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| Product | Description | |
|---|---|---|
| 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. |  |
| 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. | |
| Enterokinase, Ultrapure, Porcine, Cleavage Buffer | Enterokinase, Ultrapure, Porcine, Cleavage Buffer. Group: Molecular Biology. Grades: Molecular Biology Grade. CAS No. 9014-74-8. Pack Sizes: 5x1Vial. US Biological Life Sciences. |  Worldwide |
| Enterokinase, Ultrapure, Porcine, Cleavage Control | Enterokinase, Ultrapure, Porcine, Cleavage Control. Group: Molecular Biology. Grades: Molecular Biology Grade. CAS No. 9014-74-8. Pack Sizes: 5x10ug. US Biological Life Sciences. | Worldwide |
| Enterokinase, Ultrapure, Porcine (Enteropeptidase) | Enterokinase, Ultrapure, Porcine (Enteropeptidase). Group: Molecular Biology. Alternative Names: EC=3.4.21.9. Grades: Molecular Biology Grade. CAS No. 9014-74-8. Pack Sizes: 5x100U. US Biological Life Sciences. | Worldwide |
| Enterokinase, Ultrapure, Porcine, Storage Buffer | Enterokinase, Ultrapure, Porcine, Storage Buffer. Group: Molecular Biology. Grades: Molecular Biology Grade. CAS No. 9014-74-8. Pack Sizes: 5x1Vial. US Biological Life Sciences. | Worldwide |
| 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. | |
| Native Porcine 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 from porcine intestine has been used in a study to report a new experimental model of the anomalous pancreatico-biliary junction. enterokinase from porcine intestine has also ...peptide. the enzyme from creative enzymes has been used for the activation of trypsinogen in order to measure the activity of trypsin in hog pancreas. the study showed that antimicrobial treatment reduces intestinal microflora and improves protein digestive capacity without changes in villous structure of weanling pigs. 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. Activity: Type I, > 20 units/mg protein. Storage: -20°C. Form: salt-free, lyophilized powder. Source: Porcine intestine. Species: Porcine. enterokinase; enteropeptidase; EC 3.4.21.9; 9014-74-8. Cat No: NATE-0225. | |
| 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. |  |
| enteropeptidase | Is not inhibited by protein inhibitors of trypsin. In peptidase family S1 (trypsin family). Group: Enzymes. Synonyms: enterokinase. Enzyme Commission Number: EC 3.4.21.9. CAS No. 9014-74-8. Enterokinase. 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-4181; enteropeptidase; EC 3.4.21.9; 9014-74-8; enterokinase. Cat No: EXWM-4181. | |
| FLAG peptide | FLAG peptide, an eight amino acids peptide with an enterokinase-cleavage site, is a frequently applied hydrophilic and immunogenic fusion tag which was specifically designed to facilitate rapid purification by immunoaffinity chromatography. Synonyms: DYKDDDDK Peptide; H-Asp-Tyr-Lys-Asp-Asp-Asp-Asp-Lys-OH; L-alpha-aspartyl-L-tyrosyl-L-lysyl-L-alpha-aspartyl-L-alpha-aspartyl-L-alpha-aspartyl-L-alpha-aspartyl-L-lysine; FLAG tag Peptide; FRAG Epitope; FLAG Epitope Peptide. Grades: >95%. CAS No. 98849-88-8. Molecular formula: C41H60N10O20. Mole weight: 1012.97. |  |
| FLAG peptide | FLAG peptide is a multifunctional fusion tag for the purification of recombinant proteins. FLAG peptide maintances the natural folding of its fusing proteins. FLAG peptide can be removed by enterokinase, and eluted under non-denaturing conditions [1]. Uses: Scientific research. Group: Peptides. CAS No. 98849-88-8. Pack Sizes: 5 mg; 10 mg; 25 mg; 50 mg; 100 mg. Product ID: HY-P0223. | |
| FLAG peptide (TFA salt) | FLAG peptide, an eight amino acids peptide with an enterokinase-cleavage site, is a frequently applied hydrophilic and immunogenic fusion tag which was specifically designed to facilitate rapid purification by immunoaffinity chromatography. Synonyms: H-Asp-Tyr-Lys-Asp-Asp-Asp-Asp-Lys-OH.TFA; L-alpha-aspartyl-L-tyrosyl-L-lysyl-L-alpha-aspartyl-L-alpha-aspartyl-L-alpha-aspartyl-L-alpha-aspartyl-L-lysine trifluoroacetate salt; FLAG peptide TFA salt; DYKDDDDK Peptide TFA salt. Molecular formula: C41H60N10O20 (free base). Mole weight: 1012.97 (free base). | |
| Gly-Asp-Asp-Asp-Asp-Lys--naphthylamide | It is a specific substrate for the determination of enteropeptidase (enterokinase), also used in histochemistry. Synonyms: H-Gly-Asp-Asp-Asp-Asp-Lys-bNA; H-Gly-Asp-Asp-Asp-Asp-Lys-βNA. Grades: 98%. CAS No. 70023-02-8. Molecular formula: C34H44N8O14. Mole weight: 788.76. | |
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