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| Product | Description | |
|---|---|---|
| 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 |  |
| 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; | |
| Enterokinase from bovine intestine, Recombinant | Enteropeptidase (also called enterokinase) is an enzyme produced by cells of the duodenum and involved in human and animal digestion. It is secreted from intestinal glands (the crypts of Lieberkühn) following the entry of ingested food passing from the stomach. Enteropeptidase converts trypsinogen (a zymogen) into its active form trypsin, resulting in the subsequent activation of pancreatic digestive enzymes. Absence of enteropeptidase results in intestinal digestion impairment. Applications: Enterokinase is a member of the s1 peptidase family. in vivo, it is responsble for the proteolytic activation of trypsin from trypsinogen. enterokinase is used for site specific ...yme from creative enzymes has been used to compare the specific activity with that of purified, recombinant bovine enterokinase (light chain) overexpressed in escherichia coli. Group: Enzymes. Synonyms: enterokinase; enteropeptidase; EC 3.4.21.9; 9014-74-8. Enzyme Commission Number: EC 3.4.21.9. CAS No. 9014-74-8. Enterokinase. Mole weight: 28 kDa light chain form. Activity: Type I, > 20 units/mg protein. Storage: -20°C. Form: Type I, supplied as a solution in 20 mM Tris-HCl, 200 mM NaCl, and 50% glycerol; Type II, white powder. Source: E. coli. Species: Bovine intestine. enterokinase; enteropeptidase; EC 3.4.21.9; 9014-74-8. Pack: vial of ~0.2 unit. Cat No: NATE-0226. | |
| Native Bovine Enterokinase | Enteropeptidase (also called enterokinase) is an enzyme produced by cells of the duodenum and involved in human and animal digestion. It is secreted from intestinal glands (the crypts of Lieberkühn) following the entry of ingested food passing from the stomach. Enteropeptidase converts trypsinogen (a zymogen) into its active form trypsin, resulting in the subsequent activation of pancreatic digestive enzymes. Absence of enteropeptidase results in intestinal digestion impairment. Enterokinase is a highly specific serine protease that is used for the removal of the flag peptide from n-terminal and met-n-terminal fusion proteins. it does not remove the c-terminal flag. Applications...ytic activation of trypsin from trypsinogen. enterokinase is used for site specific cleavage of recombinant fusion proteins containing an accessible enterokinase recognition site for removal of affinity tags. removes flag peptide from n-terminal and met-n-terminal fusion proteins. Group: Enzymes. Synonyms: enterokinase; enteropeptidase; EC 3.4.21.9; 9014-74-8. Enzyme Commission Number: EC 3.4.21.9. CAS No. 9014-74-8. Enterokinase. Mole weight: 150 kDa (consisting of 115kDa and 35kDa subunits.). Activity: Type I, > 20 units/mg protein. Storage: -20°C. Form: powder. Source: Bovine intestine. Species: Bovine. enterokinase; enteropeptidase; EC 3.4.21.9; 9014-74-8. Cat No: NATE-0224. | |
| Native Calf Enterokinase | Enteropeptidase (also called enterokinase) is an enzyme produced by cells of the duodenum and involved in human and animal digestion. It is secreted from intestinal glands (the crypts of Lieberkühn) following the entry of ingested food passing from the stomach. Enteropeptidase converts trypsinogen (a zymogen) into its active form trypsin, resulting in the subsequent activation of pancreatic digestive enzymes. Absence of enteropeptidase results in intestinal digestion impairment. Applications: Enterokinase is used for the cleavage of fusion proteins at definite cleavage sites. for the processing of recombinant proteins, the desired protein is fused with enterokinase recognition sequence. after purification of the entire fusion protein, the protein or peptide is released by incubation with enterokinase. Group: Enzymes. Synonyms: enterokinase; enteropeptidase; EC 3.4.21.9; restriction protease enterokinase. Enzyme Commission Number: EC 3.4.21.9. CAS No. 9014-74-8. Enterokinase. Mole weight: 150 kDa. Storage: Store at 2-8°C. Form: Lyophilized. Source: Calf intestine. Species: Calf. enterokinase; enteropeptidase; EC 3.4.21.9; restriction protease enterokinase. Cat No: NATE-0872. | |
| Recombinant enterokinase | Recombinant enterokinase (rEK) is a serine protease and functions as the physiological activator of trypsinogen. Recombinant enterokinase plays a role of turning trypsinogen to its active form trypsin [1]. Uses: Scientific research. Group: Signaling pathways. Alternative Names: rEK. CAS No. 9014-74-8. Pack Sizes: 100 U. Product ID: HY-E70202. |  |
| 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. | |
| 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. | |
| Carboxypeptidase B from Porcine, Recombinant | Carboxypeptidase B (or peptidyl-L-lysine (-L-arginine) hydrolase) catalyzes the hydrolysis of the basic amino acids, lysine, arginine, and ornithine from the C-terminal position of polypeptides. It has been shown to be a single polypeptide of 34 kDa Da. Trypsin is capable of converting native enzyme to the active enzyme, carboxypeptidase B II in vitro. The optimum pH is found to be 9.0. The enzyme may be used for sequence analysis by successive cleavage of C-terminal basic amino acids. It can also be used as a serum marker for the diagnosis of acute pancreatitis. Carboxypeptidase b (ec 3.4.17.2), also well known as protaminase, pancreatic procarboxy-peptidase b (pcpb), ... mature chain. the secreted cpb zymogen is converted to enzymatically active cpb by limited proteolysis by trypsin. Group: Enzymes. Synonyms: carboxypeptidase B; protaminase; CPB1; pancreatic carboxypeptidase B; tissue carboxypeptidase B; peptidyl-L-lysine [L-arginine]hydrolase; EC 3.4.17.2; 9025-24-5. Enzyme Commission Number: EC 3.4.17.2. Purity: >90% (SDS-PAGE test). Mole weight: About 35kDa (SDS-PAGE detection). Activity: >180U/mg. Appearance: White powder, lyophilized. Storage: Redissolved in 20% glycerol, 4°C, store at -20°C for long-term preservation, Avoid multiple freeze-thaw cycles. Form: Freeze dried powder. Source: Porcine. carboxypeptidase B; protaminase; C | |
| Carboxypeptidase-B rat, 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. Caspase 3 is synthesized as a 32 kda proenzyme. the active enzyme is a heterodimer of two large (17 kda) subunit...sponsible for rapidly metabolizing the c5a protein into c5a des-arg, with one less amino acid. 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. CAS No. 9025-24-5. CPB1. Activity: 50-55 units/mg protein carboxypeptidase B. Storage: -20°C. Form: Lyophilized from 20 mM Tris, pH 8.0 + 50 mM NaCl. Source: E. coli. Species: Rat. carboxypeptidase B; protaminase; CPB1; pancreatic carboxypeptidase B; tissue carboxypeptidase B; peptidyl-L-lysine [L-arginine]hydrolase; EC 3.4.17.2; 9025-24-5. Cat No: NATE-0153. | |
| Enterokinase from Human, Recombinant | Enteropeptidase (also called enterokinase) is an enzyme produced by cells of the duodenum and involved in human and animal digestion. It is secreted from intestinal glands (the crypts of Lieberkühn) following the entry of ingested food passing from the stomach. Enteropeptidase converts trypsinogen (a zymogen) into its active form trypsin, resulting in the subsequent activation of pancreatic digestive enzymes. Absence of enteropeptidase results in intestinal digestion impairment. > 90% (sds-page), > 90% (hplc), cell culture tested. Group: Enzymes. Synonyms: enterokinase; enteropeptidase; EC 3.4.21.9; 9014-74-8. Enzyme Commission Number: EC 3.4.21.9. CAS No. 9014-74-8. Enterokinase. Mole weight: 108.7 kDa. Activity: Type I, > 20 units/mg protein. Form: Lyophilized from 10 mM Sodium Phosphate, pH 7.5 + 1 mM Calcium Chloride. Source: CHO cells. Species: Human. enterokinase; enteropeptidase; EC 3.4.21.9; 9014-74-8. Cat No: NATE-0227. | |
| Granzyme A from Human, Recombinant (carrier-free) | Granzyme A is a serine protease belonging to the granzyme family and is expressed exclusively by cytotoxic T cells (CTL) and NK cells. Most circulating CD56+CD8- NK cells, and approximately half of circulating CD8+ T cells, coexpress both granzymes A and B. Group: Enzymes. Synonyms: Hanukah factor serine protease (HFSP); Cytolytic T cell-and natural killer cell-specific trypsin-like serine protease; Cytotoxic T-lymphocyte-associated serine esterase 3; CTLA3; Granzyme A; Granzyme. Enzyme Commission Number: EC 3.4.21.78. CAS No. 143180-73-8. Purity: >90%, as determined by Coomassie stained SDS-PAGE. Granzyme A. Mole weight: 55 kD in non-reducing conditions by SDS-PAGE. Activity: >5,000 pmol/min/ug. Storage: Unopened vial can be stored at -70°C for six months. For maximum results, quick spin vial prior to opening. Avoid repeated freeze/thaw cycles. Form: 0.22 um filtered protein solution is in 20 mM Tris, 150 mM NaCl, pH 7.5. Source: 293E cell line. Species: Human. Hanukah factor serine protease (HFSP); Cytolytic T cell-and natural killer cell-specific trypsin-like serine protease; Cytotoxic T-lymphocyte-associated serine esterase 3; CTLA3; Granzyme A; Granzyme. Cat No: NATE-1934. | |
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