Enterokinase, GMP Grade

Enterokinase (light chain), highly specifically recognizes the Asp-Asp-Asp-Asp-Lys sequence and hydrolyzes the polypeptides at the C-terminus of Lys. It can convert trypsinogen to trypsin in vivo, and fusion proteins with this recognition sequence can also be cleaved. This product, enterokinase, produced by recombinant yeast secretion and expression system, is of a high purity, high bio-activity, and an excellent stability, which allows a wide range of working condition (4-45°C, pH 4.5-9.5) even keeps a part of bio-activity in the presence of various detergent and denatured agents.
This product is from a large scale GMP leveled recombinant enterokinase production via Pichia pastoris expression. Applying pharmaceutical leveled adjuvant and material for production, strictly controlling host protein residues, nucleic acid residues and other impurities, we guarantee manufacture and quality control practice complying to GMP regulation, as well as all the materials traceable.

Appearance: Clear and transparent solution
Bacterial Endotoxin Residues: < 10EU/ml
Colony Count aerobic bacteria: < 10³cfu/ml, yeasts and moulds: < 10²cfu/ml
Host-cell Protein Residues: ≤ 50ppm
Exogenous DNA Residues: ≤ 100pg/mg
Mycoplasma: Negative
Heavy Metal Residues: ≤ 10ppm
Activity Definition: At 37°C, within 16 hours, the amount of enzyme required that will degrade 95% of 0.5 mg Thioredoxin-NP-27, the substrate, turning to NP-27 is defined as one unit of enzyme activity

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