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In vitro transcription of capped mRNA with modified nucleotides and Poly(A) tail
TSA (Tyramide Signal Amplification), used for signal amplification of ISH, IHC and IC etc.
Separation of phosphorylated and non-phosphorylated proteins without phospho-specific antibody
A convenient and sensitive way for cell proliferation assay and cytotoxicity assay
Protect the integrity of proteins from multiple proteases and phosphatases for different applications.
Enterokinase (EK) is an amino protease existing in duodenum of mammal and is involved in digestion. It consists of a disulfide-linked 82–140 kDa heavy chain which anchors enterokinase in the intestinal brush border membrane and a 35–62 kDa light chain which contains the catalytic subunit. Additionally, both of the chains are derived from a single precursor that is cleaved by a trypsin-like protease. EK can specially recognize the amino acid sequence DDDDK, and digest the peptide bond after the lysine residue. rEK was report to be more effective than nature EK in cleaving recombinant proteins. Furthermore, the light chain possesses the whole enzyme activity of EK. rBoEK has the highest activity than EK of other species and is used wildly in biochemical applications. rBoEK with 6 × His-tag binds with Ni2+ affinity chromatography and was designed for removing from digestion system.
Reference
1. Yuan LDandHua ZC. 2002. Protein Expr Purif, 25: 300-4
2. Peng L, Zhong X, Ou J, et al. 2004. J Biotechnol, 108: 185-92
3. Light AandJanska H. 1991. J Protein Chem, 10: 475-80
4. Kubitzki T, Minor D, Mackfeld U, et al. 2009. Biotechnol J, 4: 1610-8.