Polyclonal antibody to Caspase-8
Fig:1 Formalin-fixed, paraffin-embedded sections from a brain tumor tissue array stained for Caspase-8 expression using 20-1111 at 1:2000. A. Anaplastic glioma cores from two different patients, positive (left) and negative (right) staining for caspase-8. B. Higher magnification from the caspase-8 positive (A, left) core.
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| Format : | Sera |
| Amount : | 50 µl |
| Isotype : | Rabbit IgG |
| Content : | 50 µl sera |
| Storage condition : | Store the antibody at 4°C, stable for 6 months. For long-term storage, store at -20°C. Avoid repeated freeze and thaw cycles. |
| Gene : | CASP8 |
| Gene ID : | 841 |
| Uniprot ID : | Q14790 |
| Alternative Name : | Apoptotic cysteine protease, Apoptotic protease Mch-5, CAP4, FADD-homologous ICE/ced-3-like protease, FADD-like ICE, ICE-like apoptotic protease 5, MORT1-associated ced-3 homolog, MCH5 |
| Immunogen Information : | A peptide sequence of the C-terminus of human Caspase-8 (PQPTFTLRKKLVFPSD) was used as immunogen for this antibody |
Apoptosis, or programmed cell death, is a common property of all multicellular organisms. The current dogma of apoptosis suggests that the components of the core cell-death machinery are integral to cells and widely conserved across species. Caspases, a family of cysteinyl aspartate-specific proteases, are integral components of the cell death machinery (reviewed in Siegal, 2006; and Lavrik et al, 2005). They play a central role in the initiation and execution of apoptotic cell death and in inflammation. Caspases are typically divided into 3 major groups, depending on the structure of their prodomain and their function. Group 1: inflammatory caspases (caspases 1, 4, 5, 11, 12, 14). Group II: initiator of apoptosis caspases (caspases 2, 8, 9). Group II: effector caspases (caspases 3, 6, 7). Caspases are constitutively expressed in almost all cell types as inactive proenzymes (zymogens: enzyme precursors which require a biochemical change to become active enzymes) that are processed and activated in response to a variety of pro-apoptotic or inflammatory stimuli. The procaspases (32-56 kDa) contain four domains: an N-terminal prodomain (2-25 kDa), a large subunit (p20: 17-21 kDa), a small subunit (p10: 10-13 kDa) and a short linker region between the large and small subunits. Caspase activation involves proteolytic processing of the proenzyme at specific aspartate residues between the domains. This results in removal of the prodomain as well as the linker region and formation of a heterodimer containing one large and one small subunit (p20-p10). The active caspase is a tetramer composed of two heterodimers (p202-p102). Active caspases mediate cell death and inflammation through cleavage of particular cellular substrates that are involved in these processes.The antisera recognizes caspase-8 forms that contain the peptide immunogen sequence (PQPTFTLRKKLVFPSD).
WB: 1:1000-1:2000, IHC (paraffin): 1:1000-1:5000, IHC (frozen): Users should optimize, IP: 1:50-1:200
For Research Use Only. Not for use in diagnostic/therapeutics procedures.
| Subcellular location: | Cytoplasm |
| Post transnational modification: | 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. |
| Tissue Specificity: | 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. |
| BioGrid: | 107291. 153 interactions. |
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