Bovine Enterokinase (rbEK)
Enterokinase (EK) is an enzyme produced by cells of the duodenum and involved in human digestion.
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Introduction
Human Trypsin 1, encoded by the PRSS1 gene, is also known as cationic trypsinogen. It contains a signal peptide (residues 1‑15), a pro region (residues 16‑23), and a mature chain (residues 24‑247). Trypsin is part of the serine protease family. Trypsin cleaves lysine and arginine at the C-terminal side of the peptide. Trypsin optimum pH is pH-7 to 9. The enzyme is inhibited by serine protease inhibitors, e.g. PMSF, and by metal chelating agents, e.g. EDTA.
Product Description
Recombinant Human Trypsin-1 is a genetically engineered protein expressed in E. coli and purified by standard chromatography techniques. Recombinant Human Trypsin-1 is free from any animal and human sources. There are no contaminating enzyme activities such as carboxypeptidase A and chymotrypsin. No protease inhibitors such as PMSF are contained in the preparation.
Source
Human trypsin-1, expressed in E. coli, with a C-terminal 6-His tag
Purity
>95% as determined by SDS-PAGE
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Unit Definition: One USP unit of trypsin activity will produce a Delta A253 of 0.003 per minute in a reaction volume of 3.0ml at pH7.6 and 25℃, with BAEE as a substrate (1cm light path).
Specific activity: ≥ 2500 USP U/mg
Storage: Store at -20°C. Avoid multiple freeze-thaw cycles.
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Enterokinase (EK) is an enzyme produced by cells of the duodenum and involved in human digestion.
Enzyme for digesting proteins in biological samples. Form: solution, concentration 20 mg/ml, activity ≥ 30 U/mg.
Human Trypsin 1, encoded by the PRSS1 gene, is also known as cationic trypsinogen. It contains a signal peptide (residues 1‑15), a pro region (residues 16‑23), and a mature chain (residues 24‑247).
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