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.

规格	价格/CNY		货期	数量
100 U	￥ 580	5日内发货

规格

价格/CNY

货期

数量

100 U

￥ 580

5日内发货

生物活性

One unit is defined as the amount of enzyme needed to cleave 50μg fusion protein in 16 hours at 20℃ in a buffer containing 20 mM Tris-HCl, 50 mM NaCl, and 2 mM CaCl2>, pH 7.4.

产品描述

种属	Bovine
表达系统	P. pastoris (Yeast)
标签	Tag Free
别名	EK, Enterokinase, PRSS7, Enteropeptidase, EC 3.4.21.9, Serine protease 7, ENTK, MGC133046.
蛋白构建	light chain (Ile 801-His 1035) of bovine Enterokinase (NP_776864)
蛋白纯度	> 95%, as determined by SDS-PAGE and SEC-HPLC Analysis
分子量	26.1kDa (predicted)

内毒素	< 1.0 EU/μg of the cytokine as determined by the LAL method
复溶方法	Resuspend the enzyme powder with sterile water. Keep reconstituted enzyme at -20℃ in aliquots.
存储	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.
运输方式	In general, Lyophilized powders are shipping with blue ice.
研究背景	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.