Programmed cell death via apoptosis is a key controlled physiological process instigated by the cell death receptor family, their ligands, and the caspase cysteine protease family. All caspases exist in a precursor form that contains a prodomain, and large and small catalytic subunits. A cleavage event adjacent to an aspartate liberates one large and one small subunit, which are now free to associate into an active a2b2 tetramer. Caspases are activated by triggers such as ligand-receptor interactions, growth factor deprivation, and cell function inhibitors. Caspase 8 is the directly connection between CD95 activation and the caspase network, and caspase 8 overexpression causes apoptosis.
Immunohistochemistry-Paraffin: Caspase 8 Antibody [NBP1-05123] - Formalin-fixed, paraffin-embedded sections from a brain tumor tissue array stained for Caspase-8 expression using NBP1-05123 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.
The Caspase 8 antibody was used by Niu et al to characterize the role of the death receptor 5 (DR5) in the developing CNS, where they found that DR5 exhibits very selective and specific expression in a subset of neuroprogenitor cells and newborn neurons (1). Experiments with Caspase 8 antibody enabled Schultz’s group at the Henry Ford Hospital to investigate the importance the AKT pathway and SPARC inhibitors in glioma cell tumor survival, and their possible use as treatment regimens for aggressive cases with poor outcomes (2). Their promising early data indicates that a combination of HSP27 and pAKT is more effective than current temozolomide (TMZ) therapy. Studies out of Hermel's group on the autosomal dominant progressive disorder Huntington’s disease (HD) used the Caspase 8 antibody to exclude the role of a subset of caspases (3, 8, and 9) in HD-associated neuronal death (3). Recent work from Kasloff et al relied upon immunofluorescence with the Caspase 8 antibody to examine the potential of using the avian influenza virus (IAV) as a therapeutic in pancreatic ductal adenocarcinoma (PDA) (4). Their intriguing data indicates that slightly pathogenic IAVs can virally replicate upon seeding in the proper cell subtype, and that these IAVs cause apoptosis and slow down tumor progression. Additional Caspase 8 antibody immunohistochemical studies were performed in Herold’s lab from the Hanover Medical School, where they established and validated a novel extracorporeal perfusion bioreactor system that is useful for visually and biochemically assessing fat cell viability and apotosis (5).
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