A introduction to rEK Enzyme

Enterokinase (EC3.4.21.9) belongs to serine proteases, produced by cells in the duodenal wall, and specifically recognizes and cleaves proteins or peptides-asp-asp-asp-asp-lys-↓-X. Natural bovine enterokinase contains a heavy chain of 800 amino acids and a light chain of 235 amino acids.
This product is a monoglycosylated form of bovine enterokinase light chain, recombinant expression by Pichia yeast and purified by high-performance chromatography, containing 6 His-tags, theoretical molecular weight of about 43 kDa, optimal digestion pH of 4.5-9.5, and optimal digestion temperature of 25°C. Recombinant interic kinase activity is inhibited to varying degrees by imidazole, sodium chloride, glycerin, phosphate, etc.
rEK applications:

1. Due to the high specificity and high hydrolysis efficiency of enterokinase, it is widely used in the development of genetic engineering products. It can specifically recognize and cleave substrates containing the enterokinase cleavage site DDDDK- as a protease, and one of its applications is as a tool protease for specific breakage of recombinant fusion proteins, especially in the bioengineering pharmaceutical industry and research in genetic engineering, biochemistry, molecular biology, etc. [2].
2. Enterokinase can be solidified, more effective in cleaving fusion proteins, and maintaining higher activity of enterokinase, which is conducive to reducing the production cost of biological drugs [3].
3. Scientific research use: fusion tag excision of recombinant expressed proteins; Activation of trypsinogen.

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