Find where to buy products from suppliers in the USA, including: distributors, industrial manufacturers in America, bulk supplies and wholesalers of raw ingredients & finished goods.
Search for products or services, then visit the American suppliers website for prices, SDS or more information. You can also view suppliers in Australia, NZ or the UK.
| Product | Description | |
|---|---|---|
| Trypsin | [Source]: porcine pancreas (or bovine pancreas) [Molecular weight] :~23.3KDa [Structure features]: folding single-chain (alkalescence) [Nature]: As a protein enzyme, a type of serine proteases, specialized hydrolysis carboxyl terminal is peptide linkage of alkaline amino acid. Applications: (1) used to research, with polypeptide and protein to survey and evaluate sequence. (2) bio-products tools enzyme, such as activation of the recombinant human insulin original, and so on. (3) biochemical medicine bulk drug. Group: Enzymes. Synonyms: Trypsin; EGF. CAS No. 9002-7-7. Trypsin. Appearance: inquire. Trypsin; EGF. Pack: inquire. Cat No: BIO-1011. |  |
| Trypsin | Trypsin. |  CA, FL & NJ |
| Trypsin | Trypsin is a serine protease enzyme, and hydrolyzes proteins at the carboxyl side of the Lysine or Arginine. Trypsin activates PAR2 and PAR4. Trypsin induces cell-to-cell membrane fusion in PDCoV infection by the interaction of S glycoprotein of PDCoV and pAPN. Trypsin also promotes cell proliferation and differentiation. Trypsin can be used in the research of wound healing and neurogenic inflammation [1] [2] [3] [4] [6]. Uses: Scientific research. Group: Signaling pathways. CAS No. 9002-7-7. Pack Sizes: 100 mg; 500 mg; 1 g. Product ID: HY-129047. |  |
| Trypsin | Trypsin. Uses: For analytical and research use. Group: Impurity standards. CAS No. 9002-7-7. Molecular Formula: C35H47N7O10. Mole Weight: 725.8. Catalog: APB9002077. |  |
| Trypsin (EP) | Trypsin (EP). Uses: For analytical and research use. Group: Enzyme activators, inhibitors & substrates. Alternative Names: Trypsin 1, Trypzean, PTN 6.0S, Serine protease PRSS1, Tripcellim, E.C. 3.4.21.4, PTN, Parenzymol, Trypsin I, Typtar, Sperm receptor hydrolase, E.C. 3.4.4.4, TRYPLE, PTN 3.0S, Pancreatic Trypsin Novo, Trypure, Cocoonase, Pseudotrypsin, Parenzyme, Tryptec Formula One, PTN 6.0S (Pancreatic Trypsin Novo), Trypsin V,Trypsin, PYN 3.0S, Tryptec Formula 4X, PTN 3.0 Special, Trypsin Gold, Pancreatic Trypsin Novo (PTN), Tryptar. CAS No. 9002-7-7. Catalog: APS9002077. Format: Neat. Shipping: Ice pack (-20°C). | |
| Trypsin from Bovine, Recombinant | Trypsin (EC 3.4.21.4) is a serine protease from the PA clan superfamily, found in the digestive system of many vertebrates, where it hydrolyses proteins. Trypsin is produced in the pancreas as the inactive protease trypsinogen. Trypsin cleaves peptide chains mainly at the carboxyl side of the amino acids lysine or arginine, except when either is followed by proline. It is used for numerous biotechnological processes. The process is commonly referred to as trypsin proteolysis or trypsinisation, and proteins that have been digested/treated with trypsin are said to have been trypsinized. Trypsin eliminates the introduction of animal source contaminants found in traditional bovin...tro production of bovine embryos. Group: Enzymes. Synonyms: α-trypsin; β-trypsin; cocoonase; parenzyme; parenzymol; tryptar; trypure; pseudotrypsin; tryptase; tripcellim; sperm receptor hydrolase; Alpha-trypsin; Beta-trypsin; EC 3.4.21.4; Trypsin; Acetyltrypsin. Enzyme Commission Number: EC 3.4.21.4. CAS No. 9002-7-7. Trypsin. Activity: > 3650 units/mg solid (USP). Storage: -20°C. Form: lyophilized powder. Source: Corn. Species: Bovine. α-trypsin; β-trypsin; cocoonase; parenzyme; parenzymol; tryptar; trypure; pseudotrypsin; tryptase; tripcellim; sperm receptor hydrolase; Alpha-trypsin; Beta-trypsin; EC 3.4.21.4; Trypsin; Acetyltrypsin. Cat No: NATE-0724. | |
| Trypsin from Human, Recombinant | Trypsin is a member of the serine protease family. Trypsin cleaves peptides on the C-terminal end of lysine and arginine amino acid residues. The optimum pH is pH 7.0 - 8.0. The enzyme is inhibited by serine protease inhibitors, e.g. PMSF, and by metal chelating agents, e.g., EDTA.Recombinant human trypsin is a genetically engineered protein expressed in E.coli and purified by high pressure liquid chromatography. There are no contaminating enzyme activities such as carboxypeptidase A and chymotrypsin. No protease inhibitors such as PMSF are contained in the preparation. Group: Enzymes. Synonyms: α-trypsin; β-trypsin; coc. Enzyme Commission Number: EC 3.4.21.4. CAS No. 9002-7-7. Purity: ≥ 95% by HPLC. Trypsin. Activity: >2500 USP u/mg protein. Storage: Recombinant human trypsin 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. It is stable within 24 months and above 90% activity remained after 10 times repeated freezing and thawing. Form: White or White-like lyophilized powder. Source: E. Coli. Species: Human. α-trypsin; β-trypsin; cocoonase; parenzyme; parenzymol; tryptar; trypure; pseudotrypsin; tryptase; tripcellim; sperm receptor hydrolase; Alpha-trypsin; Beta-trypsin; EC 3.4.21.4; Trypsin; Acetyltrypsin. Cat No: NATE-1863. | |
| Trypsin from Porcine, Recombinant | Trypsin (EC 3.4.21.4) is a serine protease from the PA clan superfamily, found in the digestive system of many vertebrates, where it hydrolyses proteins. Trypsin is produced in the pancreas as the inactive protease trypsinogen. Trypsin cleaves peptide chains mainly at the carboxyl side of the amino acids lysine or arginine, except when either is followed by proline. It is used for numerous biotechnological processes. The process is commonly referred to as trypsin proteolysis or trypsinisation, and proteins that have been digested/treated with trypsin are said to have been trypsinized. Applications: Trypsin can be used to re-suspend cells adherent to the cell culture dish wal...ring the industrial production of insulin, trypsin is necessary. Group: Enzymes. Synonyms: α-trypsin; β-trypsin; cocoonase; parenzyme; parenzymol; tryptar; trypure; pseudotrypsin; tryptase; tripcellim; sperm receptor hydrolase; Alpha-trypsin; Beta-trypsin; EC 3.4.21.4; Trypsin; Acetyltrypsin. Enzyme Commission Number: EC 3.4.21.4. Purity: >90% (by SDS-PAGE). Mole weight: 24KDa (Determined by SDS-PAGE). Activity: 120 Units/mg protein. Appearance: Colorless aqueous solution. Storage: 4°C, store at -20°C/-80°C for long-term preservation?Avoid multiple freeze-thaw cycles. Form: Freeze dried powder. Source: Porcine. α-trypsin; β-trypsin; cocoonase; parenzyme; | |
| Trypsin inhibitor | Trypsin inhibitor. Group: Biochemicals. Grades: Highly Purified. CAS No. 9035-81-8. Pack Sizes: 250mg, 500mg, 1g, 2g. US Biological Life Sciences. |  Worldwide |
| TRYPSIN INHIBITOR | Heterocyclic Organic Compound. Alternative Names: TRYPSIN INHIBITOR, SOYBEAN;TRYPSIN INHIBITOR TYPE I-S;TRYPSIN INHIBITOR TYPE II-S;TRYPSIN, SOYBEAN INHIBITOR;STI;SOYBEAN TRYPSIN INHIBITOR, IMMOBILIZED;SOYBEAN TRYPSIN INHIBITOR;SBTI. CAS No. 12786-39-9. Catalog: ACM12786399. |  |
| Trypsin Inhibitor (soybean) | Trypsin Inhibitor (soybean) is a peptide inhibitor of serine proteases that reduces trypsin, as well as plasma kallikrein, thrombin, plasmin, and other serine proteases. Synonyms: Kunitz Trypsin Inhibitor; MR 20; SBTI. CAS No. 9035-81-8. |  |
| Trypsin Inhibitor, soybean | Trypsin Inhibitor, soybean is a potent and reversible inhibitor of trypsin [1]. Uses: Scientific research. Group: Biochemical assay reagents. CAS No. 9035-81-8. Pack Sizes: 50 mg; 100 mg. Product ID: HY-126388. | |
| Trypsin, Laboratory Grade, 25 g | Hydrolyzes protein. Health Risk: 2. Flammability: 1. Reactivity: 0. Grades: chem-grade laboratory. CAS No. 9002-7-7. Product ID: 897000. -- SOLD FOR EDUCATIONAL USE ONLY -- |  |
| Trypsin (MS grade) | Trypsin MS grade is a serine protease enzyme, and hydrolyzes proteins at the carboxyl side of the Lysine or Arginine. Trypsin MS grade activates PAR2 and PAR4. Trypsin MS grade induces cell-to-cell membrane fusion in PDCoV infection by the interaction of S glycoprotein of PDCoV and pAPN. Trypsin MS grade also promotes cell proliferation and differentiation. Trypsin MS grade can be used in the research of wound healing and neurogenic inflammation [1] [2] [3] [4] [6]. Uses: Scientific research. Group: Signaling pathways. CAS No. 9002-7-7. Pack Sizes: 100 μg. Product ID: HY-129047A. | |
| Aprotinin, Bovine (Pancreatic trypsin inhibitor) | Aprotinin is a competitive serine protease inhibitor that inhibits trypsin, chymotrypsin, kallikrein and plasmin. Aprotinin forms stable complexes with and blocks the active sites of enzymes. Binding is reversible with most aprotinin-protease complexes, dissociating at pH >10 or <3. Effective concentration is equimolar with protease. Group: Biochemicals. Alternative Names: Antikrein; Antilysin; Antilysine; Aprostat; Aprotinin; BPTI; BPTI Trypsin Inhibitor; Basic Pancreatic Trypsin Inhibitor; Bayer A 128; Bovine Basic Pancreatic Trypsin Inhibitor; Bovine Pancreatic Trypsin Inhibitor; Bovine Trypsin Inhibitor; Fosten; Kallikrein-trypsin Inactivator; Kiker 52G; Kir Richter; Kunitz Pancreatic Trypsin Inhibitor; Kunitz Protease Inhibitor; Kunitz Trypsin Inhibitor; Kunitz-type Inhibitor; Kunitz-type Proteinase Inhibitor; Kunitz-type Trypsin Inhibitor; Onquinin; Pancreatic Basic Trypsin Inhibitor; Pancreatic Trypsin Inhibitor; Pancreatic Trypsin Inhibitor (Kunitz); Protease Inhibitor, Kunitz Type; RP 9921; Repulson; Trasuylol; Trasylol; Trazinin; Triazinin; Trypsin Inhibitor, Trasylol; Trypsin-kallikrein Inhibitor (Kunitz); Zymofren. Grades: Highly Purified. CAS No. 9087-70-1. Pack Sizes: 100mg, 250mg, 500mg, 1g. Molecular Formula: C???H???N??O??S?, Molecular Weight: 6511.45. US Biological Life Sciences. | Worldwide |
| 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. | |
| chymotrypsin C | Formed from pig chymotrypsinogen C, and from cattle subunit II of procarboxypeptidase A. Reacts more readily with Tos-Leu-CH2Cl than Tos-Phe-CH2Cl in contrast to chymotrypsin. In peptidase family S1 (trypsin family). Group: Enzymes. Enzyme Commission Number: EC 3.4.21.2. CAS No. 9036-9-3. 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-4119; chymotrypsin C; EC 3.4.21.2; 9036-09-3. Cat No: EXWM-4119. | |
| Immobilized bovine trypsin | Immobilized bovine trypsin is ideal for digestions of proteins and peptides. Trypsin is a protease that cleaves peptide bonds at Arg and Lys. Trypsin protease is TPCK treated to remove chymotryptic activity before immobilization. Trypsin can be used to provide complementary sequence coverage when compared to chymotryptic digested samples. Group: Enzymes. Synonyms: α-trypsin; β-trypsin; cocoonase; parenzyme; parenzymol; tryptar; trypure; pseudotrypsin; tryptase; tripcellim; sperm receptor hydrolase; Alpha-trypsin; Beta-trypsin; EC 3. 4. 21. 4; Trypsin. Enzyme Commission Number: EC 3. 4. 21. 4. Purity: >95% by SDS-PAGE analysis. Mole weight: 23300. Stability: 12 months from delivery. Storage: 4°C. Form: Resin. Source: Bovine pancreas. Species: Bovine. α-trypsin; β-trypsin; cocoonase; parenzyme; parenzymol; tryptar; trypure; pseudotrypsin; tryptase; tripcellim; sperm receptor hydrolase; Alpha-trypsin; Beta-trypsin; EC 3. 4. 21. 4; Trypsin; Immobilized trypsin. Cat No: NATE-1755. | |
| Immobilized TPCK-Trypsin on F7m | Trypsin hydrolyzes proteins, peptides, amides and esters specifically at the carboxyl groups of the basic amino acids L-arginine or L-lysine. F7m: 1. 0 mg trypsin per CR-column, immobilized on polyvinyl10,200 ST-units immobilized per CR-column. Nr. 15 Storage buffer: 50 mM Tris/HCl at pH 8. 0 at 4°CNr. 67 Reaction buffer: 50 mM phosphate at pH 8. 0Nr. 68 Washing buffer: 50 mM phosphate at pH 8. 0, 1 M NaCl. Group: Enzymes. Synonyms: α-trypsin; β-trypsin; cocoonase; parenzyme; parenzymol; tryptar; trypure; pseudotrypsin; tryptase; tripcellim; sperm receptor hydrolase; Alpha-trypsin; Beta-trypsin; EC 3. 4. 21. 4; Trypsin. Enzyme Commission Number: EC 3. 4. 21. 4. Storage: 4 °C. Source: Bovine pancreas. α-trypsin; β-trypsin; cocoonase; parenzyme; parenzymol; tryptar; trypure; pseudotrypsin; tryptase; tripcellim; sperm receptor hydrolase; Alpha-trypsin; Beta-trypsin; EC 3. 4. 21. 4; Trypsin; Immobilized TPCK-Trypsin; Immobilized Trypsin; TPCK-Trypsin. Cat No: NATE-1771. | |
| Immobilized TPCK-Trypsin on G3m | Trypsin hydrolyzes proteins, peptides, amides and esters specifically at the carboxyl groups of the basic amino acids L-arginine or L-lysine. G3m: 25 ug trypsin per CR-column, immobilized on dextran. 260 ST-units immobilized per CR-column. This CR-column cuts at least 50 ug tubulin per application. Nr. 15 Storage buffer: 50 mM Tris/HCl at pH 8. 0Nr. 67 Reaction buffer: 50 mM phosphate at pH 8. 0 (S?rensen)Nr. 68 Washing buffer: 50 mM phosphate at pH 8. 0, 1 M NaCl. Group: Enzymes. Synonyms: α-trypsin; β-trypsin; cocoonase; parenzyme; parenzymol; tryptar; trypure; pseudotrypsin; tryptase; tripcellim; sperm receptor hydrolase; Alpha-trypsin; Beta-trypsin; EC 3. 4. 21. 4; Trypsin. Enzyme Commission Number: EC 3. 4. 21. 4. Storage: 4 °C. Source: Bovine pancreas. α-trypsin; β-trypsin; cocoonase; parenzyme; parenzymol; tryptar; trypure; pseudotrypsin; tryptase; tripcellim; sperm receptor hydrolase; Alpha-trypsin; Beta-trypsin; EC 3. 4. 21. 4; Trypsin; Immobilized TPCK-Trypsin; Immobilized Trypsin; TPCK-Trypsin. Cat No: NATE-1772. | |
| Immobilized Trypsin, TPCK Treated (Agarose Resin) | Trypsin immobilized on beaded agarose makes it possible to eliminate enzyme contamination of tryptic digests. The trypsin can be easily removed from the digest by separating the trypsin gel from the digestion solution. The Thermo Scientific Immobilized TPCK Trypsin is treated with L-1-tosylamido-2-phenylethyl chloromethyl ketone (TPCK), which is a reagent that has been reported to inhibit chymotrypsin activity without effect on trypsin. Trypsin is a 23,200 molecular weight protein with a pH optimum between 7.5 and 9.0. The isoelectric points of trypsinogen and trypsin are 10.5 and 9.3, respectively. Trypsin has a wide range of applications including amino acid analys...estimated from the number of lysine and arginine residues in the protein. Ionexchange chromatography, paper electrophoresis or peptide mapping can be used to separate digestion fragments. Group: Enzymes. Synonyms: Immobilized Trypsin. Enzyme Commission Number: EC 3.4.21.4. Trypsin. Activity: > 200 TAME units per mL of gel. Storage: Upon receipt store at 4°C. Product is shipped at ambient temperature. Form: 2mL of settled gel supplied as a 50% slurry containing glycerol and 0.05% sodium azide as a preservative. Source: Bovine pancreas. Immobilized Trypsin, TPCK Treated (Agarose Resin); Immobilized Trypsin; Trypsin; Protein Fragmentation Enzymes Kits. Cat No: NATE-1867. | |
| 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 | |
| Native Bovine α-Chymotrypsin | Chymotrypsin is a digestive enzyme component of pancreatic juice acting in the duodenum where it performs proteolysis, the breakdown of proteins and polypeptides. Chymotrypsin preferentially cleaves peptide amide bonds where the carboxyl side of the amide bond (the P1 position) is a large hydrophobic amino acid (tyrosine, tryptophan, and phenylalanine). These amino acids contain an aromatic ring in their sidechain that fits into a 'hydrophobic pocket' (the S1 position) of the enzyme. It is activated in the presence of trypsin. Applications: Chymotrypsin (ec 3.4.21.1, chymotrypsins a and b, alpha-chymar ophth, avazyme, chymar, chymotest, enzeon, quimar, quimotrase, alpha-chym...ate p1 sidechain and the enzyme s1 binding cavity accounts for the substrate specificity of this enzyme. chymotrypsin also hydrolyzes other amide bonds in peptides at slower rates, particularly those containing leucine and methionine at the p1 position. structurally, it is the archetypal structure for its superfamily, the pa clan of proteases. Group: Enzymes. Synonyms: EC 3.4.21.1; α-Chymotrypsin; chymotrypsins A and B; alpha-chymar ophth; avazyme; chymar; chymotest; enzeon; quimar; quimotrase; alpha-chymar; alpha-chymotrypsin A; alpha-chymotrypsin; Chymotrypsin. Enzyme Commission Number: EC 3.4.21.1. CAS No. 9004-7-3. Chymotrypsin. Activity: > 40 units/mg protein. Sto | |
| Native Bovine Trypsin | Trypsin (EC 3.4.21.4) is a serine protease from the PA clan superfamily, found in the digestive system of many vertebrates, where it hydrolyses proteins. Trypsin is produced in the pancreas as the inactive protease trypsinogen. Trypsin cleaves peptide chains mainly at the carboxyl side of the amino acids lysine or arginine, except when either is followed by proline. It is used for numerous biotechnological processes. The process is commonly referred to as trypsin proteolysis or trypsinisation, and proteins that have been digested/treated with trypsin are said to have been trypsinized. Trypsin consists of a single chain polypeptide of 223 amino acid residues, produced by the remova...te is dependent primarily on the cell type and the age of the culture. trypsins have also been used for the re-suspension of cells during cell culture, in proteomics research for digestion of proteins and in various in-gel digestions. additional applications include assessing crystallization by membrane-based techniques and in a study to determine that protein folding rates and yields can be limited by the presence of kinetic traps. trypsin can be used to release adherent cells from tissue culture plates for passaging. trypsin has been used in a study to assess the effects of macromolecular crowding on the structural stability of human α-lactalbumin. trypsin has also been use | |
| Native Bovine Trypsin Acetylated | Trypsin (EC 3.4.21.4) is a serine protease from the PA clan superfamily, found in the digestive system of many vertebrates, where it hydrolyses proteins. Trypsin is produced in the pancreas as the inactive protease trypsinogen. Trypsin cleaves peptide chains mainly at the carboxyl side of the amino acids lysine or arginine, except when either is followed by proline. It is used for numerous biotechnological processes. The process is commonly referred to as trypsin proteolysis or trypsinisation, and proteins that have been digested/treated with trypsin are said to have been trypsinized. The trypsin molecule has two domains: one is related to the enzyme active site and the trypt...e bacterial multidrug atp-binding cassette transporter. Group: Enzymes. Synonyms: α-trypsin; β-trypsin; cocoonase; parenzyme; parenzymol; tryptar; trypure; pseudotrypsin; tryptase; tripcellim; sperm receptor hydrolase; Alpha-trypsin; Beta-trypsin; EC 3.4.21.4; Trypsin; Acetyltrypsin. Enzyme Commission Number: EC 3.4.21.4. Trypsin. Activity: > 8,500 BAEE units/mg protein (biuret). Storage: -20°C. Source: Bovine pancreas. Species: Bovine. α-trypsin; β-trypsin; cocoonase; parenzyme; parenzymol; tryptar; trypure; pseudotrypsin; tryptase; tripcellim; sperm receptor hydrolase; Alpha-trypsin; Beta-trypsin; EC 3.4.21.4; Trypsin; Acetyltrypsin. Cat No: NATE-0720. | |
| Native Bovine Trypsin & Chymotrypsin Mixtures | Native Bovine Trypsin & Chymotrypsin Mixtures. Creative enzymes is a world leading producer of trypsin / chymotrypsin mixtures. trypsin and chymotrypsin are extracted from bovine pancreas and pancreatic juices using multiple precipitation, fractionation, and filtration steps. creative enzymes products are not intended for use in pharmaceutical applications. Applications: In combination with chymotrypsinogen and ribonuclease it is used to formulate anti-inflammatory tablets /treatment of wounds (internal and external) / mixtures of trypsin and chymotrypsin in different ratios frequently are used in digestive aids and food. Group: Enzymes. Synonyms: Trypsin & Chymotrypsin. Trypsin-Chymotrypsin. Activity: >1000 :1000 NF U/mg. Storage: Store at <-15°C. Source: Bovine pancreas. Species: Bovine. Trypsin & Chymotrypsin. Cat No: NATE-0719. | |
| Native Human α-1-Antitrypsin | Alpha-1 Antitrypsin or α1-antitrypsin (A1AT) is a protease inhibitor belonging to the serpin superfamily. It is generally known as serum trypsin inhibitor. Alpha 1-antitrypsin is also referred to as alpha-1 proteinase inhibitor (A1PI) because it inhibits a wide variety of proteases. It protects tissues from enzymes of inflammatory cells, especially neutrophil elastase, and has a reference range in blood of 1.5-3.5 gram/liter (in US the reference range is generally expressed as mg/dL or micromoles), but the concentration can rise manyfold upon acute inflammation. In its absence, neutrophil elastase is free to break down elastin, which contributes to the elasticity of the lungs, resulting in respiratory complications such as emphysema, or COPD (chronic obstructive pulmonary disease) in adults and cirrhosis in adults or children. Group: Enzymes. Synonyms: Alpha-1-Antitrypsin; A1AT; α1-antitrypsin; SERPINA1; A1A; A1AT; AAT; PI; PI1; PRO2275; alpha1AT. CAS No. 9041-92-3. Purity: > 95% (SDS-PAGE). A1AT. Mole weight: 54kDa. Storage: 2-8°C. Form: Lyophilized. Source: Human Plasma. Species: Human. Alpha-1-Antitrypsin; A1AT; α1-antitrypsin; SERPINA1; A1A; A1AT; AAT; PI; PI1; PRO2275; alpha1AT. Cat No: NATE-0010. | |
| Native Human α-Chymotrypsin | Chymotrypsin is a digestive enzyme component of pancreatic juice acting in the duodenum where it performs proteolysis, the breakdown of proteins and polypeptides. Chymotrypsin preferentially cleaves peptide amide bonds where the carboxyl side of the amide bond (the P1 position) is a large hydrophobic amino acid (tyrosine, tryptophan, and phenylalanine). These amino acids contain an aromatic ring in their sidechain that fits into a 'hydrophobic pocket' (the S1 position) of the enzyme. It is activated in the presence of trypsin. Applications: Human α-chymotrypsin has been used in a study to assess the quantitative structure-activity relationships for organophosphates binding to trypsin and chymotrypsin. human α-chymotrypsin has also been used in a study to investigate the direct detection of native proteins in biological matrices using extractive electrospray ionization mass spectrometry. Group: Enzymes. Synonyms: EC 3.4.21.1; α-Chy. Enzyme Commission Number: EC 3.4.21.1. CAS No. 9004-7-3. Chymotrypsin. Mole weight: mol wt 25 kDa. Storage: -20°C. Form: lyophilized powder. Source: Human pancreas. Species: Human. EC 3.4.21.1; α-Chymotrypsin; chymotrypsins A and B; alpha-chymar ophth; avazyme; chymar; chymotest; enzeon; quimar; quimotrase; alpha-chymar; alpha-chymotrypsin A; alpha-chymotrypsin; Chymotrypsin. Cat No: NATE-0747. | |
| Native Human Trypsin | Trypsin (EC 3.4.21.4) is a serine protease from the PA clan superfamily, found in the digestive system of many vertebrates, where it hydrolyses proteins. Trypsin is produced in the pancreas as the inactive protease trypsinogen. Trypsin cleaves peptide chains mainly at the carboxyl side of the amino acids lysine or arginine, except when either is followed by proline. It is used for numerous biotechnological processes. The process is commonly referred to as trypsin proteolysis or trypsinisation, and proteins that have been digested/treated with trypsin are said to have been trypsinized. Applications: Trypsin has been used in a study to assess the similarities between the hepatitis e virus and human astrovirus. trypsin has also been used in a study to characterize a unique technique for culturing primary adult human epithelial progenitor, or stem, cells. Group: Enzymes. Synonyms: α-trypsin; β-trypsin; cocoonase; parenzyme; parenzymol; trypta. Enzyme Commission Number: EC 3.4.21.4. CAS No. 9002-7-7. Trypsin. Activity: vial of > 1 ,000 BAEE units. Storage: 2-8°C. Form: salt-free, lyophilized powder. Source: Human pancreas. Species: Human. α-trypsin; β-trypsin; cocoonase; parenzyme; parenzymol; tryptar; trypure; pseudotrypsin; tryptase; tripcellim; sperm receptor hydrolase; Alpha-trypsin; Beta-trypsin; EC 3.4.21.4; Trypsin. Cat No: NATE-0722. | |
| Native Porcine Trypsin | Trypsin (EC 3.4.21.4) is a serine protease from the PA clan superfamily, found in the digestive system of many vertebrates, where it hydrolyses proteins. Trypsin is produced in the pancreas as the inactive protease trypsinogen. Trypsin cleaves peptide chains mainly at the carboxyl side of the amino acids lysine or arginine, except when either is followed by proline. It is used for numerous biotechnological processes. The process is commonly referred to as trypsin proteolysis or trypsinisation, and proteins that have been digested/treated with trypsin are said to have been trypsinized. Trypsin cleaves peptides on the c-terminal side of lysine and arginine residues. the rate of hydr... others, will inhibit trypsin. Applications: For use in immunohistochemical procedures to enhance staining and to unmask antigens after routine fixation and processing. for trypsin digestion of peptides, use a ratio of about 1:100 to 1:20 for trypsin:peptide. the typical use for this product is in removing adherent cells from a culture surface. the concentration of trypsin necessary to dislodge cells from their substrate is dependent primarily on the cell type and the age of the culture. trypsins have also been used for the re-suspension of cells during cell culture, in proteomics research for digestion of proteins and in various in-gel digestionsns+. additional applications inclu | |
| Native Swine (Bovine) Trypsin-Chymotrypsin 1: 1 | Trypsin-Chymotrypsin is the co-crystal of Chymotrypsin and Trypsin so it has the properties of both. The activity of hydrolyzing casein is as much as Chymotrypsin. But the activity of its Chemotrypsin to hydrolyze N-Benzoyl-L-tyrosine ethyl ester?BTEE?is three times higher than Chemotrypsin.The activity of hydrolyze ester bond similar to that of Trypsin. It is stable when dry and easy to be inactivated in solutions. The optimum pH is 7.0-8.0. The high purity Trypsin-Chymotrypsin is purified by re-crystallization, and then by Ion Exchange Chromatography and ultra-filtration. Applications: 1. as pharmaceutical raw materials for antibacterial, anti-inflammatory, clinical. 2. as analytical reagents used in scientific research institutions. Group: Enzymes. Synonyms: Trypsin-Chymotrypsin 1: 1. Trypsin-Chymotrypsin. Activity: Trypsin: 1000 ~1100 USP units/mg, powder; Chymotrypsin 1000 ~1100 USPunits/mg, powder. Appearance: White or almost white powder. Storage: Sealed, Dark, at temperature 2-8°C. Form: Powder. Source: Swine (Bovine) pancreas. Species: Swine (Bovine). Trypsin-Chymotrypsin 1: 1. Cat No: PHAM-378. | |
| Native Swine (Bovine) Trypsin-Chymotrypsin 1: 250 | Trypsin-Chymotrypsin is the co-crystal of Chymotrypsin and Trypsin so it has the properties of both. The activity of hydrolyzing casein is as much as Chymotrypsin. But the activity of its Chemotrypsin to hydrolyze N-Benzoyl-L-tyrosine ethyl ester?BTEE?is three times higher than Chemotrypsin.The activity of hydrolyze ester bond similar to that of Trypsin. It is stable when dry and easy to be inactivated in solutions. The optimum pH is 7.0-8.0. The high purity Trypsin-Chymotrypsin is purified by re-crystallization, and then by Ion Exchange Chromatography and ultra-filtration. Applications: 1. as a laboratory analysis reagent, is scientific research institutions widely used. 2. animal cell culture of tissue processing. Group: Enzymes. Synonyms: Trypsin-Chymotrypsin 1: 250. Trypsin-Chymotrypsin. Activity: Trypsin > 2400 USP units/mg, powder; Chymotrypsin < 75 USP units/mg, powder. Appearance: White or almost white powder. Storage: Sealed, Dark, at temperature 2-8°C. Form: Powder. Source: Swine (Bovine) pancreas. Species: Swine (Bovine). Trypsin-Chymotrypsin 1: 250. Cat No: PHAM-379. | |
| Native Swine (Bovine) Trypsin-Chymotrypsin 6: 1 | Trypsin-Chymotrypsin is the co-crystal of Chymotrypsin and Trypsin so it has the properties of both. The activity of hydrolyzing casein is as much as Chymotrypsin. But the activity of its Chemotrypsin to hydrolyze N-Benzoyl-L-tyrosine ethyl ester?BTEE?is three times higher than Chemotrypsin.The activity of hydrolyze ester bond similar to that of Trypsin. It is stable when dry and easy to be inactivated in solutions. The optimum pH is 7.0-8.0. The high purity Trypsin-Chymotrypsin is purified by re-crystallization, and then by Ion Exchange Chromatography and ultra-filtration. Applications: 1. in the clinical, the treatment of various inflammatory, inflammatory edema, hematoma, postoperative adhesion, ulcer, thrombus and so on and have a certain effect to chronic bronchitis asthma, gastritis, cervicitis, pelvic inflammatory disease, suppurative otitis media, prostatitis, thrombophlebitis and cerebral thrombosis. 2. application in modern industrial fields, such as senior leather depilation, softener. Group: Enzymes. Synonyms: . Trypsin-Chymotrypsin. Activity: Trypsin > 2400 USP units/mg, powder; Chymotrypsin > 400 USP units/mg, powder. Appearance: White or almost white powder. Storage: Sealed, Dark, at temperature 2-8°C. Form: Powder. Source: Swine (Bovine) pancreas. Species: Swine (Bovine). Trypsin-Chymotrypsin 6: 1. Cat No: PHAM-380. | |
| 1,2-Dilaurin | 1,2-Dilaurin is a diacylglycerol containing lauric acid at the sn-1 and sn-2 positions. It has been used as an internal standard for the quantification of diglycerides in rat desheathed sciatic nerves. [1] Monomolecular films containing 1,2-dilauroyl-rac-glycerol have been used as substrates to measure surface pressure and the effect of pancreatic procolipase and colipase on porcine pancreatic lipase activity. [2] References: [1]. Zhu, X. and Eichberg, J. 1,2-Diacylglycerol content and its arachidonyl-containing molecular species are reduced in the sciatic nerve of streptozotocin-induced diabetic rats. J. Neurochemistry. 55(3), 1087-1090 (1990).[2]. Wieloch, T., Borgstr m, B., Piéroni, G. et al. Porcine trypsinogen and its trypsin-activated form: lipid binding and lipase activation on monomolecular membranes. FEBS Express. 128(2), 217-220 (1981). Uses: Scientific research. Group: Biochemical assay reagents. Alternative Names: (Rac)-1,2-Didodecanoylglycerol. CAS No. 17598-94-6. Pack Sizes: 5 mg; 10 mg. Product ID: HY-W127391. | |
| 1-Methyl-1H-benzotriazole | A benzotriazole derivative with potential inhibitory effect on protease enzymes chymotrypsin, trypsin and papain. Group: Biochemicals. Grades: Highly Purified. CAS No. 13351-73-0. Pack Sizes: 1g, 2.5g. Molecular Formula: C7H7N3. US Biological Life Sciences. | Worldwide |
| 1-Methyl-1H-benzotriazole-d3 | 1-Methyl-1H-benzotriazole-d3 is the labeled derivative of 1-Methyl-1H-benzotriazole (M289810), which is the benzotriazole derivative with potential inhibitory effect on protease enzymes chymotrypsin, trypsin and papain. Group: Biochemicals. Grades: Highly Purified. Pack Sizes: 1g, 10g. Molecular Formula: C7H4D3N3, Molecular Weight: 136.169999999999. US Biological Life Sciences. | Worldwide |
| 3-Acetylbenzoyl Chloride | 3-Acetylbenzoyl Chloride is used in the synthesis of aminimdes as potential CNS acting agents. Also, it is an intermediate used in the synthesis of 3-[ (Dimethylamino) carbonyl]phenol (D461635), which can be used in the synthesis of novel purine and bicyclic pyrimidine, which are factor Xa inhibitors, and also have high selectivity over thrombin and trypsin. Group: Biochemicals. Grades: Highly Purified. CAS No. 31076-85-4. Pack Sizes: 100mg, 250mg. Molecular Formula: C9H7ClO2, Molecular Weight: 182.6. US Biological Life Sciences. | Worldwide |
| 4-Aminobenzamidine-13C2,15N4 Dihydrochloride | A labeled synthetic diamidine derivative that acts as a urokinase inhibitor as well as trypsin inhibitor. Group: Biochemicals. Alternative Names: 4-Amino Benzene carboximidamide-13C2, 15N4 Dihydrochloride; 4-Amidinoaniline-13C2,15N4 Dihydrochloride; 4-Aminobenzamidine-13C2,15N4 Dihydrochloride; SC 67235-13C2,15N4 ; p-Aminobenzamidine-13C2,15N4 Dihydrochloride. Grades: Highly Purified. Pack Sizes: 2.5mg. US Biological Life Sciences. | Worldwide |
| 4-Aminobenzamidine dihydrochloride | A synthetic diamidine derivative that acts as a urokinase inhibitor as well as trypsin inhibitor. Synonyms: p-Aminobenzamidine 2HCl. Grades: ≥ 99 % (Assay). CAS No. 2498-50-2. Molecular formula: C7H9N3·2HCl. Mole weight: 208.09. | |
| 4-Aminobenzamidine Dihydrochloride | A synthetic diamidine derivative that acts as a urokinase inhibitor as well as trypsin inhibitor. Group: Biochemicals. Alternative Names: 4-Amino Benzene carboximidamide Dihydrochloride; 4-Amidinoaniline Dihydrochloride; 4-Aminobenzamidine Dihydrochloride; SC 67235; p-Aminobenzamidine Dihydrochloride. Grades: Highly Purified. CAS No. 2498-50-2. Pack Sizes: 2.5g. US Biological Life Sciences. | Worldwide |
| 4-Iodobenzylamine | 4-Iodobenzylamine ((4-Iodophenyl)methanamine) is a probe that can detect the binding patterns of serine proteases that are like trypsin, as well as urokinase-type plasminogen activator (uPA). 4-Iodobenzylamine is stable in aqueous solution [1] [2]. Uses: Scientific research. Group: Signaling pathways. Alternative Names: (4-Iodophenyl)methanamine. CAS No. 39959-59-6. Pack Sizes: 5 g; 10 g; 25 g. Product ID: HY-W013964. | |
| Ac-Arg-Gly-Lys-AMC | Ac-Arg-Gly-Lys-AMC is a control for the two step histone deacetylase assay with Ac-Arg-Gly-Lys(Ac)-AMC. It corresponds to the product of the deacetylase reaction, which is subsequently cleaved by trypsin. Synonyms: Ac-RGK-AMC; N2-Acetyl-L-arginylglycyl-N-(4-methyl-2-oxo-2H-1-benzopyran-7-yl)-L-Lysinamide; N2-Acetyl-L-arginylglycyl-N-(4-methyl-2-oxo-2H-chromen-7-yl)-L-lysinamide; (S)-2-(2-((S)-2-acetamido-5-guanidinopentanamido)acetamido)-6-amino-N-(4-methyl-2-oxo-2H-chromen-7-yl)hexanamide. Grades: ≥95%. CAS No. 660846-99-1. Molecular formula: C26H38N8O6. Mole weight: 558.64. | |
| Ac-Arg-Leu-Arg-AMC | Ac-Arg-Leu-Arg-AMC is a fluorogenic substrate for the determination of the trypsin-like activity of purified proteasomes (Km = 78 μM). Synonyms: Ac-RLR-AMC; N2-Acetyl-L-arginyl-L-leucyl-N-(4-methyl-2-oxo-2H-chromen-7-yl)-L-argininamide; L-Argininamide, N2-acetyl-L-arginyl-L-leucyl-N-(4-methyl-2-oxo-2H-1-benzopyran-7-yl)-. Grades: ≥95%. CAS No. 929903-87-7. Molecular formula: C30H46N10O6. Mole weight: 642.76. | |
| Ac-RLR-AMC trifluoroacetate salt | Ac-RLR-AMC is a fluorogenic substrate for the 26S proteasome. Ac-RLR-AMC is cleaved to release the fluorescent moiety 7-amino-4-methylcoumarin (AMC), which can be used to quantify the trypsin-like activity of 26S proteasomes. Synonyms: Ac-Arg-Leu-Arg-7-amino-4-methylcoumarin; (S)-2-acetamido-5-guanidino-N-((S)-1-(((S)-5-guanidino-1-((4-methyl-2-oxo-2H-chromen-7-yl)amino)-1-oxopentan-2-yl)amino)-4-methyl-1-oxopentan-2-yl)pentanamide, 2,2,2-trifluoroacetate salt. Grades: ≥98%. Molecular formula: C30H46N10O6·CF3COOH. Mole weight: 756.8. | |
| acrosin | Occurs in spermatozoa; formed from proacrosin by limited proteolysis. Inhibited by naturally occurring trypsin inhibitors. In peptidase family S1 (trypsin family). Group: Enzymes. Synonyms: acrosomal proteinase; acrozonase; α-acrosin; β-acrosin; upsilon-acrosin; acrosomal protease; acrosin amidase. Enzyme Commission Number: EC 3.4.21.10. CAS No. 9068-57-9. 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-4094; acrosin; EC 3.4.21.10; 9068-57-9; acrosomal proteinase; acrozonase; α-acrosin; β-acrosin; upsilon-acrosin; acrosomal protease; acrosin amidase. Cat No: EXWM-4094. | |
| Adenovirus Proteinase Inhibitor, NSC 37249 (2- (Dicyclohexylamino) -N- (4- (4- ( (2- (dicyclohexylamino) acetyl) amino) phenyl) sulfonylphenyl) acetamide, N, N?- (Sulfonyldi-4, 1-phenylene) bis (2- (dicyclohexylamino) acetamide, AVP Inhibitor) | A sulfonyl diphenyl ene -bis-dicyclohexyl aminoacetamide compound that acts as a potent and selective inhibitor against adenovirus cysteine proteinase AVP by targeting simultaneously AVP co-factor pVIc (GVQSLKRRRCF) N-terminal binding pocket (Ki = 150nM) and AVP-pVIc substrate-binding site (Ki = 400nM), blocking both AVP-pVIc active complex formation (IC50 = 140nM; [substrate] = 5uM & [pVIc] = 40uM) and catalytic activity (IC50 = 490nM; [substrate] = 5uM) without affecting trypsin or papain protease activity even at concentrations as high as 10uM. Group: Biochemicals. Grades: Purified. CAS No. 2907-88-2. Pack Sizes: 10mg. Molecular Formula: C??H??N?O?S. US Biological Life Sciences. | Worldwide |
| AEBSF HCl | AEBSF is a water-soluble, irreversible serine protease inhibitor that inhibits proteases like chymotrypsin, kallikrein, plasmin, thrombin, and trypsin. Synonyms: 4-(2-Aminoethyl)benzenesulfonyl fluoride hydrochloride; AEBSF hydrochloride; AEBSF. Grades: 98%. CAS No. 30827-99-7. Molecular formula: C8H11ClFNO2S. Mole weight: 239.69. | |
| AEBSF hydrochloride | AEBSF hydrochloride is an irreversible inhibitor of serine proteases , such as chymotrypsin, kallikrein, plasmin, thrombin, and trypsin. Uses: Scientific research. Group: Signaling pathways. CAS No. 30827-99-7. Pack Sizes: 10 mM * 1 mL; 100 mg; 200 mg. Product ID: HY-12821. | |
| Aloxistatin (E-64d) | Aloxistatin (E-64d), is a selective cysteine protease inhibitor or calpain and autophagy inhibitor. E-64d prevents in vitro cerulein- induced trypsinogen activation. E-64d can enter the intact cell and inhibit calpain. E-64d has been shown safe for the treatment of Alzheimer's disease in human. E-64d is potentially useful in the treatment of developmental seizure-induced brain damage both by regulating abnormal zinc signal transduction and through the modulation of altered lipid metabolism via ApoE/clusterin pathway in hippocampus. Group: Inhibitors. Alternative Names: E-64d; E 64d; E64d; E64-d; E64-d; E64 d; ethyl ester Loxistatin; NSC 694281; NSC694281; NSC-694281; EST; EP-453; EP453; EP 453; Aloxistatin. CAS No. 88321-09-9. Molecular formula: C17H30N2O5. Mole weight: 342.44. Appearance: Solid powder. Purity: >98%. IUPACName: ethyl (2S,3S)-3-(((S)-1-(isopentylamino)-4-methyl-1-oxopentan-2-yl)carbamoyl)oxirane-2-carboxylate. Canonical SMILES: CCOC ([C@@H]1[C@@H] (C (N[C@H] (C (NCCC (C)C)=O)CC (C)C)=O)O1)=O. Catalog: ACM88321099. | |
| 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. | |
| α-Lytic Protease M190A Mutant, Recombinant | Alpha-lytic protease (aLP) is an alternative specificity protease for proteomics applications, whose wild-type (WT) version cleaves after T, A, S, and V residues. The M190A (Met190 ? Ala190) mutant of aLP has different cleavage specificities, and cleaves after M, F, and L residues. Both the WT and M190A forms of aLP geneRate peptides of similar average length as trypsin. Group: Enzymes. Synonyms: ALP M190A; Alpha-Lytic Protease M190A Mutant. ALP M190A. Activity: > 0.05 U/mg. Storage: -70°C. ALP M190A; Alpha-Lytic Protease M190A Mutant. Cat No: NATE-0051. | |
| alternative-complement-pathway C3/C5 convertase | A bimolecular complex of complement fragment Bb with either C3b or cobra venom factor; Bb contains the active site. Bb is formed by cleavage of proenzyme factor B by factor D. Cleavage of complement component C5 requires additional C3b which binds C5 and renders it susceptible to cleavage by C3b,Bb complex. C3b,Bb is stabilized in plasma by factor P. Complement factor B is in peptidase family S1 (trypsin family). Group: Enzymes. Synonyms: complement component C3/C5 convertase (alternative); proenzyme factor B; properdin factor B; C3 proactivator; glycine-rich β-glycoprotein; heat-labile factor; C3 convertase; C3. Enzyme Commission Number: EC 3.4.21.47. CAS No. 80295-67-6. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4140; alternative-complement-pathway C3/C5 convertase; EC 3.4.21.47; 80295-67-6; complement component C3/C5 convertase (alternative); proenzyme factor B; properdin factor B; C3 proactivator; glycine-rich β-glycoprotein; heat-labile factor; C3 convertase; C3b,Bb,CVF,Bb,C5 convertase; (C3b)n,Bb; complement C 3(C 5) convertase (amplification); alternative complement pathway C3(C5) convertase; C5 convertase; CVF,Bb; (CVF)-dependent glycine-rich-β-glucoprotein; cobra venom factor-dependent C3 convertase. Cat No: EXWM-4140. | |
| Antifungal protein J | Antifungal protein J is an antimicrobial peptide found in Solanum tuberosum (Potato). It has antifungal activity and is an inhibitor of serine proteases chymotrypsin, pepsin and trypsin. Synonyms: AFP-J; Leu-Pro-Ser-Asp-Ala-Thr-Leu-Val-Leu-Asp-Gln-Thr-Gly-Lys-Glu-Leu-Asp-Ala-Arg-Leu. Grades: ≥96%. Molecular formula: C93H159N25O33. Mole weight: 2155.43. | |
| Aprotinin | Aprotinin is a bovine pancreatic trypsin inhibitor (BPTI) inhibitor which inhibits trypsin and chymotrypsin with K i s of 0.06 pM and 9 nM, respectively. Uses: Scientific research. Group: Peptides. CAS No. 9087-70-1. Pack Sizes: 5 mg; 10 mg; 25 mg; 50 mg; 100 mg. Product ID: HY-P0017. | |
| aspergillopepsin I | Found in a variety of Aspergillus species (imperfect fungi): Aspergillus awamori (awamorin, aspergillopepsin A:), A. foetidus (aspergillopepsin F:), A. fumigatus, A. kawachii, A. niger (proteinase B, proctase B:), A. oryzae (trypsinogen kinase:), A. saitoi (aspergillopeptidase A:), and A. sojae. In peptidase family A1 (pepsin A family). Formerly included in EC 3.4.23.6. Group: Enzymes. Synonyms: Aspergillus acid protease; Aspergillus acid proteinase; Aspergillus aspartic proteinase; Aspergillus awamori acid proteinase; Aspergillus carboxyl proteinase; (see also Comments); carboxyl proteinase; Aspergillus kawachii aspartic proteinase; Aspergillus saitoi acid proteinase; pepsin-type aspartic proteinase. Enzyme Commission Number: EC 3.4.23.18. CAS No. 9025-49-4. Storage: Store it at +4 ?C for short term. For long term storage, store it at -20 ?C?-80 ?C. Form: Liquid or lyophilized powder. EXWM-4255; aspergillopepsin I; EC 3.4.23.18; 9025-49-4; Aspergillus acid protease; Aspergillus acid proteinase; Aspergillus aspartic proteinase; Aspergillus awamori acid proteinase; Aspergillus carboxyl proteinase; (see also Comments); carboxyl proteinase; Aspergillus kawachii aspartic proteinase; Aspergillus saitoi acid proteinase; pepsin-type aspartic proteinase; Aspergillus niger acid proteinase; sumizyme AP; proctase P; denapsin; denapsin XP 271; proctase. Cat No: EXWM-4255. | |
| Aureoquinone | Aureoquinone is produced by the strain of Aureobasidium sp. The IC50 (μg/mL) for inhibiting the activity of protease, including trypsin, papain, thermophilic protease, collagenase and pound-protease are 11.4?14.5?17.8?7.1?and 8.7 respectively. Synonyms: 2,5,7,8-tetrahydroxy-3,6-dimethylnaphthalene-1,4-dione. Molecular formula: C12H10O6. Mole weight: 250.20. | |
| Benzamidine hydrochloride | Benzamidine hydrochloride is a trypsin-like serine proteases with K i s of 20, 21, 97, 110, 320 and 750 μM against Tryptase, Trypsin, uPA, Factor Xa, Thrombin and tPA, respectively [1]. Uses: Scientific research. Group: Signaling pathways. CAS No. 1670-14-0. Pack Sizes: 10 mM * 1 mL; 100 mg; 500 mg. Product ID: HY-W018781. | |
| Benzamidine hydrochloride | Benzamidine is a reversible inhibitor of serine proteases, including trypsin, plasmin, and thrombin (Kis = 35, 350, and 220 μM, respectively). Benzamidine inhibits the autoactivation of human blood coagulation factor VII, useful as a tool for studying the interactions between this and other relevant growth factors. Uses: Serine proteinase inhibitors. Synonyms: Benzenecarboximidamide, hydrochloride (1:1); Benzamidine, monohydrochloride; Benzenecarboximidamide, monohydrochloride; Amidinobenzene hydrochloride; Benzamidinium chloride; Benzimidamide hydrochloride. Grades: ≥98%. CAS No. 1670-14-0. Molecular formula: C7H8N2.HCl. Mole weight: 156.61. | |
| Benzamidine hydrochloride hydrate | Benzamidine (Benzenecarboximidamide) hydrochloride hydrate is a reversible competitive trypsin-like serine proteases inhibitor with K i s of 20, 21, 97, 110, 320 and 750 μM against Tryptase, Trypsin, uPA, Factor Xa, Thrombin and tPA, respectively [1] [2]. Uses: Scientific research. Group: Biochemical assay reagents. Alternative Names: Benzenecarboximidamide hydrochloride hydrate. CAS No. 206752-36-5. Pack Sizes: 5 g; 10 g. Product ID: HY-W087937. | |
| BMS-354326 | BMS-354326 is a tryptase inhibitor with IC50 value of 1.8 nM. It has excellent selectivity against trypsin and most other related serine proteases. Synonyms: BMS-354326; BMS 354326; BMS354326; CHEMBL306448; BDBM50144532.(2S,3R)-4-oxo-1-((4-(1-oxo-6-phenylhexyl)-1-piperazinyl)carbonyl)-3-(2-(3-piperidinyl)ethyl)- 2-Azetidinecarboxylic acid. Grades: 98%. CAS No. 708258-16-6. Molecular formula: C28H40N4O5. Mole weight: 512.65. | |
| BMS-36313 | BMS-363131 is very potent inhibitor of human tryptase with inhibitory activity against bovine trypsin. Uses: Tryptase inhibitor. Synonyms: BMS-363131; BMS 363131; BMS363131. (2S,3R)-3-[[(3R)-1-carbamimidoylpiperidin-3-yl]methyl]-4-oxo-1-[4-(6-phenylhexanoyl)piperazine-1-carbonyl]azetidine-2-carboxylic acid. Grades: ≥98%. CAS No. 384829-65-6. Molecular formula: C28H40N6O5. Mole weight: 540.66. | |
| Boc-Gln-Ala-Arg-pNA | Boc-Gln-Ala-Arg-pNA is a chromogenic substrate for trypsin and matriptase-2. Synonyms: Boc-QAR-pNA; L-Argininamide, N2-[(1,1-dimethylethoxy)carbonyl]-L-glutaminyl-L-alanyl-N-(4-nitrophenyl)-; N2-{[(2-Methyl-2-propanyl)oxy]carbonyl}-L-glutaminyl-L-alanyl-N-(4-nitrophenyl)-L-argininamide; N-Boc-Gln-Ala-Arg-p-nitroanilide. Grades: ≥95% by HPLC. CAS No. 1926163-47-4. Molecular formula: C25H39N9O8. Mole weight: 593.63. | |
| Boc-Glu(OBzl)-Gly-Arg-AMC HCl | Substrate for coagulation factors IXa and XIIa as well as for trypsin and soybean trypsin-like enzyme. Synonyms: benzyl (4S)-5-[[2-[[(2S)-5-(diaminomethylideneamino)-1-[(4-methyl-2-oxochromen-7-yl)amino]-1-oxopentan-2-yl]amino]-2-oxoethyl]amino]-4-[(2-methylpropan-2-yl)oxycarbonylamino]-5-oxopentanoate hydrochloride. Grades: ≥ 96% (HPLC). CAS No. 133448-22-3. Molecular formula: C35H45N7O9·HCl. Mole weight: 744.24. | |
| Boc-glycine 4-nitrophenyl ester | A substrate for chymotrypsin and trypsin. Synonyms: Boc-Gly-Onp; 4-nitrophenyl n-(tert-butoxycarbonyl)glycinate; 4-Nitrophenyl N-((1,1-dimethylethoxy)carbonyl)glycinate. Grades: ≥ 98% (TLC). CAS No. 3655-5-8. Molecular formula: C13H16N2O6. Mole weight: 296.30. | |
| Boc-Val-Pro-Arg-AMC hydrochloride | Boc-Val-Pro-Arg-AMC hydrochloride is a sensitive fluorogenic substrate for measuring trypsin-like serine proteases activity [1]. Uses: Scientific research. Group: Peptides. CAS No. 70375-24-5. Pack Sizes: 5 mg; 10 mg. Product ID: HY-137784. | |
| 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. | |
| Camostat mesylate | Camostat mesylate (Camostat mesilate) is an orally active, synthetic serine protease inhibitor for chronic pancreatitis. Camostat mesylate, an inhibitor of TMPRSS2 , shows antiviral activity against SARS-CoV-2. Camostat mesylate also inhibits the activity of prostasin, trypsin, and matriptase [1] [2] [3]. Uses: Scientific research. Group: Natural products. Alternative Names: Camostat mesilate; FOY305; FOY-S980. CAS No. 59721-29-8. Pack Sizes: 10 mM * 1 mL; 5 mg; 10 mg; 50 mg; 100 mg. Product ID: HY-13512. | |
| Camostat Mesylate | Camostat (INN) or FOY-305 is a serine protease inhibitor. Serine protease enzymes have a variety of functions in the body, and so camostat has a diverse range of uses. It is used in the treatment of some forms of cancer and is also effective against some viral infections, as well as inhibiting fibrosis in liver or kidney disease orpancreatitis. Uses: Trypsin inhibitors. Synonyms: 4-(2-(2-(dimethylamino)-2-oxoethoxy)-2-oxoethyl)phenyl 4-guanidinobenzoate methanesulfonate; Camostat Mesilate; Camostat Mesylate; FOY 305; FOY-305; FOY305. Grades: >98%. CAS No. 59721-29-8. Molecular formula: C20H22N4O5.CH4O3S. Mole weight: 494.52. | |
| Camostat Mesylate | Orally active, non-peptide proteolitic enzyme inhibitor with anti-trypsin and anti-plasmin activities, related structurally to gabexate. Protease inhibitor. Camostat mesilate is a serine protease inhibitor that inhibits plasmin, kallikrein, thrombin as well as trypsin, which attenuates pancreatic fibrosis. It reduces weight gain and improves metabolism in obese rodent models. It is in clinical use (in Japan) for pancreatitis. Camostat has been found to inhibit influenza virus replication in human tracheal epithelial cells and is also a direct prostasin inhibitor which may be useful in reducing sodium transport in cystic fibrosis. Additionally it has been shown to reduce infection of Calu-3 lung cells by SARS-CoV-2 (the coronavirus responsible for COVID-19) via inhibition of the serine protease TMPRSS2 required for viral spike protein priming. Group: Biochemicals. Alternative Names: 4- [ [4- [ (Aminoiminomethyl) amino] benzoyl] oxy] benzeneacetic Acid 2-(Dimethylamino)-2-oxoethyl Ester Methanesulfonate; FOY 305; FOY-S 980; Foipan. Grades: Highly Purified. CAS No. 59721-29-8. Pack Sizes: 5mg, 10mg, 25mg, 50mg, 100mg. Molecular Formula: C??H??N?O?S. US Biological Life Sciences. | Worldwide |
Our database is helping our users find suppliers everyday.
