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Recombinant Bovine Enterokinase / EK PDF Download

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SEKP01
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50ug  Inquring Price;    200ug  Inquring Price;    ≥1mg Bulk  Inquring Price

Manufactured By: Sino Biological Inc.

Synonym: EK, PRSS7

Protein Construction: A DNA sequence encoding the light chain (Ile 801-His 1035) of bovine Enterokinase(NP_776864)was expressed.

Source: Bovine

Expression Host: Human Cell

Purity: > 95%, as determined by SDS-PAGE and SEC-HPLC Analysis

Endotoxin: < 1.0 EU per 1 μg of the cytokine as determined by the LAL method

Stability: Samples are stable for up to twelve months from date of receipt -70C

Predicted N terminal: Ile 801

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.

SDS-PAGE:

Storage: Store at –70°C; Avoid repeated freeze-thaw cycles

Reconstitution: Follow the instructions on the vial. Centrifuge the vial at 4℃ before opening to recover the entire contents.

Protein 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.

References

1: Light, A. et al., 1989, Trends Biochem. Sci. 14: 110-112.
2: Kitamoto, Y. et al., 1994, Proc. Natl. Acad. Sci. 91: 7588-7592.
3: Lavallie, E.R. et al., 1993, J. Biol. Chem. 268: 23311-23317.
4: Collins-Racie, L.A. et al., 1995, Biotechnology. 13: 982-957.