Enterokinase/EK Protein, Bovine, Recombinant

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.

Pack Size	Availability	Price/USD	Quantity
100 U	5 days	$ 91.00

Pack Size

Availability

Price/USD

Quantity

100 U

5 days

$ 91.00

Description

Species	Bovine
Expression System	P. pastoris
Tag	Tag Free
Synonyms	EK, Enterokinase, PRSS7, Enteropeptidase, EC 3.4.21.9, Serine protease 7, ENTK, MGC133046.
Construction	A DNA sequence encoding the light chain (Ile 801-His 1035) of bovine Enterokinase (NP_776864) was expressed.
Protein Purity	> 95%, as determined by SDS-PAGE and SEC-HPLC Analysis
Molecular Weight	Approxiamtely 26.1kDa

Endotoxin	< 1.0 EU per 1 μg of the cytokine as determined by the LAL method
Reconstitution	Resuspend the enzyme powder with sterile water. Keep reconstituted enzyme at -20℃ in aliquots.
Stability & Storage	Samples are stable for up to twelve months from date of receipt -70℃. The liquid or lyophilized enzyme is stable for at least 21d when stored at 37 ℃ (or room temperature).
Shipping	Shipped at room temperature.
Research Background	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.