| Cat. No. : |
PRSS7-286B |
| Description : |
Enterokinase is a member of the trypsin family of serine proteases. The precursor protein is cleaved into two chains which then forms a heterodimer linked by a disulfide bond. The heavy chain anchors enterokinase in the intestinal brush border membrane and the light chain is the catalytic subunit, which initiates conversion activation of a subset of pancreatic proteolytic proenzymes. Enterokinase is the physiological activator of trypsinogen and has a specificity for the sequence (Asp)4-Lys-Ile. The mature trypsin in turn activates other proenzymes including chymotrypsinogen, procarboxypeptidases, and proelastases. In addition, Enterokinase is a tool protease widely utilized in the cleavage of recombinant fusion proteins. |
| Molecular Mass : |
The recombinant bovine Enterokinase consists of 234 amino acids and has a calculated molecular mass of 26.1kDa. As a result of glycosylation, the recombinant protein migrates as an approximately 45kDa protein in SDS-PAGE under reducing conditions. |
| Source : |
Human Cells (HEK293). |
| Predicted N Terminal : |
Ile 801. |
| Purity : |
> 95%, as determined by SDS-PAGE and SEC-HPLC Analysis. |
| Stability : |
Samples are stable for up to twelve months from date of receipt -70℃. |
| Endotoxin : |
< 1.0 EU per 1μg cytokine as determined by the LAL method. |
| Reconstitution : |
Follow the instructions on the vial. Centrifuge the vial at 4℃ before opening to recover the entire contents. |
| Storage : |
Store at –70°C; Avoid repeated freeze-thaw cycles. |
