Enterokinase Cleavage Enzyme
Enterokinase
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Detailed Information
Description
The enterokinase included in this kit is the catalytic
subunit of the native holoenzyme, and is highly active and specific for cleaving fusion proteins with the recognition sequence, DDDDK, in the interdomain linker.
Because this product is produced from mammalian expression system, it is highly glycosylated and shows extremely specific cleavage activity compared to other E. coli produced enterokinases. The purified enterokinase behaves as a 47kD band under denaturing and reducing conditions as visualized on SDS-PAGE.
subunit of the native holoenzyme, and is highly active and specific for cleaving fusion proteins with the recognition sequence, DDDDK, in the interdomain linker.
Because this product is produced from mammalian expression system, it is highly glycosylated and shows extremely specific cleavage activity compared to other E. coli produced enterokinases. The purified enterokinase behaves as a 47kD band under denaturing and reducing conditions as visualized on SDS-PAGE.
Applications
Enterokinase is a site-specific protease that recognizes and cleaves after the C-terminal end of lysine residue in the recognition sequence, DDDDK. Unlike other site-specific proteases that cut within the recognition sequences leaving extra amino acids in the cleaved peptide products, the C-terminal peptide fragment produced from the enterokinase cleavage reaction doesn't inherent any residues from the DDDDK recognition sequence*. Therefore, the application can be extremely advantageous for producing a 100% native protein sequence and structure from recombinant fusion protein,
which has the desired product immediately after the enterokinase recognition sequence, DDDDK. [*Note: Enterokinase will not cleave at site when lysine is followed by proline.]
In addition, DDDDK is part of the octapeptide FLAG tag (DYKDDDDK), which has been used as a fusion tag for recognition by antibody and detection of fusion protein expression with Western blot analysis, and for purification of the fusion protein by Anti-FLAG affinity chromatography. This array of applications makes enterokinase an ideal tool in the research involving the study of protein structure and function, and protein production where native protein structures and sequences are desired.
which has the desired product immediately after the enterokinase recognition sequence, DDDDK. [*Note: Enterokinase will not cleave at site when lysine is followed by proline.]In addition, DDDDK is part of the octapeptide FLAG tag (DYKDDDDK), which has been used as a fusion tag for recognition by antibody and detection of fusion protein expression with Western blot analysis, and for purification of the fusion protein by Anti-FLAG affinity chromatography. This array of applications makes enterokinase an ideal tool in the research involving the study of protein structure and function, and protein production where native protein structures and sequences are desired.
Components
Special Features
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