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
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0.1 MG
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0.1 MG
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$533.00
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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
10 - Combustible liquids
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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)
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
D K Han et al.
Proceedings of the National Academy of Sciences of the United States of America, 94(21), 11333-11338 (1997-10-23)
Activation of the cascade of proteolytic caspases has been identified as the final common pathway of apoptosis in diverse biological systems. We have isolated a gene, termed MRIT, that possesses overall sequence homology to FLICE (MACH), a large prodomain caspase
J Bertin et al.
Proceedings of the National Academy of Sciences of the United States of America, 94(4), 1172-1176 (1997-02-18)
To identify novel antiapoptotic proteins encoded by DNA viruses, we searched viral genomes for proteins that might interfere with Fas and TNFR1 apoptotic signaling pathways. We report here that equine herpesvirus type 2 E8 protein and molluscum contagiosum virus MC159
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