FLIP (I-FLICE, CLARP, CASPER, Usurpin, CASH, FLAME-1)

FLIP is an apoptosis regulator protein which functions as a crucial link between cell survival and cell death pathways in mammalian cells and acts as an inhibitor of TNFRSF6 mediated apoptosis. A proteolytic fragment (p43) is likely retained in the death-inducing signaling complex (DISC) thereby blocking further recruitment and processing of caspase-8 at the complex. Full length and shorter isoforms have been shown either to induce apoptosis or to reduce TNFRSF-triggered apoptosis. FLIP lacks enzymatic (caspase) activity. FLIP is highly expressed in skeletal muscle, pancreas, heart, kidney, placenta and peripheral blood leukocytes.\n\nApplications:\nSuitable for use in Immunocytochemistry, Immunohistochemistry, Western Blot\n\nRecommended Dilution:\nOptimal dilutions to be determined by researcher.\n\nStorage and Stability:\nMay be stored at 4 degrees C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20 degrees C. Aliquots are stable for at least 12 months. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.

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SPECIFICATIONS

Catalog Number

044819

Size

50ug

Applications

ICC, IHC, WB

Hosts

Mouse

Form

Supplied as a liquid in PBS, 10% glycerol, 0.02% sodium azide.

P Type

Mab

Purity

Purified by Protein A affinity chromatography.

Isotype

IgG1

References

Product Reference: \n?The role of c-FLIP in modulation of CD95-induced apoptosis: S. Scaffidi, et al.; J. Biol. Chem. 274, 1541 (1999)\n?An inducible pathway for degradation of FLIP protein sensitizes tumor cells to TRAIL-induced apoptosis: Y. Kim, et al.; J. Biol. Chem. 277, 22320 (2002)\n?Caspase-10 is recruited to and activated at the native TRAIL and CD95 death-inducing signalling complexes in a FADD-dependent manner but can not functionally substitute caspase-8: M.R. Sprick, et al.; EMBO J. 21, 4520 (2002)\n?Enhancement of Apo2L/TRAIL (tumor necrosis factor-related apoptosis-inducing ligand)-induced apoptosis in non-small cell lung cancer cell lines by chemotherapeutic agents without correlation to the expression level of cellular protease: S. Frese, et al.; J. Thorac. Cardiovasc. Surg. 123, 168 (2002)\n?Lack of Proapoptotic Activity of Soluble CD95 Ligand Is Due to Its Failure to Induce CD95 Oligomers: S. Jang, et al.; J. Int. Cyt. Res. 23, 441 (2003)\n?Proteasome inhibition results in TRAIL sensitization of primary keratinocytes by removing the resistance-mediating block of effector caspase maturation: M. Leverkus, et al.; Mol. Cell. Biol. 23, 777 (2003)\n?Suramin inhibits death receptor-induced apoptosis in vitro and fulminant apoptotic liver damage in mice: S.T. Eichhorst, et al.; Nature Med. 10, 602 (2004)\n?The c-FLIP-NH2 terminus (p22-FLIP) induces NF-kappaB activation: A. Golks, et al.; J. Exp. Med. 203, 1295 (2006) \n?Caspase-2 is activated at the CD95 death-inducing signaling complex in the course of CD95-induced apoptosis: I.N. Lavrik, et al.; Blood 108, 559 (2006)\n?The role of CAP3 in CD95 signaling: new insights into the mechanism of procaspase-8 activation: A. Golks, et al.; Cell Death Diff. 13, 489 (2006)\n?Expression of c-FLIP is primarily detected in diffuse large B-cell lymphoma and Hodgkin's lymphoma and correlates with lack of caspase 8 activation: I.S. van Houdt, et al.; Histopathology 51, 778 (2007)\n?CD95 Stimulation Results in the Formation of a Novel Death Effector Domain Protein-containing Complex: I.N. Lavrik, et al.; J. Biol. Chem. 283, 26401 (2008)\n?A New C-terminal Cleavage Product of Procaspase-8, p30, Defines an Alternative Pathway of Procaspase-8 Activation: J.C. Hoffmann, et al.; Mol. Cell Biol. 29, 4431 (2009)\n?Stoichiometry of the CD95 Death-Inducing Signaling Complex: Experimental and Modeling Evidence for a Death Effector Domain Chain Model: K. Schleich, et al.; Mol. Cell 47, 1 (2012)\n?

Additional Info

Recognizes short (FLIPS) and long (FLIPL) splice variants of human FLIP.

Alternative Names

I-FLICE, CLARP, CASPER, Usurpin, CASH, FLAME-1