Recombinant Bovine Enterokinase, His (P. pastoris-expressed) 是在 P. pastoris 中產(chǎn)生的具有 His 標(biāo)簽的糖基化肽鏈。Enterokinase 起著將胰蛋白酶原轉(zhuǎn)化為其活性形式胰蛋白酶的作用。
Synonyms
rBoEnterokinase, His; Enteropeptidase; ENTK; PRSS7
Species
BovineSource
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]. |
