Anti-Caspase 8

Anti-Caspase 8

AB1853

Chemicon (Millipore)

AB1879 detects 55 and 43 kDa proteins, corresponding to the proform and large subunit of caspase-8. The antibody also detects human recombinant caspase-8 protein on SDS-PAGE immunoblots.

55 and 43 kDa

recombinant, full length, purified human caspase 8

Caspase-8 is a 55 kDa cytosolic protein that is synthesized as an inactive proenzyme. Activation of caspase-8 involves a two-step proteolysis: the cleavage of caspase-8 to generate a 43 kDa fragment and a 12 kDa which is further processed to 10 kDa, and then the p43 is then cleaved to yield p26 and the release of the active site containing p18.

• Bovine
• Human
• Mouse
• Monkey
• Rat

Western blot: 0.5 - 4 μg/mL

Optimal working dilutions must be determined by end user.

Skin/Tumor, Embryo

Immunoaffinity purified

Liquid in PBS, pH 7.2, containing 30% glycerol, 0.5% BSA and 0.01% thiomerosal. Affinity Purified immunoglobulin.

Maintain for 1 year at -20°C from date of shipment. Aliquot to avoid repeated freezing and thawing. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.

Q14790

• NM_001080124.1
• NM_001080125.1
• NM_001228.4
• NM_033355.3
• NM_033356.3
• NM_033358.3

• CASP8
• MGC78473
• CASP-8
• MACH
• procaspase-8
• MCH5
• ALPS2B
• FLICE
• CAP4
• EC 3.4.22.61 [Contains: Caspase-8 subunit p18
• Caspase-8 subunit p10].

MACH1; FLICE

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

Western Blotting

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. 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.

FUNCTION: SwissProt: Q14790 # 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. Isoforms 5, 6, 7 and 8 lack the catalytic site and may interfere with the pro-apoptotic activity of the complex.
SIZE: 479 amino acids; 55391 Da
SUBUNIT: 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.
SUBCELLULAR LOCATION: Cytoplasm.
TISSUE SPECIFICITY: Isoforms 1, 5 and 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.DOMAIN:SwissProt: Q14790 Isoform 9 contains a N-terminal extension that is required for interaction with the BCAP31 complex.
PTM: 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. & Phosphorylated upon DNA damage, probably by ATM or ATR.
DISEASE: SwissProt: Q14790 # Defects 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.
SIMILARITY: Belongs to the peptidase C14 family. & Contains 2 DED (death effector) domains.

Chemicon

Anti-Caspase 8

0.2 mg/mL

Polyclonal Antibody

50 μg

Affinity Purified

Rabbit