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| Product | Description | |
|---|---|---|
| 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. |  |
| Carboxypeptidase B from Porcine, Recombinant | Carboxypeptidase B (or peptidyl-L-lysine (-L-arginine) hydrolase) catalyzes the hydrolysis of the basic amino acids, lysine, arginine, and ornithine from the C-terminal position of polypeptides. It has been shown to be a single polypeptide of 34 kDa Da. Trypsin is capable of converting native enzyme to the active enzyme, carboxypeptidase B II in vitro. The optimum pH is found to be 9.0. The enzyme may be used for sequence analysis by successive cleavage of C-terminal basic amino acids. It can also be used as a serum marker for the diagnosis of acute pancreatitis. Carboxypeptidase b (ec 3.4.17.2), also well known as protaminase, pancreatic procarboxy-peptidase b (pcpb). mature chain. the secreted cpb zymogen is converted to enzymatically active cpb by limited proteolysis by trypsin. Group: Enzymes. Synonyms: carboxypeptidase B; protaminase; CPB1; pancreatic carboxypeptidase B; tissue carboxypeptidase B; peptidyl-L-lysine [L-arginine]hydrolase; EC 3.4.17.2; 9025-24-5. Enzyme Commission Number: EC 3.4.17.2. Purity: >90% (SDS-PAGE test). Mole weight: About 35kDa (SDS-PAGE detection). Activity: >180U/mg. Appearance: White powder, lyophilized. Storage: Redissolved in 20% glycerol, 4°C, store at -20°C for long-term preservation, Avoid multiple freeze-thaw cycles. Form: Freeze dried powder. Source: Porcine. carboxypeptidase B; protaminase; C. | |
| D-Val-Leu-Lys 4-nitroanilide dihydrochloride | D-Val-Leu-Lys 4-nitroanilide dihydrochloride stands as a crucial substrate to gauge the efficiency of trypsin-like serine proteases. Proteolysis event leads to the release of a yellow colored product, whose quantification can be done at 405 nm. Its utility can be seen in trypsin activity detection and the evaluation of agents restricting trypsin-like proteases. Consistent usage of this product aids in experimental design and the analysis of diverse protease substrates. Synonyms: (S)-6-Amino-2-((S)-2-((R)-2-amino-3-methylbutanamido)-4-methylpentanamido)-N-(4-nitrophenyl)hexanamide dihydrochloride; H-D-Val-Leu-Lys-pNA 2HCl. CAS No. 62354-43-2. Molecular formula: C23H40Cl2N6O5. Mole weight: 551.5. |  |
| L-Homoarginine hydrochloride | L-Homoarginine hydrochloride. Uses: L-homoarginine may be used to create non-natural proteins for studies of post-translational protein modifications. arginine residues are often located at the active centers of proteins and enzymes. replacing these arginines with homoarginine can elucidate protein function and structural requirements. l-homoarginine is used to study the mechanisms of nitric oxide production by cells via nitric oxide synthase(s). l-homoarginine is used as a selective mammalian alkaline phosphatase isoenzyme inhibitor. the substitution of homoarginine for arginine or lysine renders proteins resistant to proteolysis by trypsin. Additional or Alternative Names: (S)-2-Amino-6-guanidinohexanoic acid hydrochloride. Product Category: Amino Acids. CAS No. 1483-01-8. Molecular formula: H2NC(=NH)NH(CH2)4CH(NH2)CO2H · HCl. Mole weight: 224.69. Canonical SMILES: Cl[H].N[C@@H](CCCCNC(N)=N)C(O)=O. ECNumber: 216-045-6. Product ID: ACM1483018-1. Alfa Chemistry ISO 9001:2015 Certified. |  |
| 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 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 Factor XIa | Prepared from Human Factor XI using Human Factor Xlla. This Xlla was removed using a corn trypsin inhibitor column. Complete activation is observed by SDS-PAGE. Factor XI, through the contact factor pathway cascade, is activated to Factor XIa via Factor Xlla and High Molecular Weight Kininogen. During activation by Factor Xlla and HK, FXI undergoes proteolytic cleavage in which the Mr=80,000 chain reportedly is cleaved to a heavy and light chain with Mr of about 48,000 and 33,000. This Factor XIa is responsible for the activation of Factor IX to Factor IXa. Unlike other examples of activation of Vitamin K-dependent blood-clotting proteins, Factor XIa proteolysis of Factor IX does not require membrane surfaces. Group: Enzymes. Synonyms: Human Factor XIa; Factor XIa. Factor XIa. Mole weight: 160 kDa. Storage: < -60°C. Source: Human. Species: Human. Human Factor XIa; Factor XIa. Cat No: NATE-0886. | |
| Native Human 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. | |
| plasmin | Formed from plasminogen by proteolysis which results in multiple forms of the active plasmin. In peptidase family S1 (trypsin family). Group: Enzymes. Synonyms: fibrinase; fibrinolysin; actase; serum tryptase; thrombolysin. Enzyme Commission Number: EC 3.4.21.7. CAS No. 9001-90-5. PLG. 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-4161; plasmin; EC 3.4.21.7; 9001-90-5; fibrinase; fibrinolysin; actase; serum tryptase; thrombolysin. Cat No: EXWM-4161. | |
| TPCK-treated Trypsin | TPCK-treated Trypsin is a trypsin whose activity is inhibited by tosyl phenylalanyl chloromethyl ketone. TPCK-treated Trypsin reduces autolysis and nonspecific proteolysis during experiments, exhibits stability in storage and handling. TPCK-treated trypsin can be used in proteomics research[1]. TPCK-treated Trypsin renders the virus hemagglutinin active, which allows multicycle replication of the virus. TPCK-treated Trypsin can be used for the study of influenza virus[2]. Uses: Scientific research. Group: Signaling pathways. CAS No. 9002-7-7. Pack Sizes: 5 mg; 10 mg; 25 mg; 50 mg; 100 mg. Product ID: HY-129047C. |  |
| 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 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. | |
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