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Recombinant Enterokinase, For Removing N-terminal Fusion Protein, Supplier

Recombinant Enterokinase, For Removing N-terminal Fusion Protein, Supplier

  • Recombinant Enterokinase, For Removing N-terminal Fusion Protein, Supplier
  • Recombinant Enterokinase, For Removing N-terminal Fusion Protein, Supplier
  • Recombinant Enterokinase, For Removing N-terminal Fusion Protein, Supplier
  • Recombinant Enterokinase, For Removing N-terminal Fusion Protein, Supplier
  • Recombinant Enterokinase, For Removing N-terminal Fusion Protein, Supplier
Recombinant Enterokinase, For Removing N-terminal Fusion Protein, Supplier
Product Details:
Place of Origin: China, Shanghai
Brand Name: YAXINBIO
Certification: NQA ISO 9001:2015
Model Number: REK08
Payment & Shipping Terms:
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
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Detailed Product Description
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

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.

Recombinant Enterokinase, For Removing N-terminal Fusion Protein, Supplier 0

 

Contact Details
Shanghai Yaxin Biotechnology Co.,Ltd.

Contact Person: Miss Eland

Tel: +8613482039151

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