| Field | Specification |
|---|---|
| Mfr No | |
| Alternative Names | 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; Caspase-8 subunit p18; Caspase-8 subunit p10; CASP8; MCH5 |
| Cellular Localization | |
| Clonality | |
| Concentration | |
| Host | |
| Immunogen | E. coli-derived human Caspase 8 recombinant protein (Position: Q389-D479). |
| Isotype | |
| Molecular Weight | |
| Product Type | |
| Reactivity | |
| Reconstitution | |
| Target | |
| UniProt # |
Overview
This antibody is intended for detection of CASP8 in biological samples using common immunoassay formats. It is typically selected based on target identity, species reactivity, clonality/clone information, and detection modality.
Vendor notes: Boster Bio Anti-Caspase 8/CASP8 Antibody Picoband® catalog # A00042-1. Tested in ELISA, WB applications. This antibody reacts with Human, Mouse, Rat. The brand Picoband indicates this is a premium antibody that guarantees superior quality, high affinity, and strong signals with minimal background in Western blot applications. Only our best-performing antibodies are designated as Picoband, ensuring unmatched performance.
Key elements and design rationale
- Antibody format: Rabbit Polyclonal Rabbit IgG
- Immunogen / epitope context: E. coli-derived human Caspase 8 recombinant protein (Position: Q389-D479). (reported region: Q389-D479).
- Molecular weight context: reported MW: 55-60 kDa; calculated MW: nan
- Reactivity: Human,Mouse,Rat
- Applications: ELISA, WB
As a polyclonal antibody, the reagent recognizes multiple epitopes on the target, which can improve detection robustness but may increase sensitivity to sample-dependent epitope changes.
Biological background
caspase 8. CASP8 is also known as CAP4, MACH or MCH5. This gene encodes 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. This protein is involved in the programmed cell death induced by Fas and various apoptotic stimuli. The N-terminal FADD-like death effector domain of this protein suggests that it may interact with Fas-interacting protein FADD. In addtion, this protein was detected in the insoluble fraction of the affected brain region from Huntington disease patients but not in those from normal controls, which implicated the role in neurodegenerative diseases. Many alternatively spliced transcript variants encoding different isoforms have been described, although not all variants have had their full-length sequences determined. Functional note: 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- Reported localization: Cytoplasm. Expression/tissue context: 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.
Research relevance and current trends
- Apoptosis: Researchers commonly examine how CASP8 relates to this theme using model systems and orthogonal readouts.
- Apoptotic Markers: Researchers commonly examine how CASP8 relates to this theme using model systems and orthogonal readouts.
- Cancer: Researchers commonly examine how CASP8 relates to this theme using model systems and orthogonal readouts.
Common research applications
- Western blotting: compare relative CASP8 levels across conditions; band patterns may reflect isoforms and processing.
- ELISA-compatible use: when applicable, interpret signal as relative abundance across sample sets with consistent handling and dilution strategy.
Notes for experimental interpretation
- Specificity notes: No cross reactivity with other proteins.
- Cross-reactivity: No cross-reactivity with other proteins.
- Isoforms and PTMs: Apparent size and signal patterns can differ across splice isoforms, proteolytic processing, and post-translational modifications.
- Controls: Include an isotype control (as relevant), no-primary control for imaging, and orthogonal validation such as KD/KO samples when available.
Customization & Add-ons: Can’t find the antibody you need—or require a custom format for your assay? We can help you source the best match or support custom antibody solutions for diverse research needs, including species and isotype selection, conjugations and labeling (e.g., HRP/AP, biotin, fluorophores), purification grade options (Protein A/G, affinity purified), formulation preferences (buffer selection, carrier-free, glycerol-free), custom concentrations and aliquoting, low-endotoxin options for cell-based work, and application-focused QC/validation support (project dependent). Click Talk to a Scientist to submit a request, email us at support@biohippo.com, or explore our Research Services for additional support—our team will follow up with feasibility details and next steps.
