Caspase-8 Antibody (YA5419)

Cat. No.: HY-P85727: Fiche technique User Guide for Antibodies
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Caspase-8 Antibody (YA5419) is a Mouse-derived and non-conjugated monoclonal antibody, targeting to Caspase-8.

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Size		Stock
50 μL		Obtenir un devis
100 μL		Obtenir un devis

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WB: Western Blot;
IHC-P: Immunohistochemistry-Paraffin;
IHC-F: Immunohistochemistry-Frozen;
ICC/IF: Immunocytochemistry/Immunofluorescence;
IF-Tissue: Immunofluorescence-Tissue;
mIHC: Multiplex Immunohistochemical;
IP: Immunoprecipitation;
ChIP: Chromatin Immunoprecipitation;
FC: Flow Cytometry;
ELISA: Enzyme Linked Immunosorbent Assay

Product Detail
Background
Description

Description

Caspase-8 Antibody (YA5419) is a Mouse-derived and non-conjugated monoclonal antibody, targeting to Caspase-8.

Host

Mouse

Clonality

Monoclonal

Masse moléculaire

Observed band size: 43,57 kDa

Note: Due to possible protein modifications or aggregation, the molecular weight should be confirmed by actual measurement, and the predicted value is for reference only.

Species Reactivity

Human, Mouse, Rat

SwissProt ID

Q14790

Gene ID

841 [NCBI]

Immunogen

Recombinant Protein of Caspase-8

Application &
Dilution Ratio

Application	Dilution Ratio
WB WB: Western Blot	1:1000-2000
IHC-P IHC-P: Immunohistochemistry-Paraffin	1:200-500
ICC/IF ICC/IF: Immunocytochemistry/Immunofluorescence	1:200

Pureté	affinity chromatography.	Conjugation	Non-conjugated
Modification	Unmodified

Appearance

Liquid

Formulation

Supplied in PBS, pH 7.4, containing 0.5%BSA, 0.02% sodium azide as Preservative and 50% Glycerol.

Storage & Stability

Stored at -20°C for 1 year. Avoid repeated freeze / thaw cycles.

Livraison

Shipping with blue ice.

Background

Function：Thiol protease that plays a key role in programmed cell death by acting as a molecular switch for apoptosis, necroptosis and pyroptosis, and is required to prevent tissue damage during embryonic development and adulthood (PubMed:23516580, PubMed:35338844, PubMed:35446120, PubMed:8681376, PubMed:8681377, PubMed:8962078, PubMed:9006941, PubMed:9184224). Initiator protease that induces extrinsic apoptosis by mediating cleavage and activation of effector caspases responsible for FAS/CD95-mediated and TNFRSF1A-induced cell death (PubMed:23516580, PubMed:35338844, PubMed:35446120, PubMed:8681376, PubMed:8681377, PubMed:8962078, PubMed:9006941, PubMed:9184224). Cleaves and activates effector caspases CASP3, CASP4, CASP6, CASP7, CASP9 and CASP10 (PubMed:16916640, PubMed:8962078, PubMed:9006941). Binding to the adapter molecule FADD recruits it to either receptor FAS/TNFRSF6 or TNFRSF1A (PubMed:8681376, PubMed:8681377). The resulting aggregate called the death-inducing signaling complex (DISC) performs CASP8 proteolytic activation (PubMed:9184224). The active dimeric enzyme is then liberated from the DISC and free to activate downstream apoptotic proteases (PubMed:9184224). Proteolytic fragments of the N-terminal propeptide (termed CAP3, CAP5 and CAP6) are likely retained in the DISC (PubMed:9184224). In addition to extrinsic apoptosis, also acts as a negative regulator of necroptosis: acts by cleaving RIPK1 at 'Asp-324', which is crucial to inhibit RIPK1 kinase activity, limiting TNF-induced apoptosis, necroptosis and inflammatory response (PubMed:31827280, PubMed:31827281). Also able to initiate pyroptosis by mediating cleavage and activation of gasdermin-C and -D (GSDMC and GSDMD, respectively): gasdermin cleavage promotes release of the N-terminal moiety that binds to membranes and forms pores, triggering pyroptosis (PubMed:32929201, PubMed:34012073). Initiates pyroptosis following inactivation of MAP3K7/TAK1 (By similarity). Also acts as a regulator of innate immunity by mediating cleavage and inactivation of N4BP1 downstream of TLR3 or TLR4, thereby promoting cytokine production (By similarity). May participate in the Granzyme B (GZMB) cell death pathways (PubMed:8755496). Cleaves PARP1 and PARP2 (PubMed:8681376). Independent of its protease activity, promotes cell migration following phosphorylation at Tyr-380 (PubMed:18216014, PubMed:27109099); Lacks the catalytic site and may interfere with the pro-apoptotic activity of the complex; Lacks the catalytic site and may interfere with the pro-apoptotic activity of the complex; Lacks the catalytic site and may interfere with the pro-apoptotic activity of the complex (Probable). Acts as an inhibitor of the caspase cascade (PubMed:12010809); Lacks the catalytic site and may interfere with the pro-apoptotic activity of the complex

Subcellular Localization：Cytoplasm; Nucleus; Cell projection, lamellipodium

Expression：
Tissue_specificity:Isomers 1, 5, and 7 are expressed in a variety of tissues. They are most highly expressed in peripheral blood leukocytes, spleen, thymus, and liver. They are almost undetectable in the brain, testes, and skeletal muscle.

Isoforms & Post-Translational Modification：Q14790 has 9 isomers: Q14790-1: 55391 Da (predicted); Q14790-2: 53768 Da (predicted); Q14790-3: 45929 Da (predicted); Q14790-4: 57701 Da (predicted); Q14790-5: 27484 Da (predicted); Q14790-6: 25862 Da (predicted); Q14790-7: 32330 Da (predicted); Q14790-8: 30707 Da (predicted); Q14790-9: 61836 Da (predicted).
Generation of the p10 and p18 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 (PubMed:20937773). Phosphorylation on Tyr-380 by SRC is mediated by interaction with the SRC SH2 domain and does not affect dimerization or recruitment to the death-inducing signaling complex (DISC) but negatively regulates DISC-mediated processing and activation of CASP8, down-regulating its proapoptotic function (PubMed:16619028, PubMed:27109099). Phosphorylation on Tyr-380 also enhances localization to lamellipodia in migrating cells (PubMed:18216014);(Microbial infection) ADP-riboxanation by C.violaceum CopC blocks CASP8 processing, preventing CASP8 activation and ability to mediate extrinsic apoptosis;(Microbial infection) Proteolytically cleaved by the cowpox virus CRMA death inhibitory protein

Subunit：Heterotetramer that consists of two anti-parallel arranged heterodimers, each one formed by a 18 kDa (p18) and a 10 kDa (p10) subunit (PubMed:10508784). Component of the death-induced signaling complex (DISC) composed of cell surface receptor FAS/CD95 or TNFRSF1A, adapter protein FADD and the CASP8 protease; recruitment of CASP8 to the complex is required for processing of CASP8 into the p18 and p10 subunits (PubMed:8681376, PubMed:8681377, PubMed:9184224). Component of the AIM2 PANoptosome complex, a multiprotein complex that drives inflammatory cell death (PANoptosis) (By similarity). Interacts with CFLAR and PEA15 (PubMed:10442631). Interacts with TNFAIP8L2 (By similarity). Interacts with CASP8AP2 (PubMed:16378960). Interacts with RFFL and RNF34; negatively regulate CASP8 through proteasomal degradation (PubMed:15069192). Interacts with NOL3; decreases CASP8 activity in a mitochondria localization- and phosphorylation-dependent manner and this interaction is dissociated by calcium (PubMed:15509781). Interacts with UBR2ca (PubMed:28602583). Interacts with RIPK1 (By similarity). Interacts with stimulated TNFRSF10B; this interaction is followed by CASP8 proteolytic cleavage and activation (PubMed:18846110). Interacts (phosphorylated on Tyr-380) with PIK3R1 (PubMed:27109099)

Synonyms

CASP8; MCH5; Caspase-8; CASP-8; Apoptotic cysteine protease; Apoptotic protease Mch-5; CAP4; FADD-homologous ICE/ced-3-like protease; FADD-like ICE; FLICE; ICE-like apoptotic protease 5; MORT1-associated ced-3 homolog; MACH

Documentation

User Guide for Antibodies (1077 KB)