ek 6

Expression system: HEK293 Cells
Length: 18-540, Partial
Activity: Not Tested

Expression system: HEK293 Cells
Length: 34-559, Extracellular Domain
Activity: Not Tested

Enterokinase (EK) is a duodenal protease involved in digestion by activating trypsinogen into trypsin, which in turn activates other pancreatic enzymes. EK specifically cleaves after the sequence Asp-Asp-Asp-Asp-Lys (DDDDK↓) and is inactive if a proline follows the site. Recombinant bovine enterokinase (rbEK) shows higher activity than EK from other species and is widely used in biochemical applications. It is a glycosylated single-chain protein of ~200 amino acids, tagged with C-terminal 6×His for Ni²⁺ affinity purification and easy removal after digestion. The purified rbEK has a molecular weight of ~40 kDa and is fully biologically active.

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.