| Cat. No. : |
PRSS7-02B |
| Description : |
Enterokinase is a serine proteinase in the duodenum that plays a critical role in mammalian digestion. It is the physiological activator of pancreatic trypsinogen. It converts trypsinogen into its active form trypsin, by cleaving its aminoterminal hexapeptide Val(Asp)4-Lys. More recently, the enterokinase has been shown to have a broad utility in cleaving fusion proteins produced in Escherichia coli. The enzyme is particularly suitable for this role because of its high degree of specificity, its tolerance to a wide range of reaction conditions, and the fact that its recognition sequence lies entirely on the aminoterminal side of the scissile bond. This enzymatic activity allows release of carboxyl-terminal fusion partners from fusion proteins without leaving unwanted amino acid residues on their amino termini. |
| Unit Definition : |
One unit is defined as the amount of enzyme needed to cleave 50 ug of fusion protein in 16 hours to 95% completion at 25°C in a buffer containing 25 mM Tris-HCl, pH 7.6, 50 mM NaCl, and 2 mM CaCl2. |
| Formulation : |
50 mM Tris-HCl, pH 8.0, 0.5M NaCl and 50% glycerol. |
| Physical Appearance : |
Sterile liquid |
| Endotoxin : |
Less than 1EU/mg of rbEK as determined by LAL method. |
| Storage : |
One year when stored at -20°C. Avoid repeated freeze/thaw cycles. |
| Enzyme Commission Number : |
EC3.4.21.9 |
| Reaction : |
The reactioncatalysedby Enteropeptidase: trypsinogen → trypsin + octapeptide Enteropeptidase cleaves after Lysine if the Lys is preceded by four Asp and not followed by a Pro. |
