Enterokinase/Enteropeptidase, Bovine
Proteases play an important role in many diseases and biological processes including prenatal and postnatal development, reproduction, signal transduction, the immune response, various autoimmune and degenerative diseases, and cancer. Enteropeptidase is critical to converting trypsinogen(a zymogen) to trypsin, resulting in activating a number of pancreaticdigestive enzymes. Enteropeptidase, a serine protease (EC3.4.21.9), is structurally similar to the Chymotrypsin-clan of serine proteases. They are also an important research tool, frequently used in the analysis and production of proteins.
Full Name | Enterokinase/Enteropeptidase Light Chain Bovine Recombinant |
Synonyms | Enteropeptidase, EC 3.4.21.9, Enterokinase, Serine protease 7, ENTK, MGC133046. |
Source | Yeast |
Molecular Weight | Porcine enteropeptidase is a specific protease that cleaves after the lysine at its recognition site: Asp-Asp-Asp-Asp-Lys. The predicted MW of the protein based on its Amino Acid Sequence is 22 kDa, but the apparent MW obtained by SDS-PAGE is ≈ 40 kDa. |
Formulation | 2 U/ul, Sterile Liquid with 50mM Tris-HCl, pH 8.0, 0.5M NaCl and 50% glycerol. |
Stability | ≈ 1 year at -20°C and ≤ 1 week at room temperature. Avoid frequent freeze-thaw cycles. |
Biological Activity | One unit is defined as the amount of enzyme needed to cleave 50 µg of fusion protein in 16 hours to 95% completion at 22°C in a buffer containing 25 mM Tris-HCl, pH 8.0. |
Usage | FOR LABORATORY RESEARCH USE ONLY. Not intended for diagnostic or therapeutic purposes. |
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Product Code: EN121
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