| 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.
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