|Place of Origin:||China, Shanghai|
|Certification:||NQA ISO 9001:2015|
|Minimum Order Quantity:||100U|
|Packaging Details:||ice packaging|
|Supply Ability:||1000ku per week|
|Specific Activity:||One Unit Is Defined As The Amount Of Enzyme Needed To Cleave 0.5mg Of Fusion Protein In 12 To16 Hours To Get 95% Completion At 25°C In A Buffer 25mMTris-HCl, PH 8.0.Substrate: A Special Fusion Protein.||Fusion Protein Concentration:||≥5 U/μl|
|Storage:||Store At -20°C After Delivery.||RELATED PRODUCT:||Recombinant Chymotrypsin|
Recombinant Bovine Enterokinase a protease can remove unwanted Protein Tags
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 (DDDDK). So, Enterokinase can remove N-terminal fusion protein or tags to get aim protein with native amino acids sequence.
Enterokinase is a member of the S1 peptidase family. In vivo, it is responsble for the proteolytic activation of trypsin from trypsinogen. Enterokinase is used for site specific cleavage of recombinant fusion proteins containing an accessible enterokinase recognition site for removal of affinity tags.
Enterokinase from bovine intestine has been used in a study to assess duodenase as a potential activator of cascade digestive proteases. Enterokinase from bovine intestine has also been used in a study to investigate an inhibitor of enteropeptidases and trypsin from the bovine duodenum.
The enzyme has been used to compare the specific activity with that of purified, recombinant bovine enterokinase (light chain) overexpressed inEscherichia coli.
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.
Main Features Advantages
One unit is defined as the amount of enzyme needed to cleave 0.5mg of fusion protein in 12 to 16 hours to get 95% completion at 25°C in 25mMTris-HCl, pH 8.0. Substrate: a special fusion protein.
-20°C or below.
Keep cool with blue ice during shipping. Remained stable at 25°C for one week without activity lost. No activity lost after 5 cycles of frozen-thawing.
Contact Person: Miss Eland
Source: E. Coli
M.W.: Theoretical MW: 25,850 Da;The apparent MW on SDS-PAGE: about 27,000 Da
Storage: Store at -20°C after delivery.
Specific activity: One unit is defined as the amount of enzyme needed to cleave 0.5mg of fusion protein in 12 to16 hours to get 95% completion at 25°C in a buffer 25mMTris-HCl, pH 8.0.Substrate: a special fusion protein.