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Recombinant Bovine Enterokinase, His (P.pastoris-expressed)
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| 性状 | Recombinant Bovine Enterokinase, His (P. pastoris-expressed) 是在 P. pastoris 中产生的具有 His 标签的糖基化肽链。Enterokinase 起着将胰蛋白酶原转化为其活性形式胰蛋白酶的作用。
Synonyms rBoEnterokinase, His; Enteropeptidase; ENTK; PRSS7 Species Bovine Source P. pastoris Molecular Weight Approximately 40 kDa AA Sequence Biological Activity 100 IU/μg Appearance Lyophilized powder. Formulation Lyophilized after extensive dialysis against 20 mM Tris-HCl, pH 7.4, 200 mM NaCl, 2 mM CaCl2. Endotoxin Level <0.2 EU/μg, determined by LAL method. Reconstitution Reconstitute the lyophilized recombinant Bovine Enterokinase, His (P.pastoris-expressed) (rBoEnterokinase, His) to 1 mg/mL using sterile deionied water, then dilute in sterile EK Storage Buffer (20 mM Tris-HCl, pH 7.4, 200 mM NaCl, 2 mM CaCl2). Storage & Stability Lyophilized recombinant Bovine Enterokinase, His (P.pastoris-expressed) (rBoEnterokinase, His) is stored at -20°C. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer. It is recommended to freeze aliquots at -20°C or -80°C for extended storage. Shipping Room temperature in continental US; may vary elsewhere. Background Bovine enterokinase is a serine protease and functions as the physiological activator of trypsinogen. The amino acid composition shows that the light chain has nine half-cystine residues and that one half-cystine was in a disulfide link between the light and heavy subunits. The sequence has homologies with other serine proteases containing one or two chains. The homologies suggest that the catalytic subunit has the same three-dimensional structure and, therefore, the same mechanism of enzymatic action as pancreatic chymotrypsin, trypsin, and elastase. The presence of the conserved amino-terminal activation peptide sequence (IVGG) shows that enterokinase must have a zymogen precursor and that the two-chain enzyme arises from limited proteolysis during posttranslational processing[1]. |
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