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| Place of Origin: | China, Shanghai |
| Brand Name: | YAXINBIO |
| Certification: | NQA ISO 9001:2015 |
| Model Number: | REK08 |
| Minimum Order Quantity: | 100U |
|---|---|
| Price: | 65$/100u |
| Packaging Details: | ice packaging, carton |
| Delivery Time: | 5 days |
| Payment Terms: | T/T |
| Supply Ability: | 10,000ku per week |
| Product: | Recombinant Enterokinase | Manufacturer: | YaxinBio |
|---|---|---|---|
| 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 |
| Packaging: | 100U, 1KU ,10KU | RELATED PRODUCT: | Recombinant Carboxypeptidase B |
| High Light: | bovine enterokinase,recombinant enzymes |
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Recombinant Enterokinase, For Removing N-terminal Fusion Protein, Supplier
Recombinant Enterokinase
CAS:9017-74-8
EC:3.4.21.9
Source: bovine enterokinase, expressed in E. Coli
Description
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.
Advantages
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 sites.
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)
EK content: 1-2U
Temperature: 25℃
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.
Main Features
|
Source |
E.Coli |
|
M.W. |
25,850 Da |
|
Specific Activity |
One unit is defined as the amount of enzyme needed to cleave 0.5mg of fusion protein in 16 to 24 hours to get 95% completion at 25°C in 25mMTris-HCl, pH 8.0. Substrate: a special fusion protein. |
|
Storage Temperature |
-20°C or below. |
|
Stability |
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. |
Product Information
|
Product |
Activity |
Packaging |
Manufacturer |
|
Recombinant Enterokinase |
≥5 u/μl |
100u;500u;1ku; 10ku |
YaxinBio |
Unit Definition
One unit will produce 1.0 nanomole of trypsin from trypsinogen per min at pH 5.6 at 25 °C.
Application
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 from Sigma has been used to compare the specific activity with that of purified, recombinant bovine enterokinase (light chain) overexpressed inEscherichia coli.
Contact Person: Miss Eland
Tel: +8613482039151
