Recombinant Human Enteropeptidase/Enterokinase, Light Chain - rHuEK



Data Sheet
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Recombinant Human Enteropeptidase/Enterokinase, Light Chain - rHuEK

Description: Human enteropeptidase is a specific protease that cleaves after the sequence Asp-Asp-Aps-Aps-Lys. The light chain of enteropeptidase has full enzymatic activity. No other protease activity was detected. Human enteropeptidase binds specifically to STI-agarose.
Source: Escherichia Coli.
Physical Appearance: Liquid.
Formulation : 50 mM Tris-HCl, pH 8.0, 0.5M NaCl and 50% glycerol.
Stability : One year when stored at -20°C, three weeks at room temperature.
Unit Defenition: One unit of human enteropeptidase will cleave 2 mg of thioredoxin/human EGF fusion protein with the Asp-Asp-Aps-Aps-Lys sequence at the joining point in 22 hours at 4°C, in 16 hours at 25°C or in 8 hours at 37°C.
Assay Conditions: 50 mM TRIS-HCl or sodium phosphate (pH 8.0) at 25°C with or without CaCl2. The enzyme is active at a pH range of 6.0-9.0.
Dilution buffers: 50 mM Tris-Hcl, pH 8.0, 500 mM NaCl and 50% glycerol.
Endotoxin: Less than 0.1 ng/µg (IEU/µg) of enteropeptidase.