Coding

Part:BBa_K4575027

Designed by: Sumohit Sharma   Group: iGEM23_Stuttgart   (2023-10-11)


enterokinase cleavage site Variant 7

An enterokinase cleavage site is a specific peptide sequence recognized and cleaved by enterokinase, a protease enzyme. The consensus recognition sequence for enterokinase is typically DDDDK/↓, where "↓" indicates the cleavage site. Upon encountering this sequence, enterokinase cleaves the peptide bond after the last aspartic acid (D) residue. This cleavage is vital in biotechnology and molecular biology, as it allows for the controlled release of a target protein from a fusion protein or peptide construct, enabling downstream purification or activation of the desired protein. Enterokinase cleavage is widely employed in protein expression and purification processes.

Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    COMPATIBLE WITH RFC[25]
  • 1000
    COMPATIBLE WITH RFC[1000]


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Categories
Parameters
None