzae. Type example of peptidase family S6. Some other bacterial endopeptidases with similar specificity are of metallo- type (see EC 3.4.24.13, IgA-specific metalloendopeptidase). Group: Enzymes. Synonyms: IgA protease; IgA proteinase; IgA-specific proteinase; immunoglobulin A protease; immunoglobulin A proteinase. Enzyme Commission Number: EC 3.4.21.72. CAS No. 55127-02-1. 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-4164; IgA-specific serine endopeptidase; EC 3.4.21.72; 55127-02-1; IgA protease; IgA proteinase; IgA-specific proteinase; immunoglobulin A protease; immunoglobulin A proteinase. Cat No: EXWM-4164. | |
| Immobilized Endoproteinase Glu-C on F7m | Endoproteinase Glu-C hydrolyzes peptide and ester linkages specifically at the carboxyl end of glutamic acid (-Glu/-X; in ammonium carbonate pH 7. 8, or ammonium acetate pH 4. 0, buffer A) or of glutamic and aspartic acid (-Glu/-X and -Asp/-X; in phosphate buffer pH 7. 8, buffer B). F7m: 1. 0 mg endoproteinase Glu-C immobilized on matrix F7m per CR-column. 900 units immobilized per CR-column. Nr. 7 Storage buffer: 50 mM Tris/HCl at pH 7. 5, 5 mM EDTA. Nr. 31 Reaction buffer A: 25 mM ammonium acetate, pH 4. 0 (see above)Nr. 32 Washing buffer A: 25 mM ammonium acetate, pH 4. 0, 1 M NaClNr. 62 Reaction buffer B: 50 mM phosphate buffer, pH 7. 8 (see above)Nr. 63 Washing buffer B: 50 mM phosphate buffer, pH 7. 8, 1 M NaCl. Group: Enzymes. Synonyms: EC 3. 4. 21. 19; Staph aureus V8 Protease; Protease, Staph aureus (Endoproteinase Glu-C); Glutamyl endopeptidase; V8 proteinase, endoproteinase Glu-C; staphylococcal serine proteinase. Enzyme Commission Number: EC 3. 4. 21. 19. Storage: 4 °C. Source: Staphylococcus aureus. EC 3. 4. 21. 19; Staph aureus V8 Protease; Protease, Staph aureus (Endoproteinase Glu-C); Glutamyl endopeptidase; V8 proteinase, endoproteinase Glu-C; staphylococcal serine proteinase; Immobilized Endoproteinase Glu-C. Cat No: NATE-1763. | |
| Immobilized Endoproteinase Glu-C on G3m | Endoproteinase Glu-C hydrolyzes peptide and ester linkages specifically at the carboxyl end of glutamic acid (-Glu/-X; in ammonium carbonate pH 7. 8, or ammonium acetate pH 4. 0, buffer A) or of glutamic and aspartic acid (-Glu/-X and -Asp/-X; in phosphate buffer pH 7. 8, buffer B). G3m: 25 ug (22 units) endoproteinase Glu-C per CR-column immobilized on dextran. This CR-column cuts at least 12 ug tubulin or 5 ug BSA per application in phosphate buffer. Nr. 7 Storage buffer: 50 mM Tris/HCl at pH 7. 5, 5 mM EDTA. Nr. 31 Reaction buffer: 25 mM NH4-acetate, pH 4. 0 (see above)Nr. 32 Washing buffer: 25 mM NH4-acetate, pH 4. 0, 1 M NaClNr. 62 Reaction buffer: 50 mM phosphate buffer, pH 7. 8 (see above)Nr. 63 Washing buffer: 50 mM phosphate buffer, pH 7. 8, 1 M NaCl. Group: Enzymes. Synonyms: EC 3. 4. 21. 19; Staph aureus V8 Protease; Protease, Staph aureus (Endoproteinase Glu-C); Glutamyl endopeptidase; V8 proteinase, endoproteinase Glu-C; staphylococcal serine proteinase. Enzyme Commission Number: EC 3. 4. 21. 19. Storage: 4 °C. Source: Staphylococcus aureus. EC 3. 4. 21. 19; Staph aureus V8 Protease; Protease, Staph aureus (Endoproteinase Glu-C); Glutamyl endopeptidase; V8 proteinase, endoproteinase Glu-C; staphylococcal serine proteinase; Immobilized Endoproteinase Glu-C. Cat No: NATE-1764. | |
| 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. | |
| 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. | |
| leishmanolysin | A membrane-bound glycoprotein found on the promastigote of various species of Leishmania protozoans. Contains consensus sequence for a zinc-binding site; Z-Tyr-Leu-NHOH is a strong inhibitor. The enzyme can activate its proenzyme by cleavage of the Val100?Val bond. An acid pH optimum is found with certain protein substrates. Type example of peptidase family M8. Group: Enzymes. Synonyms: promastigote surface endopeptidase; glycoprotein gp63; Leishmania metalloproteinase; surface acid proteinase; promastigote surface protease. Enzyme Commission Number: EC 3.4.24.36. CAS No. 161052-06-8. 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-4318; leishmanolysin; EC 3.4.24.36; 161052-06-8; promastigote surface endopeptidase; glycoprotein gp63; Leishmania metalloproteinase; surface acid proteinase; promastigote surface protease. Cat No: EXWM-4318. | |
| Lys-Lys/Arg-Xaa endopeptidase | The enzyme is a serine peptidase, which has been shown to cleave prothrombin and prekallikrein. It hydrolyses the complement component C5 releasing complement component C5a. Group: Enzymes. Synonyms: ASP (Aeromonas sobria)-type peptidase; Aeromonas extracellular serine protease. Enzyme Commission Number: EC 3.4.21.121. 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-4117; Lys-Lys/Arg-Xaa endopeptidase; EC 3.4.21.121; ASP (Aeromonas sobria)-type peptidase; Aeromonas extracellular serine protease. Cat No: EXWM-4117. | |
| lysyl endopeptidase | From Achromobacter lyticus. Enzymes with similar specificity are produced by Lysobacter enzymogenes (Endoproteinase Lys-C;) and Pseudomonas aeruginosa (Ps-1;). In peptidase family S1 (trypsin family). Group: Enzymes. Synonyms: Achromobacter proteinase I (also see Comment); Achromobacter lyticus alkaline proteinase I; protease I; achromopeptidase; lysyl bond specific proteinase. Enzyme Commission Number: EC 3.4.21.50. CAS No. 123175-82-6. Achromopeptidase. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4144; lysyl endopeptidase; EC 3.4.21.50; 123175-82-6; Achromobacter proteinase I (also see Comment); Achromobacter lyticus alkaline proteinase I; protease I; achromopeptidase; lysyl bond specific proteinase. Cat No: EXWM-4144. | |
| magnolysin | An endopeptidase of 58 kDa known from bovine pituitary neurosecretory granules and bovine and human corpus luteum. Inhibited by EDTA. Group: Enzymes. Synonyms: bovine neurosecretory granule protease cleaving pro-oxytocin/neurophysin; pro-oxytocin/neurophysin convertase; prooxyphysin proteinase; pro-oxytocin convertase. Enzyme Commission Number: EC 3.4.24.62. CAS No. 162875-09-4. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4345; magnolysin; EC 3.4.24.62; 162875-09-4; bovine neurosecretory granule protease cleaving pro-oxytocin/neurophysin; pro-oxytocin/neurophysin convertase; prooxyphysin proteinase; pro-oxytocin convertase. Cat No: EXWM-4345. | |
| matriptase | This trypsin-like integral-membrane serine peptidase has been implicated in breast cancer invasion and metastasis. The enzyme can activate hepatocyte growth factor/scattering factor (HGF/SF) by cleavage of the two-chain form at an Arg residue to give active α- and β-HGF, but It does not activate plasminogen, which shares high homology with HGF.The enzyme can also activate urokinase plasminogen activator (uPA), which initiates the matrix-degrading peptidase cascade. Belongs in peptidase family S1A. Group: Enzymes. Synonyms: serine protease 14; membrane-type serine protease 1; MT-SP1; prostamin; serine protease TADG-15; tumor-associated differentially-expressed gene 15 protein; ST14; breast cancer 80 kDa protease; epithin; serine endopeptidase SNC19. Enzyme Commission Number: EC 3.4.21.109. CAS No. 241475-96-7. 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-4104; matriptase; EC 3.4.21.109; 241475-96-7; serine protease 14; membrane-type serine protease 1; MT-SP1; prostamin; serine protease TADG-15; tumor-associated differentially-expressed gene 15 protein; ST14; breast cancer 80 kDa protease; epithin; serine endopeptidase SNC19. Cat No: EXWM-4104. | |
| Mutation Detection Kit | Mutation Detection Kit. Mutation detection kit provides a simple, reliable, and rapid method for the detection of site specific cleavage of genomic dna that is extracted from cells transfected with constructs expressing engineered nucleases such as transcription activator-like effector nucleases (talen), clustered regularly interspaced short palindromic repeats (crispr)/cas9, or zinc-finger nucleases (zfn). mutation detection kit includes high-fidelity dna polymerase for amplifying the target regions from cells, and t7 endonuclease i for recognizing and detecting the mismatches caused by gene editing tools. it provides an easy and reliable approach for estimating the efficiency of genome editing. components. high-fidelity dna polymerase. 5x pcr reaction buffer. t7 endonuclease i. 10x gencrispr t7 endonuclease i reaction buffer. control template dna. control primer mix. protease k. dntp. Group: Cloning Enzymes. Purity: 25 reactions/kit. Storage: Store at -20 ?. Source: E.coli. Pack: 10 mM Tris, 300 mM NaCl, 0.1 mM EDTA, 1 mM DTT, 50% Glycerol pH7.4, at 25°C. Cat No: CE-3508. | |
| Native Achromobacter lyticus Achromopeptidase | Lysyl endopeptidase (EC 3.4.21.50, Achromobacter proteinase I, Achromobacter lyticus alkaline proteinase I, protease I, achromopeptidase, lysyl bond specific proteinase) is an enzyme. This enzyme catalyses the following chemical reaction:Preferential cleavage:Lys-, including-Lys-Pro-. This enzyme is isolated from Achromobacter lyticus. Group: Enzymes. Synonyms: Achromobacter proteinase I; Achromobacter lyticus alkaline proteinase I; protease I; achromopeptidase; lysyl bond specific proteinase; EC 3.4.21.50; 123175-82-6; Lysyl endopeptidase. Enzyme Commission Number: EC 3.4.21.50. CAS No. 123175-82-6. Achromopeptidase. Storage: -20°C. Form: lyophilized powder, Protein ~5 % by biuret, 300-600 units/mg solid. Source: Achromobacter lyticus. Achromobacter proteinase I; Achromobacter lyticus alkaline proteinase I; protease I; achromopeptidase; lysyl bond specific proteinase; EC 3.4.21.50; 123175-82-6; Lysyl endopeptidase. Cat No: NATE-0021. | |
| Native Aspergillus aculeatus Pectinase | Pectinase is an active pectolytic enzyme preparation that is produced by a selected strain of Aspergillus aculeatus. It contains mainly pectintranseliminase, polygalacturonase and pectinesterase, along with small amounts of hemicellulases and cellulases. Pectinase hydrolyzes pectin, which is a component of the cell wall. They may attack methyl-esterified pectin or de-esterified pectin. Fungal protease/peptidase complex produced by submerged fermentation of a selected strain of aspergillus oryzae and contains both endoprotease and exopeptidase activities. Applications: Pectinase from aspergillus aculeatus is used in plant protoplast preparation to digest cell wall prior to organelle isolation. it has been used to conduct partial saccharification of sugars. pectinases are used to study their role in the invasion of plant tissues using phytopathogens, as well as various food processing and plant biotechnology applications. the enzyme from creative enzymes has been used to determine the content of quercetin produced and also to evaluate its rutinase activity. Group: Enzymes. Synonyms: Pectinase. CAS No. 9032-75-1. Pectinase. Activity: > 500 U/g. Form: aqueous solution. Source: Aspergillus aculeatus. Pectinase. Cat No: NATE-0534. | |
| Native Aspergillus oryzae Protease | Protease catabolizes proteins by hydrolysis of peptide bonds. Protease, from Aspergillus oryzae, contains both endoprotease and exopeptidase activities. Fungal protease/peptidase complex produced by submerged fermentation of a selected strain of aspergillus oryzae and contains both endoprotease and exopeptidase activities. Applications: Protease is an enzyme used to break down proteins by hydrolyzing peptide bonds. protease is used to degrade proteins, to study protease inhibitors and to study thermal inactivation kinetics. protease is used in nucleic acid isolation procedures in incubations. this product is a fungal protease/peptidase complex produced by submerged fermentation of a selected strain of aspergillus oryzae. it has been injected into flies with a nanoject apparatus for infection and survival experiments. the enzyme from creative enzymes has been used in the semi-purification of mouse colorectal mucins during protein digestion. Group: Enzymes. Synonyms: Protease; Flavourzyme. CAS No. 9001-92-7. Protease. Source: Aspergillus oryzae. Protease; Flavourzyme. Cat No: NATE-0631. | |
| Native Bacillus licheniformis Alkaline Protease | Proteinase catabolizes proteins by hydrolysis of peptide bonds. Proteases are inactivated by serine active-site inhibitors, such as phenylmethylsulfonyl fluoride (PMSF) and diisopropylfluorophosphate. Subtilisin a is a member of the serine s8 endoproteinase family. it has broad specificity with a preference for a large uncharged residue in the p1 position. it hydrolyzes native and denatured proteins, and is active under alkaline conditions. Applications: The enzyme has been used to optimize release of all mitochondrial populations from homogenized ventricular tissue of rat heart.1 it has also been used in the pre-hybridisation treatment of formalin fixed, paraffin wax...ex); MCP; proteasome; large multicatalytic protease; multicatalytic proteinase; proteasome organelle; alkaline protease; 26S protease; triCorn proteinase; triCorn protease; EC 3.4.25.1. Enzyme Commission Number: EC 3.4.25.1. CAS No. 140879-24-9. Alkaline Protease. Mole weight: 27 Kda. Activity: 7.0-14.0 units/mg. Form: lyophilized powder. Source: Bacillus licheniformis. ingensin; macropain; multicatalytic endopeptidase complex; prosome; multicatalytic proteinase (complex); MCP; proteasome; large multicatalytic protease; multicatalytic proteinase; proteasome organelle; alkaline protease; 26S protease; triCorn proteinase; triCorn protease; EC 3.4.25.1. Cat No: NATE-0444. | |
| Native Bacillus licheniformis Protease | Protease catabolizes proteins by hydrolysis of peptide bonds. Proteases are inactivated by serine active-site inhibitors, such as phenylmethylsulfonyl fluoride (PMSF) and diisopropylfluorophosphate. Protease is a serine endoproteinase with a broad specificity towards native and denatured proteins, and is active under alkaline conditions. It is active in some organic solvents such as dry octane. The enzyme is found to be stable at ph 8-10, retaining activity of up to 90% for 24 hours. it shows maximum activity at temperatures between 55-60°c. Applications: The product has been used with other enzymes for in situ proteolysis to produce crystals suitable for structure determi...f bacillus licheniformis. it is a serine endoproteinase with a broad specificity towards native and denatured proteins, and is active under alkaline conditions. Group: Enzymes. Synonyms: Protease; 9014-01-1; Subtilisin A; EC 3.4.21.62; Alcalase. Enzyme Commission Number: EC 3.4.21.62. CAS No. 9001-92-7. Protease. Mole weight: Subtilisin is a non-glycosylated single polypeptide chain without disulfide bonds and has a molecular weight of 27 KDa. Activity: Type VIII, 7-15 units/mg solid; Type I, > 2.4 U/g. Form: Type VIII, lyophilized powder; Type I, aqueous solution. Source: Bacillus licheniformis. Protease; 9014-01-1; Subtilisin A; EC 3.4.21.62; Alcalase. Cat No: NATE-0633. | |
| Native Bacteria Achromopeptidase | Lysyl endopeptidase (EC 3.4.21.50, Achromobacter proteinase I, Achromobacter lyticus alkaline proteinase I, protease I, achromopeptidase, lysyl bond specific proteinase) is an enzyme. This enzyme catalyses the following chemical reaction:Preferential cleavage:Lys-, including-Lys-Pro-. This enzyme is isolated from Achromobacter lyticus. Hemolysins are lipids and proteins that cause lysis of red blood cells by destroying their cell membrane. although the lytic activity of some microbe-derived hemolysins on red blood cells may be of great importance for nutrient acquisition, many hemolysins produced by pathogens do not cause significant destruction of red blood cells during infe...and the effect of ciprofloxacin on biofilm formation. Group: Enzymes. Synonyms: Achromobacter proteinase I; Achromobacter lyticus alkaline proteinase I; protease I; achromopeptidase; lysyl bond specific proteinase; EC 3.4.21.50; 123175-82-6; Lysyl endopeptidase. Enzyme Commission Number: EC 3.4.21.50. CAS No. 123175-82-6. Achromopeptidase. Mole weight: ~27 kDa. Activity: > 1,000 units/mg solid; > 20,000 units/mg solid. Storage: 2-8°C. Form: lyophilized powder. Source: Bacteria. Achromobacter proteinase I; Achromobacter lyticus alkaline proteinase I; protease I; achromopeptidase; lysyl bond specific proteinase; EC 3.4.21.50; 123175-82-6; Lysyl endopeptidase. Cat No: NATE-0022. | |
| Native Bovine Cathepsin D | Cathepsin D is an endosomal-lysosomal aspartic protease implicated in breast cancer metastasis and Alzheimers disease. Lysosomal release of cathepsin D has been found to precede cytochrome c release and loss of membrane potential in apoptotic Human foreskin fibroblasts. Cathepsin D levels in PC12 cells increase 12 to 24 hours after apoptosis is induced. Group: Enzymes. Synonyms: CTSD; cathepsin D; 9025-26-7; EC 3.4.23.5; CLN10; CPSD; HEL-S-130P. Enzyme Commission Number: EC 3.4.23.5. CAS No. 9025-26-7. CTSD. Mole weight: 45 kDa. Activity: > 2.0 units/mg protein. Form: Lyophilized powder containing Citrate buffer salts. Source: Bovine spleen. Species: Bovine. CTSD; cathepsin D; 9025-26-7; EC 3.4.23.5; CLN10; CPSD; HEL-S-130P. Cat No: NATE-0171. | |
| Native Flavobacterium meningosepticum PNGase F | In enzymology, a peptide-N4-(N-acetyl-beta-glucosaminyl) asparagine amidase (EC 3.5.1.52) is an enzyme that catalyzes a chemical reaction that cleaves a N4-(acetyl-beta-D-glucosaminyl)asparagine residue in which the glucosamine residue may be further glycosylated, to yield a (substituted) N-acetyl-beta-D-glucosaminylamine and a peptide containing an aspartate residue. This enzyme belongs to the family of hydrolases, specifically those acting on carbon-nitrogen bonds other than peptide bonds in linear amides. Pngase f is purified from flavobacterium meningosepticum (3) and it is free of proteases and endo f activities. the following reagents are supplied with this produ...osaminyl)asparagine amidase; EC 3.5.1.52; PNGase F; 83534-39-8. Enzyme Commission Number: EC 3.5.1.52. CAS No. 83534-39-8. PNGase F. Mole weight: 36 kDa. Activity: 500,000 units/ml. Stability: Storage Conditions: 20 mM Tris-HCl, 50 mM NaCl, 5 mM Na2EDTA, 50% Glycerol, pH 7.5 25°C Heat Inactivation: 75°C for 10 min. Storage: Store at -20°C. Source: Flavobacterium meningosepticum. glycopeptide N-glycosidase; glycopeptidase; N-oligosaccharide glycopeptidase; N-glycanase; glycopeptidase; Jack-bean glycopeptidase; PNGase A; PNGase F; glycopeptide N-glycosidase; peptide-N4-(N-acetyl-β-glucosaminyl)asparagine amidase; EC 3.5.1.52; PNGase F; 83534-39-8. Cat No: NATE-0603. | |
| Native Human Cathepsin D | Cathepsin D is an endosomal-lysosomal aspartic protease implicated in breast cancer metastasis and Alzheimers disease. Lysosomal release of cathepsin D has been found to precede cytochrome c release and loss of membrane potential in apoptotic human foreskin fibroblasts. Cathepsin D levels in PC12 cells increase 12 to 24 hours after apoptosis is induced. Group: Enzymes. Synonyms: CTSD; cathepsin D; CLN10; CPSD; HEL-S-130P; EC 3.4.23.5; 9025-26-7. Enzyme Commission Number: EC 3.4.23.5. CAS No. 9025-26-7. CTSD. Activity: > 250 units/mg protein (E1%/280). Storage: -20°C. Form: lyophilized powder. Source: Human liver. Species: Human. CTSD; cathepsin D; CLN10; CPSD; HEL-S-130P; EC 3.4.23.5; 9025-26-7. Cat No: NATE-0172. | |
| Native Human Elastase | Neutrophil elastase is a serine proteinase in the same family as chymotrypsin and has broad substrate specificity. Secreted by neutrophils and macrophages during inflammation, it destroys bacteria and host tissue. It also localizes to Neutrophil extracellular traps (NETs), via its high affinity for DNA, an unusual property for serine proteases. Leuk ocyte elastase is a 29 kda serine endoprotease of the proteinase s1 family. it exists as a single 238 amino acid-peptide chain with four disulfide bonds. it contains two or thee n-linked glycans of variable composition which account for its three major isoforms. Applications: Elastase from creative enzymes has been used to digest fibro...mal models. Group: Enzymes. Synonyms: ELANE; elastase; EC 3.4.21.37; leukocyte elastase; ELA2; elastase 2; neutrophil elaszym; serine elastase; lysosomal elastase; neutrophil elastase; polymorphonuclear leukocyte elastase; elaszym; granulocyte elastase. Enzyme Commission Number: EC 3.4.21.37. CAS No. 9004-6-2. ELA2. Mole weight: 29 kDa. Activity: > 50 units/mg protein (Bradford). Storage: -20°C. Form: Lyophilized from 0.05 M sodium acetate (pH 5.5) and 0.6 M NaCl. Source: Human leuk ocytes. Species: Human. ELANE; elastase; EC 3.4.21.37; leukocyte elastase; ELA2; elastase 2; neutrophil elaszym; serine elastase; lysosomal elastase; neutrophil elastase; polymorphonuclear leukocyte ela | |
| Native Human Protein C | Protein C is a plasma, vitamin κ-dependent zymogen of a serine protease that can inhibit blood coagulation by inhibiting thrombin formation, selectively inactivating Factors Va and VIIIa. The Protein C anticoagulant pathway is triggered when thrombin binds to the endothelial cell proteoglycan, thrombomodulin. This complex, which cannot clot blood, is a potent activator of the protein C zymogen. Activation involves the release of a dodecapeptide from the N-terminal domain of the heavy chain. The activated Protein C (APC) then binds to protein S on cell surfaces and inactivates the coagulation factors Va and VIIIa by proteolysis. APC has also been shown to bind to receptors on the endothelium of large blood vessels. Group: Enzymes. Synonyms: PROC; protein C; blood-coagulation factor XIVa; activated blood coagulation factor XIV; activated protein C; autoprothr. Enzyme Commission Number: EC 3.4.21.69. CAS No. 42617-41-4. Purity: > 90% (SDS-PAGE). Protein C. Mole weight: heavy chain mol wt 41 kDa; light chain mol wt 21 kDa. Storage: -20°C. Form: Lyophilized powder from 20 mM Tris-HCl, pH 7.4, containing 0.1 M NaCl. Source: Human plasma. Species: Human. PROC; protein C; blood-coagulation factor XIVa; activated blood coagulation factor XIV; activated protein C; autoprothrombin II-A; protein Ca; APC; GSAPC; 42617-41-4; EC 3.4.21.69; PROC1. Cat No: NATE-0626. | |
| Native Lysobacter enzymogenes Endoproteinase Lys-C | Endoproteinase Lys-C inactivates the enzyme inositol monophosphatase by cleaving it at a single site directly after Lys 36. Endoproteinase lys-c is an enzyme that preferentially cleaves at the carboxyl side of lysine residues. Applications: Endoproteinase lys-c from lysobacter enzymogenes is useful in the determination of primary structures of proteins. it has been used in a study to investigate the evidence for trisulfide bonds in a recombinant variant of a human igg2 mon oclonal antibody. endoproteinase lys-c has been used for the digestion mon oclonal antibodies for disulfide bond assignment. Group: Enzymes. Synonyms: EC 3.4.21.50; chromobacter proteinase I; Achromobacter lyticus alkaline proteinase I; protease I; achromopeptidase; lysyl bond specific proteinase; 72561-05-8; Achromobacter proteinase I; Endoproteinase Lys-C. Enzyme Commission Number: EC 3.4.21.50. CAS No. 72561-05-8. Achromopeptidase. Storage: 2-8°C. Form: lyophilized powder. Source: Lysobacter enzymogenes. EC 3.4.21.50; chromobacter proteinase I; Achromobacter lyticus alkaline proteinase I; protease I; achromopeptidase; lysyl bond specific proteinase; 72561-05-8; Achromobacter proteinase I; Endoproteinase Lys-C. Cat No: NATE-0220. | |
| Native Porcine Elastase | Pancreatic elastase is a form of elastase that is produced in the acinar cells of the pancreas, initially produced as an inactive zymogen and later activated in the duodenum by trypsin. Elastases form a subfamily of serine proteases, characterized by a distinctive structure consisting of two beta barrel domains converging at the active site that hydrolyze amides and esters amongst many proteins in addition to elastin, a type of connective tissue that holds organs together. Pancreatic elastase 1 is a serine endopeptidase, a specific type of protease that has the amino acid serine at its active site. Group: Enzymes. Synonyms: EC 3.4.21.36, pancreatopeptidase E; pancreatic elastase I; elastase; elaszym; serine elastase; elastase-1; pancreatopeptidase; ELA1. Enzyme Commission Number: EC 3.4.21.36. CAS No. 39445-21-1. ELA1. Activity: Type I, > 15 units/mg; Type II, > 4.0 units/mg protein; Type III, > 1 units/mg protein (biuret). Storage: -20°C. Form: Type I, white powder; Type II, Type III, lyophilized powder, Contains sodium carbonate. Source: Porcine pancreas. Species: Porcine. EC 3.4.21.36, pancreatopeptidase E; pancreatic elastase I; elastase; elaszym; serine elastase; elastase-1; pancreatopeptidase; ELA1. Pack: Package size based on protein content. Cat No: NATE-0211. | |
| Native Pseudomonas aeruginosa Elastase | Pancreatic elastase is a form of elastase that is produced in the acinar cells of the pancreas, initially produced as an inactive zymogen and later activated in the duodenum by trypsin. Elastases form a subfamily of serine proteases, characterized by a distinctive structure consisting of two beta barrel domains converging at the active site that hydrolyze amides and esters amongst many proteins in addition to elastin, a type of connective tissue that holds organs together. Pancreatic elastase 1 is a serine endopeptidase, a specific type of protease that has the amino acid serine at its active site. Group: Enzymes. Synonyms: EC 3.4.21.36, pancreatopeptidase E; pancreatic elastase I; elastase; elaszym; serine elastase; elastase-1; pancreatopeptidase; ELA1. Enzyme Commission Number: EC 3.4.24.26. CAS No. 9004-6-2. Purity: > 90% by SDS-PAGE. ELA1. Mole weight: 33000. Stability: Following reconstitution, aliquot and freeze (-20°C) for long-term storage or refrigerate (4°C) for short-term storage. Stock solutions are stable for up to 1 week at 4°Cor for up to 2 months at-20°C. Appearance: Lyophilized. Storage: Storage at-20°C. Source: Pseudomonas aeruginosa. EC 3.4.21.36, pancreatopeptidase E; pancreatic elastase I; elastase; elaszym; serine elastase; elastase-1; pancreatopeptidase; ELA1. Cat No: NATE-0212. | |
| Native Streptomyces griseus Pronase | Pronase is a mixture of several nonspecific endo- and exoproteases that digest proteins down to single amino acids. Applications: Use pronase to completely hydrolyze proteins in research applications. pronase is used for the degradation of proteins during the isolation of dna and rna, such as in the extraction of phage dna or the isolation of plasmid dna. it is not necessary to let pronase self-digest prior to use. it is also used in histochemistry and cell culture for tissue dissociation in conjunction with collagenase and trypsin, and for the production of glycopeptides from purified glycoproteins. Group: Enzymes. Synonyms: non-specific protease. Enzyme Commission Number: EC 3.4.24.4. CAS No. 70851-98-8. Pronase. Activity: ~7.0 units/mg protein (at 40°C with casein as the substrate, pH 7.5, equivalent to approximately 1270 PU/mg or approximately 25 PUK/mg.). Storage: 2-8°C. Form: Lyophilized powder. Source: Streptomyces griseus. non-specific protease; Pronase; EC 3.4.24.4. Cat No: NATE-0997. | |
| Native Tritirachium album limber Proteinase K | Proteinase K (PROK) is a serine protease with broad specificity towards aliphatic, aromatic and other hydrophobic amino acids. PROK has a molecular weight of 27,000 daltons and is Ca2+ dependent. It is not inactivated by metal ion chelating agents such as EDTA, sulfhydryl reagents, PCMB, TLCK, or TPCK. It also retains activity in 0.5% SDS. It can be inhibited by PMSF or DFP. Applications: Useful for the proteolytic inactivation of nucleases during the isolation of dna and rna. removes endotoxins that bind to cationic proteins such as lysozyme and ribonuclease a. reported useful for the isolation of hepatic, yeast, and mung bean mit ochondria determination of enzyme l o...oteinase; Tritirachium album proteinase K; endopeptidase K; 39450-01-6; protease K. Enzyme Commission Number: EC 3.4.21.64. CAS No. 39450-01-6. Purity: Purified to remove DNase and RNase. Proteinase K. Mole weight: 27 kDa. Activity: Type I, > 20 units per mg dry weight; Type II, > 400 u/ml. Storage: Powder: 2-8°C; Liquid: -20°C. Form: Type I, powder; Type II, Liquid in 20mg/ml in 10mM Tris-HCl, 1mM calcium acetate, pH 7.5 containing 50% glycerol. Source: Tritirachium album limber. Proteinase K; EC 3.4.21.64; Tritirachium alkaline proteinase; Tritirachium album serine proteinase; Tritirachium album proteinase K; endopeptidase K; 39450-01-6; protease K. Cat No: NATE-0637. | |
| Native Tritirachium album Proteinase K | Proteinase K is a stable and highly reactive serine protease. Evidence from crystal and molecular structure studies indicates the enzyme belongs to the subtilisin family with an active-site catalytic triad (Asp39-His69-Ser224). It is stable in a broad range of environments:pH, buffer salts, detergents (SDS), and temperature. In the presence of 0.1-0.5% SDS, proteinase K retains activity and will digest a variety of proteins and nucleases in DNA preparations without compromising the integrity of the isolated DNA. Applications: Proteinase k is useful for the proteolytic inactivation of nucleases during the isolation of dna and rna. it is used for the removal of endotoxins bo... used to facilitate the access of probes to rrna using fish techniques to detect pathogenic staphylococcus aureus. useful for the proteolytic inactivation of nucleases during the isolation of dna and rna. removes endotoxins that bind to cationic proteins such as lysozyme and ribonuclease a. reported useful for the isolation of hepatic, yeast, and mung bean mitochondria determination of enzyme localization on membranes treatment of paraffin embedded tissue sections to expose antigen binding sites for antibody labeling. digestion of proteins from brain tissue samples for prions in transmissible spongiform encephalopathies (tse) research. Group: Enzymes. Synonyms: Tritirachiu | |
| Nelfinavir Mesylate (AG-1343, AG1343, Viracept) | Nelfinavir is a potent competitive inhibitor of the HIV-1 protease. It is reported that it can also inhibit the growth of various cell types and trigger apoptosis. Besides being a protease inhibitor used in the therapeutic agent for acquired immunodeficiency syndrome (AIDS), it is also stimulates autophagy and and exhibits anti-cancer properties. It appears to do by inhibition of the Akt/PKB signaling pathway and activation of endoplasmic reticulum stress with subsequent unfolded protein response (1). Nelfinavir has also been shown to treat SARS-coronavirus (2), and is being tested currently to treat COVID-19. Group: Biochemicals. Alternative Names: AG-1343, AG1343, Viracept; (3S, 4aS, 8aS)-N-tert-butyl-2-[(2R, 3R)-2-hydroxy-3-[(3-hydroxy-2-methylbenzoyl)amino]-4-phenylsulfanylbutyl]-3, 4, 4a, 5, 6, 7, 8, 8a-octahydro-1H-isoquinoline-3-carboxamide; methanesulfonic acid. Grades: Highly Purified. CAS No. 159989-65-8. Pack Sizes: 10mg, 25mg, 50mg, 100mg. Molecular Formula: C??H??N?O?S? , Molecular Weight: 663.89. US Biological Life Sciences. |  Worldwide |
| N-Ethylmaleimide | N-Ethylmaleimide (NEM) derives from maleic acid, it can alkylates free sulfhydryl. N-Ethylmaleimide is an irreversible cysteine protease inhibitor. N-ethylmaleimide specific inhibits phosphate transport in mitochondria. N-Ethylmaleimide inhibits prolyl endopeptidase with an IC 50 value of 6.3 μM. N-Ethylmaleimide can be used to modify cysteine residues in proteins and peptides [1] [2] [3]. Uses: Scientific research. Group: Natural products. Alternative Names: NEM. CAS No. 128-53-0. Pack Sizes: 10 mM * 1 mL; 5 mg; 10 mg; 25 mg; 50 mg; 100 mg. Product ID: HY-D0843. | |
| N-Ethylmaleimide | N-Ethylmaleimide (NEM) derives from maleic acid, it can alkylates free sulfhydryl. N-Ethylmaleimide is an irreversible cysteine protease inhibitor. N-ethylmaleimide specific inhibits phosphate transport in mitochondria. N-Ethylmaleimide inhibits prolyl endopeptidase with an IC50 value of 6.3 μM. N-Ethylmaleimide can be used to modify cysteine residues in proteins and peptides. Group: Inhibitorscyclic olefin monomers. Alternative Names: NEM. CAS No. 128-53-0. Molecular formula: C6H7NO2. Mole weight: 125.13 g/mol. Appearance: White Powder to Crystal. Purity: 98.0%(HPLC)(N). IUPACName: 1-ethylpyrrole-2,5-dione. Canonical SMILES: CCN1C(=O)C=CC1=O. Density: 1.207 g/cm³. ECNumber: 204-892-4. Catalog: ACM-MO-128530. | |
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