Expression, purification, and characterization of c-FLIP tandem death effector domains from Escherichia coli.

Cellular FLICE-like inhibitory protein (c-FLIP) regulates extrinsic apoptosis by controlling procaspase-8 activation through its tandem N-terminal death effector domains (DEDs). Here, we present the expression and purification of c-FLIP tandem DEDs (tDED) from Escherichia coli. We observed that the c-FLIP ^tDED maintains monomeric form under near-physiological pH condition in vitro. Our results also reveal a significant correlation between the pH conditions and the structure of c-FLIP ^tDED (F114A). The described methods and results would be helpful for follow-up study on the structural and functional of c-FLIP.
Competing Interests: Declaration of competing interest The authors declare no conflict of interest.
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