F9675
Anti-FLIPL C-Terminal antibody produced in rabbit
~0.5 mg/mL, IgG fraction of antiserum, buffered aqueous solution
Synonym(s):
Anti-CASHα
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About This Item
Conjugate:
unconjugated
Clone:
polyclonal
Application:
ELISA, ICC, WB
Citations:
11
biological source
rabbit
conjugate
unconjugated
antibody form
IgG fraction of antiserum
antibody product type
primary antibodies
clone
polyclonal
form
buffered aqueous solution
mol wt
antigen 53 kDa
species reactivity
mouse
concentration
~0.5 mg/mL
technique(s)
ELISA: suitable, immunocytochemistry: suitable, western blot: suitable
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
Quality Level
Gene Information
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, δ. Along with splice variants, it has two endogenous forms of the protein c-FLIPlong and c-FLIPshort.
Immunogen
synthetic peptide corresponding to amino acids 449-465 of the C-terminal region of mouse FLIPL.
Application
Anti-FLIPL C-Terminal antibody is suitable for western blot at 1-2 μg/mL. Antibody can also be used for immunocytochemistry starting at 5 μg/mL.
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.
The antibody does not react with short form, FLIPS.
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
Regulatory Information
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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)
H B Shu et al.
Immunity, 6(6), 751-763 (1997-06-01)
Caspases are cysteine proteases that play a central role in apoptosis. Caspase-8 may be the first enzyme of the proteolytic cascade activated by the Fas ligand and tumor necrosis factor (TNF). Caspase-8 is recruited to Fas and TNF receptor-1 (TNF-R1)
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
N Inohara et al.
Proceedings of the National Academy of Sciences of the United States of America, 94(20), 10717-10722 (1997-10-06)
We have identified and characterized CLARP, a caspase-like apoptosis-regulatory protein. Sequence analysis revealed that human CLARP contains two amino-terminal death effector domains fused to a carboxyl-terminal caspase-like domain. The structure and amino acid sequence of CLARP resemble those of caspase-8
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