Enterokinase Protein, Bovine, Recombinant (Animal-Free, His)

5 U/μl Unit definition: One unit is defined as the amount of enzyme sufficient to cleave 50 μg of control fusion protein (~24 kDa) in 16 hours to 95% completion at 22 °C in a buffer containing 20 mM Tris-HCl, 50 mM NaCl, 2 mM CaCl 2 , pH 7.4.

Enterokinase (EK) is a serine protease produced in the duodenum and involved in mammalian digestion. It activates trypsinogen to trypsin, thereby indirectly initiating the activation of pancreatic digestive enzymes. EK specifically cleaves after the recognition sequence Asp-Asp-Asp-Asp-Lys, but is inactive if a proline follows the cleavage site. This recombinant bovine enterokinase is the light chain catalytic subunit, comprising a single glycosylated polypeptide chain corresponding to residues Ile801–His1035 of the native protein (Accession # P98072). Expressed in Pichia pastoris under animal-free conditions, the enzyme is highly active and suitable for applications in drug and vaccine development. A C-terminal 6×His tag is included to allow efficient removal by Ni²⁺ affinity chromatography following cleavage reactions.

Bovine

PRSS7,ENTK,Enteropeptidase

≥ 95% as determined by SDS-PAGE

Upon receiving, the product remains stable for up to 6 months at -20 °C. This product is stable for up to 1 week at 37 °C. Avoid repeated freeze-thaw cycles by making single-use aliquots before the solution is stored at -20 °C.

Enterokinase (EK) is a serine protease produced in the duodenum and involved in mammalian digestion. It activates trypsinogen to trypsin, thereby indirectly initiating the activation of pancreatic digestive enzymes. EK specifically cleaves after the recognition sequence Asp-Asp-Asp-Asp-Lys, but is inactive if a proline follows the cleavage site.