|Place of Origin:||China, Shanghai|
|Certification:||NSF ISO 9001:2015|
|Minimum Order Quantity:||100U|
|Packaging Details:||ice packaging, carton|
|Delivery Time:||6 days|
|Supply Ability:||1000ku per week|
|Packaging:||100U, 1KU Or Bulk||Fusion Protein Concentration:||≥5 U/μl|
|Storage:||Store At -20°C After Delivery.||RELATED PRODUCT:||Sequencing Grade Trypsin|
Recombinant Enterokinase, Genetically Engineered Protein, High Specificity and High Purity
Storage temperature: -20°C or below
Source: Recombinant enterokinase is a genetically engineered protein expressed in E.coli
Protein Sequence:The amino acid sequence of recombinant enterokinase is identical to bovine enterokinase light chain
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.
1) Protease that cleaves specifically after a lysine preceded by four aspartic acids: Asp-Asp-Asp-
2) No any other contaminated proteases, no non-specific cutting sites.
Recommend Usage Condition:
|Cutting condition||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|
Enterokinase is a membrane bound serine protease that specifically and rapidly converts trypsinogen
to trypsin, thereby, triggering the conversion of other zymogens to active enzymes. It has a molecular mass of approximately 150 kDa. The enzyme is a heterodimer, wherein, the light and the heavy chains
are linked by two disulfide bridges. Native enterokinase is composed of an 800 amino acid heavy
chain and a 235 amino acid light chain. It is a glycoprotein containing 35% carbohydrate. The polypeptide chain of trypsinogen is hydrolyzed only after an -(Asp)4-Lys- sequence. This cleavage site is incorporated into the FLAG tag.
supplied as a solution in 20 mM Tris-HCl, 200 mM NaCl, and 50% glycerol
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.
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.