protein

Enterokinase Protein, Bovine (P.pastoris, His)

HY-P7341

10 μg;50 μg;100 μg

90;150;240 USD

Enterokinase Protein, Bovine (P.pastoris, His)

proteins

P. pastoris

10 μg;50 μg;100 μg

90;150;240 USD

384647039

Enterokinase Protein, Bovine (P.pastoris, His) is a single glycosylated polypeptide chain with His tag. Enterokinase plays a role of turning trypsinogen to its active form trypsin.

Bovine

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] .

rBoEnterokinase, His; Enteropeptidase; ENTK; PRSS7

Greater than 95% as determined by reducing SDS-PAGE.

Lyophilized after extensive dialysis against 20 mM Tris-HCl, pH 7.4, 200 mM NaCl, 2 mM CaCl 2 .

Room temperature in continental US; may vary elsewhere.