5000IU

Enterokinase (EK) is an enzyme produced by cells of the duodenum and involved in human digestion. It plays a role of turning trypsinogen to its active form trypsin, and indirectly activates the pancreatic digestive enzymes. 
Enterokinase is a specific protease that cleaves after a lysine preceded by four aspartic acids: Asp-Asp-Asp-Asp-Lys. 
Enterokinase will not work if the recognition site is followed by a proline. rbEK with 6 × His-tag binds with Ni²⁺ affinity chromatography and was designed for removing from digestion system.

Recombinant Bovine Enterokinase (rbEK) as the light chain is a single glycosylated polypeptide chain containing 200 amino acids. A fully biologically active molecule, rbEK has a molecular mass of 22.7 kDa and is obtained by proprietary chromatographic techniques at GenScript.

PreScission Protease is a fusion protein of glutathione S-transferase (GST) and human rhinovirus (HRV) type 14 3C protease. The optimum recognition site for this enzyme is the sequence Leu-Glu-Val-Leu-Phe-Gln/Gly-Pro (LEVLFQ/GP) and cleavage occurs between the Gln and Gly-Pro residues. Substrate recognition and cleavage are likely to be dependent not only upon primary structural signals, but also upon the secondary and tertiary structures of the fusion protein as well.