FLIPs, CT, (FLICE Inhibitory Protein) Blocking Peptide

Apoptosis is related to many diseases and induced by a family of cell death receptors and their ligands. Cell death signals are transduced by death domain (DD)-containing adapter molecules and members of the ICE/CED-3 protease family. Caspases-8 (FLICE) and -10 (FLICE2) are two pivotal members in the ICE/CED-3 protease family. FLICE-inhibitory proteins were identified in virus and human and designated v-FLIPs and c-FLIPs, respectively (1,2). The human FLIPs were also cloned by several labs independently and termed Casper, I-FLICE, FLAME-1, CASH, CLARP and usurpin3-7. FLIP contains two death effector domains (DEDs) and a caspase-like domain. FLIP interacts with adapter protein FADD and caspase-8 and -10, and potently inhibits apoptosis induced by all known death receptors CD95, DR3, TRAIL-R and TNFR1. Four splice variants of c-FLIPs have been identified and termed FLIPa, b, g, and d, respectively.\n\nApplications:\nSuitable for use in Western Blot. Other applications not tested.\n\nRecommended Dilution:\nThis peptide is used for blocking the activity of anti-FLIPs. Incubating the peptide with equal volume of antibody for 30 minutes at 37 degrees C usually completely blocks the antibody activity in Western Blot..\n\nStorage and Stability:\nMay be stored at 4 degrees C for short-term only. For long-term storage, store at -20 degrees C. Aliquots are stable for at least 6 months at -20 degrees C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.

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SPECIFICATIONS

Catalog Number

F4550-10P

Size

50ug

Applications

WB

References

1. Thome M, Schneider P, Hofmann K, Fickenscher H, Meinl E, Neipel F, Mattmann C, Burns K, Bodmer JL, Schroter M, Scaffidi C, Krammer PH, Peter ME, Tschopp J. Viral FLICE-inhibitory proteins (FLIPs) prevent apoptosis induced by death receptors. Nature 1997;386:517-521 \n\n2. Irmler M, Thome M, Hahne M, Schneider P, Hofmann K, Steiner V, Bodmer JL, Schroter M, Burns K, Mattmann C, Rimoldi D, French LE, Tschopp J. Inhibition of death receptor signals by cellular FLIP. Nature 1997;388:190-195 \n\n3. Shu HB, Halpin DR, Goeddel DV. Casper is a FADD- and caspase-related inducer of apoptosis. Immunity 1997;6:751-763 \n\n4. Hu S, Vincenz C, Ni J, Gentz R, Dixit VM. I-FLICE, a novel inhibitor of tumor necrosis factor receptor-1- and CD-95-induced apoptosis. J Biol Chem 1997;272:17255-17257 \n\n5. Srinivasula SM, Ahmad M, Ottilie S, Bullrich F, Banks S, Wang Y, Fernandes-Alnemri T, Croce CM, Litwack G, Tomaselli KJ, Armstrong RC, Alnemri ES. FLAME-1, a novel FADD-like anti-apoptotic molecule that regulates Fas/TNFR1-induced apoptosis. J Biol Chem 1997;272:18542-18545 \n\n6. Goltsev YV, Kovalenko AV, Arnold E, Varfolomeev EE, Brodianskii VM, Wallach D. CASH, a novel caspase homologue with death effector domains. J Biol Chem 1997;272:19641-19644 \n\n7. Inohara N, Koseki T, Hu Y, Chen S, Nunez G. CLARP, a death effector domain-containing protein interacts with caspase-8 and regulates apoptosis. Proc Natl Acad Sci USA 1997;94:10717-10722 \n\n8. Tschopp J, Irmler M, Thome M. Inhibition of fas death signals by FLIPs. Curr Opin Immunol 1998;10:552-8 \n