Recombinant Enterokinase, 6xHis -tagged (rEK, 6xHis) is a highly purified preparation of the catalytic subunit of bovine enterokinase with a 6xHis tag at the C-terminus, which recognizes the identical cleavage site as the native enzyme, AspAspAspAspLys(D DDDK), and has similar enzymatic activity. rEK, 6xHis exhibits superior rates of cleavage of fusion proteins containing the recognition sequence when compared to the native enzyme (1). Biobasic rEK, 6xHis is purified to near homogeneity and, unlike some preparations of native bovine enterokinase, exhibits no secondary cleavage arising from contaminating proteases. The preparation is also functionally tested for activity with fusion proteins, and is an ideal choice for rapid removal of N-terminal fusions and production of recombinant proteins virtually free of vector-encoded
sequences.
A Cleavage Control Protein is included in each kit for conducting control digests in parallel with experimental samples, or to test cleavage under customized buffer conditions. rEK, 6xHis cleaves the 39kDa Cleavage Control Protein into two proteolytic fragments of 22 kDa and 17 kDa, each of which are easily visualized by standard SDS-PAGE followed by Coomassie blue staining.
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