ALPS2B; Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 12 protein; Apoptotic cysteine protease; Apoptotic protease Mch-5; Apoptotic protease Mch5; CAP4; CASP-8; CASP8; CASP8_HUMAN; Caspase 8; Caspase 8 apoptosis related cysteine peptidase; Caspase-8 subunit p10; CED 3; FADD Like ICE; FADD-homologous ICE/CED-3-like protease; FADD-like ICE; FLICE; FLJ17672; ICE-like apoptotic protease 5; MACH alpha 1/2/3 protein; MACH; MACH beta 1/2/3/4 protein; MCH5; MGC78473; MORT1 associated ced 3 homolog; MORT1-associated CED-3 homolog; OTTHUMP00000163717; OTTHUMP00000163720; OTTHUMP00000163724; OTTHUMP00000163725; OTTHUMP00000165062; OTTHUMP00000165063; OTTHUMP00000165064; OTTHUMP00000206552; OTTHUMP00000206582;
WB 1:500-1:2000, IHC 1:50-1:200, IF/ICC 1:100-1:500, ELISA(peptide) 1:20000-1:40000
*The optimal dilutions should be determined by the end user.
Human, Mouse, Rat, Monkey
Pig(80%), Bovine(90%), Horse(80%), Sheep(80%), Rabbit(90%), Dog(90%)
Rabbit
Polyclonal
The antiserum was purified by peptide affinity chromatography using SulfoLink™ Coupling Resin (Thermo Fisher Scientific).
Caspase 8 Antibody detects endogenous levels of total Caspase 8.
AB_2835266
Please cite this product as: Affinity Biosciences Cat# AF6442, RRID:AB_2835266.
Liquid
1mg/ml
Rabbit IgG in phosphate buffered saline , pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.Store at -20 °C.Stable for 12 months from date of receipt.
A synthesized peptide derived from human Caspase 8, corresponding to a region within the internal amino acids.
>>Visit The Human Protein Atlas
CASP8
Observed Mol.Wt.: 55kD.
Predicted Mol.Wt.: 55kDa(Calculated)..
Cytoplasm.
Q14790 CASP8_HUMAN:
Isoform 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.
This gene encodes a protein that is a member of the cysteine-aspartic acid protease (caspase) family. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes composed of a prodomain, a large protease subunit, and a small protease subunit. Activation of caspases requires proteolytic processing at conserved internal aspartic residues to generate a heterodimeric enzyme consisting of the large and small subunits.
MDFSRNLYDIGEQLDSEDLASLKFLSLDYIPQRKQEPIKDALMLFQRLQEKRMLEESNLSFLKELLFRINRLDLLITYLNTRKEEMERELQTPGRAQISAYRVMLYQISEEVSRSELRSFKFLLQEEISKCKLDDDMNLLDIFIEMEKRVILGEGKLDILKRVCAQINKSLLKIINDYEEFSKERSSSLEGSPDEFSNGEELCGVMTISDSPREQDSESQTLDKVYQMKSKPRGYCLIINNHNFAKAREKVPKLHSIRDRNGTHLDAGALTTTFEELHFEIKPHDDCTVEQIYEILKIYQLMDHSNMDCFICCILSHGDKGIIYGTDGQEAPIYELTSQFTGLKCPSLAGKPKVFFIQACQGDNYQKGIPVETDSEEQPYLEMDLSSPQTRYIPDEADFLLGMATVNNCVSYRNPAEGTWYIQSLCQSLRERCPRGDDILTILTEVNYEVSNKDDKKNMGKQMPQPTFTLRKKLVFPSD
Most 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. Cleaves RIPK1 at 'Asp-325' which is crucial for limiting apoptosis and necroptosis during embryonic development (By similarity).
Generation 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.
Phosphorylation on Ser-387 during mitosis by CDK1 inhibits activation by proteolysis and prevents apoptosis. This phosphorylation occurs in cancer cell lines, as well as in primary breast tissues and lymphocytes.
Cytoplasm.
Isoform 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.
Heterotetramer that consists of two anti-parallel arranged heterodimers, each one formed by a 18 kDa (p18) and a 10 kDa (p10) subunit. Interacts with FADD, CFLAR and PEA15. Isoform 9 interacts at the endoplasmic reticulum with a complex containing BCAP31, BAP29, BCL2 and/or BCL2L1. Interacts with TNFAIP8L2 (By similarity). Interacts with CASP8AP2. Interacts with RFFL and RNF34; negatively regulate CASP8 through proteasomal degradation. Interacts with NOL3; decreases CASP8 activity in a mitochondria localization- and phosphorylation-dependent manner and this interaction is dissociated by calcium. Interacts with UBR2. Interacts with RIPK1 (By similarity). Interacts with stimulated TNFRSF10B; this interaction is followed by CASP8 proteolytic cleavage and activation.
(Microbial infection) Interacts with human cytomegalovirus/HHV-5 protein vICA/UL36; this interaction inhibits CASP8 activation.
(Microbial infection) Interacts with NleF from pathogenic E.coli.
(Microbial infection) Interacts with molluscum contagiosum virus protein MC160.
Isoform 9 contains a N-terminal extension that is required for interaction with the BCAP31 complex.
Belongs to the peptidase C14A family.
· Cellular Processes > Cell growth and death > p53 signaling pathway.(View pathway)
· Cellular Processes > Cell growth and death > Apoptosis.(View pathway)
· Cellular Processes > Cell growth and death > Apoptosis - multiple species.(View pathway)
· Cellular Processes > Cell growth and death > Necroptosis.(View pathway)
· Environmental Information Processing > Signal transduction > TNF signaling pathway.(View pathway)
· Human Diseases > Cancers: Overview > Pathways in cancer.(View pathway)
· Human Diseases > Cardiovascular diseases > Viral myocarditis.
· Human Diseases > Infectious diseases: Bacterial > Legionellosis.
· Human Diseases > Infectious diseases: Viral > Herpes simplex infection.
· Human Diseases > Cancers: Overview > Viral carcinogenesis.
· Human Diseases > Infectious diseases: Viral > Hepatitis B.
· Human Diseases > Infectious diseases: Viral > Human papillomavirus infection.
· Human Diseases > Infectious diseases: Parasitic > Chagas disease (American trypanosomiasis).
· Human Diseases > Infectious diseases: Bacterial > Tuberculosis.
· Human Diseases > Drug resistance: Antineoplastic > Platinum drug resistance.
· Human Diseases > Neurodegenerative diseases > Huntington's disease.
· Human Diseases > Endocrine and metabolic diseases > Non-alcoholic fatty liver disease (NAFLD).
· Human Diseases > Neurodegenerative diseases > Alzheimer's disease.
· Human Diseases > Infectious diseases: Parasitic > Toxoplasmosis.
· Organismal Systems > Immune system > RIG-I-like receptor signaling pathway.(View pathway)
· Organismal Systems > Immune system > Toll-like receptor signaling pathway.(View pathway)
· Organismal Systems > Immune system > IL-17 signaling pathway.(View pathway)
· Organismal Systems > Immune system > NOD-like receptor signaling pathway.(View pathway)
Application: IHC Species:mouse; Sample:Not available
Fig. 15 Effect of PPP-40 on caspase-8 expression of splenocytes in S180 mice (magnification × 400). The arrows show the positive expression of caspase-8. (A) Normal group; (B) model group; (C) positive control group (CTX 20 mg kg−1 ); (D) low concentration of the PPP-40 group (50 mg kg−1 ); (E) medium concentration of the PPP-40 group (150 mg kg−1 ); (F) high concentration of the PPP-40 group (300 mg kg−1 ); (G) quantity analysis (mean ± SD, n = 6). *p < 0.05 and **p < 0.01 compared with the normal group; #p < 0.05 and ##p < 0.01 compared with the model group.
Application: WB Species:mouse; Sample:Not available
Figure 3. BCL2L10 induced cell apoptosis and inhibited tumor growth in nude mice. (A) BCL2L10 induced apoptosis in HepG2 and Huh7 cells, as determined by flow cytometry analysis following Annexin V and PI staining. The upper panel represents FACS images of HCC cells transfected with empty vector or BCL2L10, while the lower panel shows the quantitative analyses of early apoptotic and late apoptotic cells. The experiment was repeated three times in triplicate. Data are mean ± SD. (B) Protein expression of the active forms of apoptosis related genes caspase 3, caspase 8, and caspase 9 was evaluated by Western blot.
AF6442-BP
(Blocking peptide available as AF6442-BP)
$350/1mg.
Tips: For phospho antibody, we provide phospho peptide(0.5mg) and non-phospho peptide(0.5mg).
Blocking peptides are peptides that bind specifically to the target antibody and block antibody binding. These peptide usually contains the epitope recognized by the antibody. Antibodies bound to the blocking peptide no longer bind to the epitope on the target protein. This mechanism is useful when non-specific binding is an issue, for example, in Western blotting (immunoblot) and immunohistochemistry (IHC). By comparing the staining from the blocked antibody versus the antibody alone, one can see which staining is specific; Specific binding will be absent from the western blot or immunostaining performed with the neutralized antibody.
Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 10 mg/ml.The purity is >90%,tested by HPLC and MS.Storage Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.
This product is for research use only. Not for use in diagnostic or therapeutic procedures.
Site | PTM Type | Enzyme | Source |
---|---|---|---|
S16 | Phosphorylation | Uniprot | |
K23 | Ubiquitination | Uniprot | |
K34 | Ubiquitination | Uniprot | |
K39 | Ubiquitination | Uniprot | |
K63 | Ubiquitination | Uniprot | |
S113 | Phosphorylation | Uniprot | |
K121 | Ubiquitination | Uniprot | |
K130 | Ubiquitination | Uniprot | |
K148 | Ubiquitination | Uniprot | |
K156 | Acetylation | Uniprot | |
K156 | Ubiquitination | Uniprot | |
K161 | Ubiquitination | Uniprot | |
K169 | Ubiquitination | Uniprot | |
K173 | Ubiquitination | Uniprot | |
Y178 | Phosphorylation | Uniprot | |
K183 | Ubiquitination | Uniprot | |
S192 | Phosphorylation | Uniprot | |
S209 | Phosphorylation | Uniprot | |
S211 | Phosphorylation | Uniprot | |
S219 | Phosphorylation | Uniprot | |
K224 | Ubiquitination | Uniprot | |
K229 | Ubiquitination | Uniprot | |
Y235 | Phosphorylation | Uniprot | |
K253 | Ubiquitination | Uniprot | |
T263 | Phosphorylation | P51812 (RPS6KA3) | Uniprot |
T273 | Phosphorylation | Uniprot | |
S305 | Phosphorylation | Uniprot | |
Y334 | Phosphorylation | Uniprot | |
K344 | Ubiquitination | Uniprot | |
S347 | Phosphorylation | Q16539 (MAPK14) | Uniprot |
K351 | Ubiquitination | Uniprot | |
K353 | Ubiquitination | Uniprot | |
T373 | Phosphorylation | Uniprot | |
S375 | Phosphorylation | Uniprot | |
Y380 | Phosphorylation | P07948 (LYN) , P12931 (SRC) | Uniprot |
S387 | Phosphorylation | P28482 (MAPK1) , P06493 (CDK1) , P27361 (MAPK3) | Uniprot |
Y448 | Phosphorylation | P07948 (LYN) | Uniprot |
K461 | Ubiquitination | Uniprot | |
K473 | Ubiquitination | Uniprot |