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.

Enterokinase/EK Protein, Bovine, Recombinant

パッケージサイズ	在庫状況	単価(税別)
100 U	約5 days	￥ 21,000

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説明

Species	Bovine
Expression Host	P. pastoris (Yeast)
Tag	Tag Free
別名	EK, Enterokinase, PRSS7, Enteropeptidase, EC 3.4.21.9, Serine protease 7, ENTK, MGC133046.
Construction	light chain (Ile 801-His 1035) of bovine Enterokinase (NP_776864)
Protein Purity	> 95%, as determined by SDS-PAGE and SEC-HPLC Analysis
分子量	26.1kDa (predicted)

Endotoxin	< 1.0 EU/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	It is recommended to store recombinant proteins at -20°C to -80°C for future use. Lyophilized powders can be stably stored for over 12 months, while liquid products can be stored for 6-12 months at-80℃. For reconstituted proteinsolutions, the solution can be stored at -20°c to -80'c for at least 3 months. Please avoid multiple freeze-thaw cycles and store products in aliquots.
Shipping	In general, Lyophilized powders are shipping with blue ice.
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.

参考文献

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.

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Enterokinase/EK Protein, Bovine, Recombinant

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