FLIP_L Antibody (5D8): sc-136160

FLIPL Antibody (5D8) is a mouse monoclonal IgG3 antibody that detects FLIPL protein of mouse, rat, and human origin by western blotting (WB), immunoprecipitation (IP), and enzyme-linked immunosorbent assay (ELISA). Anti-FLIPL antibody (5D8) is available as the non-conjugated format. FLIPL protein, also known as FLICE inhibitory protein, plays a crucial role in regulating apoptosis, acting as a key modulator in cell survival and death pathways. FLIPL exists in two forms: the long form, which contains an additional caspase-like domain, and the short form, which includes two death effector domains homologous to those found in the Fas-associating protein FADD. The long form of FLIPL, while structurally similar to the cysteine protease FLICE, lacks a catalytic active site, making FLIPL a unique player in apoptosis regulation. FLIPL has been identified by various names, including Casper, I-FLICE, CLARP, FLAME-1, and MRIT, reflecting FLIPL′s diverse roles in cellular processes. FLIPL interacts with several proteins involved in apoptotic signaling, including FADD and caspases, which underscores FLIPL′s importance in maintaining cellular homeostasis and preventing inappropriate cell death. Understanding FLIPL function and interactions is vital for elucidating FLIPL′s role in diseases characterized by dysregulated apoptosis, such as cancer and autoimmune disorders.

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FLIP_L Antibody (5D8) References:

1. Modulation of caspase-8 and FLICE-inhibitory protein expression as a potential mechanism of Epstein-Barr virus tumorigenesis in Burkitt's lymphoma.  |  Tepper, CG. and Seldin, MF. 1999. Blood. 94: 1727-37. PMID: 10477698
2. Fas-associated death domain protein (FADD) and caspase-8 mediate up-regulation of c-Fos by Fas ligand and tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) via a FLICE inhibitory protein (FLIP)-regulated pathway.  |  Siegmund, D., et al. 2001. J Biol Chem. 276: 32585-90. PMID: 11384965
3. Resistance of human ovarian cancer cells to tumor necrosis factor alpha is a consequence of nuclear factor kappaB-mediated induction of Fas-associated death domain-like interleukin-1beta-converting enzyme-like inhibitory protein.  |  Xiao, CW., et al. 2003. Endocrinology. 144: 623-30. PMID: 12538625
4. Association of TRAF2 with the short form of cellular FLICE-like inhibitory protein prevents TNFR1-mediated apoptosis.  |  Kim, DJ., et al. 2008. J Mol Signal. 3: 2. PMID: 18190721
5. In mouse embryonic fibroblasts, neither caspase-8 nor cellular FLICE-inhibitory protein (FLIP) is necessary for TNF to activate NF-κB, but caspase-8 is required for TNF to cause cell death, and induction of FLIP by NF-κB is required to prevent it.  |  Moujalled, DM., et al. 2012. Cell Death Differ. 19: 808-15. PMID: 22095280
6. Viral FLICE-inhibitory proteins (FLIPs) prevent apoptosis induced by death receptors.  |  Thome, M., et al. 1997. Nature. 386: 517-21. PMID: 9087414
7. Casper is a FADD- and caspase-related inducer of apoptosis.  |  Shu, HB., et al. 1997. Immunity. 6: 751-63. PMID: 9208847
8. I-FLICE, a novel inhibitor of tumor necrosis factor receptor-1- and CD-95-induced apoptosis.  |  Hu, S., et al. 1997. J Biol Chem. 272: 17255-7. PMID: 9211860
9. Inhibition of death receptor signals by cellular FLIP.  |  Irmler, M., et al. 1997. Nature. 388: 190-5. PMID: 9217161
10. FLAME-1, a novel FADD-like anti-apoptotic molecule that regulates Fas/TNFR1-induced apoptosis.  |  Srinivasula, SM., et al. 1997. J Biol Chem. 272: 18542-5. PMID: 9228018
11. MRIT, a novel death-effector domain-containing protein, interacts with caspases and BclXL and initiates cell death.  |  Han, DK., et al. 1997. Proc Natl Acad Sci U S A. 94: 11333-8. PMID: 9326610
12. CLARP, a death effector domain-containing protein interacts with caspase-8 and regulates apoptosis.  |  Inohara, N., et al. 1997. Proc Natl Acad Sci U S A. 94: 10717-22. PMID: 9380701

The preferred FLIP_S/L antibody is FLIP_S/L Antibody (G-11): sc-5276.