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Product Details
Product Details
Enterokinase is expressed from Pichia Pastoris, it contained the light chain of the bovine enterokinase. Enterokinase is a specific protease that cleaves after lysine at its cleavage site Asp-Asp-Asp-Asp-Lys. Enterokinase will not work if the recognition site is followed by a proline. This protease with 10 × His-tag binds with Ni2+ affinity chromatography and was designed for removing from digestion system.
Application
Protein Purification.
Fusion Protein Cleavage.Unit Definition
1 unit is defined as the amount of enzyme required to cleave 25 µg of a MBP-EK-paramyosin-ΔSal substrate to 95% completion in 16 hours at 25°C in a total reaction volume of 100 µl.
Purity
>95% as determined by SDS-PAGE.
>95% as determined by SEC-MALS.
Enzyme Activity
>8 U/μL
Endotoxin
Less than 1.0 EU per μg by the LAL method / rFC method.
Formulation
Supplied as 0.2 μm filtered solution in 20 mM Tris, 200 mM NaCl, pH7.2 with glycerol as protectant.
Contact us for customized product form or formulation.
Shipping
This product is supplied and shipped with dry ice, please inquire the shipping cost.
Storage
This product is stable after storage at:
- The product MUST be stored at -20°C or lower upon receipt;
- -20°C for 3 months under sterile conditions.
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Data Display
SDS-PAGE
The gel was stained with Coomassie Blue. The purity of the protein is greater than 95% (With Star Ribbon Pre-stained Protein Marker).
SEC-MALS
The purity of Enterokinase (Cat. No. ENE-B57H4) is more than 95% and the molecular weight of this protein is around 30-45 kDa verified by SEC-MALS.
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Bioactivity
Enterokinase is a specific protease that cleaves after lysine at its cleavage site Asp-Asp-Asp-Asp-Lys. It will sometimes cleave at other basic residues, depending on the conformation of the protein substrate. The specific activity is ＞8U/ul (QC tested).
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