F9925
Anti-FLIPγ/δ, C-Terminal antibody produced in rabbit
1 mg/mL, affinity isolated antibody, buffered aqueous solution
Synonym(s):
Anti-CASH, Anti-CLARP, Anti-FLAME-1, Anti-I-FLICE
biological source
rabbit
Quality Level
conjugate
unconjugated
antibody form
affinity isolated antibody
antibody product type
primary antibodies
clone
polyclonal
form
buffered aqueous solution
mol wt
antigen 25 kDa (FLIPδ/FLIPS)
antigen 35 kDa (FLIPγ)
species reactivity
human, mouse
concentration
1 mg/mL
technique(s)
immunocytochemistry: 2 μg/mL
immunofluorescence: 10 μg/mL
western blot: 1:1,000
UniProt accession no.
storage temp.
−20°C
target post-translational modification
unmodified
Gene Information
human ... CFLAR(8837)
mouse ... Cflar(12633)
General description
In human Viral FLICE-inhibitory proteins (v-FLIPs) is identified as c-FLIP. It is composed of two death effector domains which have structural resemblance with the N-terminal half of caspase-8 and a caspase-like domain. It exist as multiple splice variants: FLIP α, β, γ and δ. Along with splice variants, it has two endogenous forms of the protein − c-FLIPlong and c-FLIPshort.
Immunogen
FLIP antibody was raised against a 19 amino acid peptide near the carboxy terminus of human FLIP.
The immunogen is located within amino acids 180 - 230 of FLIP.
The immunogen is located within amino acids 180 - 230 of FLIP.
Application
Anti-FLIPγ/δ, C-Terminal antibody is suitable for microarray and western blot at a dilution of 1:1,000 using HeLa, Jurkat, THP-1, A431, K562, and NIH-3T3 cell lysates.
Biochem/physiol Actions
C-FLIP plays an important role in apoptosis signaling pathways. It acts as proapoptotic molecule or as an anti-apoptotic molecule. It has been reported that c-FLIP can interact with both FADD and caspase-8. It prevents caspase-8 recruitment and processing through DED-DED (Death Effector Domain) interaction followed by CD95-induced apoptosis.
Physical form
Solution in 0.01 M phosphate buffered saline containing 0.02% sodium azide.
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
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Storage Class Code
10 - Combustible liquids
Regulatory Information
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S Hu et al.
The Journal of biological chemistry, 272(15), 9621-9624 (1997-04-11)
Molluscum contagiosum virus proteins MC159 and MC160 and the equine herpesvirus 2 protein E8 share substantial homology to the death effector domain present in the adaptor molecule Fas-associated death domain protein (FADD) and the initiating death protease FADD-like interleukin-1beta-converting enzyme
M Thome et al.
Nature, 386(6624), 517-521 (1997-04-03)
Viruses have evolved many distinct strategies to avoid the host's apoptotic response. Here we describe a new family of viral inhibitors (v-FLIPs) which interfere with apoptosis signalled through death receptors and which are present in several gamma-herpesviruses (including Kaposi's-sarcoma-associated human
Apoptosis. Placing death under control.
D Wallach
Nature, 388(6638), 123-123 (1997-07-10)
D M Rasper et al.
Cell death and differentiation, 5(4), 271-288 (1999-04-14)
Apoptotic cell suicide initiated by ligation of CD95 (Fas/APO-1) occurs through recruitment, oligomerization and autocatalytic activation of the cysteine protease, caspase-8 (MACH, FLICE, Mch5). An endogenous mammalian regulator of this process, named Usurpin, has been identified (aliases for Usurpin include
Y V Goltsev et al.
The Journal of biological chemistry, 272(32), 19641-19644 (1997-08-08)
CASP-8 and CASP-10, members of a cysteine protease family that participates in apoptosis, interact with MORT1/FADD, an adapter protein in the CD120a (p55 tumor necrosis factor receptor), and CD95 (Fas/Apo-1) death-inducing signaling pathways, through a shared N-terminal sequence motif, the
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