Bovine Light Chain Enterokinase, Recombinant Enterokinase,
Expressed in E.coli
Source: bovine enterokinase, expressed in E. Coli
YaxinBio Enterokinase is a kind of highly purified recombinant
bovine enterokinase. The enzyme has been extensively purified and
there are no traces of other contaminating proteases. Enterokinase
specifically hydrolyzes peptide bond at the carboxyl side of lysine
residue preceded by four aspartic acids: Asp-Asp-Asp-Asp-Lys
(D-D-D-D-K). So, Enterokinase can remove N-terminal fusion protein
or tags to get aim protein with native amino acids sequence.
Recombinant Bovine Enterokinase produced in E.coli is a single glycosylated polypeptide chain containing 235
amino acids and having a molecular mass of approximately28 kDa.
1) Protease that cleaves specifically after a lysine preceded by
four aspartic acids: Asp-Asp-Asp-Asp-Lys (D-D-D-D-K)
2) No any other contaminated proteases, no non-specific cutting
Recommend Usage Condition
|Cutting condition||given an example: 25mM Tris-HCl 8.0|
|Fusion protein concentration||0.1-1mg/ml (total protein content: 0.5-1.0mg)|
|Time||overnight or 16h-24h for digestion|
Common Components Influence the Action of Enterokinase
＞200mM imidazole or ＞200mM NaCl or ＞5%glycerin, the reaction may be
effected.The following suggestions are given:
1) To receive the optimum result, please dialyze the sample to 25
mMTris-HCl, pH 8.0.
2) If the dialysis is inconvenient, please dilute the sample to
＜100mM imidazole, ＜50mMNaCl, ＜5% glycerin, and the proportion of
fusion protein and EK may not be changed (1U:0.5mg fusion protein).
3) If there are one or more components in samples, and cannot be
removed, suggest to increase the content of EK in reaction system
or extend the reaction time.