Anti-FLIP Purified

Description: The polyclonal antibody reacts with human, mouse, and rat FLIP (N-terminus); the antibody was raised against amino acid 2-18 of human FLIP and recognizes all FLIP variants of human, mouse and rat origin. Cellular FLIP, FLICE-like inhibitory proteins, exist as a long c-FLIP_L and a short c-FLIP_S splice variant, both of them capable of protecting cells from death receptor-mediated apoptosis. FLIP proteins structurally resemble caspase-8 except that they lack proteolytic activity. FLIP variants are highly expressed in tumor cells, T lymphocytes and healthy, but not injured, myocytes; this suggests a critical role of FLIP as endogenous modulators of apoptosis. FLIP are recruited to the death-inducing signaling complex and interfere with the recruitment of caspase-8.

References:
Djerbi, M., T. Darreh-Shori, et al. 2001. Characterization of the human FLICE-inhibitory protein locus and comparison of the anti-apoptotic activity of four different flip isoforms. Scand J Immunol 54: 180-9.
Konopleva, M., S. Zhao, et al. 1999. Apoptosis. Molecules and mechanisms. Adv Exp Med Biol 457: 217-36.
Poulaki, V., N. Mitsiades, et al. 2001. Fas-mediated apoptosis in neuroblastoma requires mitochondrial activation and is inhibited by FLICE inhibitor protein and Bcl-2. Cancer Res 61: 4864-72.
Tschopp, J., M. Irmler, et al. 1998. Inhibition of fas death signals by FLIPs. Curr Opin Immunol 10: 552-8.
Krueger, A., I. Schmitz, et al. 2001. Cellular FLICE-inhibitory protein splice variants inhibit different steps of caspase-8 activation at the CD95 death-inducing signaling complex. J Biol Chem 276: 20633-40.
Kirchhoff, S., W. W. Muller, et al. 2000. TCR-mediated up-regulation of c-FLIPshort correlates with resistance toward CD95-mediated apoptosis by blocking death-inducing signaling complex activity. J Immunol 165: 6293-300.