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Merck
CN

F9675

Sigma-Aldrich

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

MDL number:
UNSPSC Code:
12352203
NACRES:
NA.41
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biological source

rabbit

Quality Level

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

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 Code

10 - Combustible liquids

Regulatory Information

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Apoptosis. Placing death under control.
D Wallach
Nature, 388(6638), 123-123 (1997-07-10)
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
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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