Key features and details
- Rabbit polyclonal to Caspase-8 (phospho S347)
- Suitable for: ELISA, IHC-P, WB
- Reacts with: Human
- Isotype: IgG
Product nameAnti-Caspase-8 (phospho S347) antibody
See all Caspase-8 primary antibodies
DescriptionRabbit polyclonal to Caspase-8 (phospho S347)
SpecificityThis antibody detects Caspase-8 only when phosphorylated at serine 347.
Tested applicationsSuitable for: ELISA, IHC-P, WBmore details
Species reactivityReacts with: Human
Predicted to work with: Mouse, Rat
Synthetic peptide corresponding to Human Caspase-8.
Database link: Q14790
- Jurkat cell extract treated with PMA, human lung carcinoma tissue.
Storage instructionsShipped at 4°C. Store at -20°C. Stable for 12 months at -20°C.
Storage bufferpH: 7.40
Preservative: 0.02% Sodium azide
Constituents: PBS, 50% Glycerol, 0.87% Sodium chloride
Concentration information loading...
PurityImmunogen affinity purified
Purification notesThe antibody against non-phosphopeptide was removed by chromatography using non-phosphopeptide corresponding to the phosphorylation site.
Our Abpromise guarantee covers the use of ab61755 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
|IHC-P||1/50 - 1/100.|
|WB||1/500 - 1/1000. Detects a band of approximately 55 kDa (predicted molecular weight: 55 kDa).|
FunctionMost upstream protease of the activation cascade of caspases responsible for the TNFRSF6/FAS mediated and TNFRSF1A induced cell death. Binding to the adapter molecule FADD recruits it to either receptor. The resulting aggregate called death-inducing signaling complex (DISC) performs CASP8 proteolytic activation. The active dimeric enzyme is then liberated from the DISC and free to activate downstream apoptotic proteases. Proteolytic fragments of the N-terminal propeptide (termed CAP3, CAP5 and CAP6) are likely retained in the DISC. Cleaves and activates CASP3, CASP4, CASP6, CASP7, CASP9 and CASP10. May participate in the GZMB apoptotic pathways. Cleaves ADPRT. Hydrolyzes the small-molecule substrate, Ac-Asp-Glu-Val-Asp-
-AMC. Likely target for the cowpox virus CRMA death inhibitory protein. Isoform 5, isoform 6, isoform 7 and isoform 8 lack the catalytic site and may interfere with the pro-apoptotic activity of the complex.
Tissue specificityIsoform 1, isoform 5 and isoform 7 are expressed in a wide variety of tissues. Highest expression in peripheral blood leukocytes, spleen, thymus and liver. Barely detectable in brain, testis and skeletal muscle.
Involvement in diseaseDefects in CASP8 are the cause of caspase-8 deficiency (CASP8D) [MIM:607271]. CASP8D is a disorder resembling autoimmune lymphoproliferative syndrome (ALPS). It is characterized by lymphadenopathy, splenomegaly, and defective CD95-induced apoptosis of peripheral blood lymphocytes (PBLs). It leads to defects in activation of T-lymphocytes, B-lymphocytes, and natural killer cells leading to immunodeficiency characterized by recurrent sinopulmonary and herpes simplex virus infections and poor responses to immunization.
Sequence similaritiesBelongs to the peptidase C14A family.
Contains 2 DED (death effector) domains.
DomainIsoform 9 contains a N-terminal extension that is required for interaction with the BCAP31 complex.
modificationsGeneration of the subunits requires association with the death-inducing signaling complex (DISC), whereas additional processing is likely due to the autocatalytic activity of the activated protease. GZMB and CASP10 can be involved in these processing events.
Phosphorylated upon DNA damage, probably by ATM or ATR.
- Information by UniProt
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Human lung carcinoma tissue stained with ab61755 at 1/50 dilution, with and without the immunising phosphopeptide.
All lanes : Anti-Caspase-8 (phospho S347) antibody (ab61755) at 1/500 dilution
Lane 1 : Jurkat cell extract treated with PMA.
Lane 2 : Jurkat cell extract treated with PMA and the immunising phosphopeptide.
Predicted band size: 55 kDa
Observed band size: 55 kDa
ab61755 has not yet been referenced specifically in any publications.