Anti-Caspase-3 Antibody Picoband® (monoclonal, 8B6)

Caspase 3 is a caspase protein which interacts with Survivin, XIAP, CFLAR, Caspase 8, HCLS1, Deleted in Colorectal Cancer, TRAF3 and GroEL. This gene which is located on 4q35 encodes a protein that is 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 that undergo proteolytic processing at conserved aspartic residues to produce two subunits, large and small, that dimerize to form the active enzyme. It is the predominant caspase involved in the cleavage of amyloid-beta 4A precursor protein, which is associated with neuronal death in Alzheimer's disease. And the caspase-3 activation in heart failure sequentially cleaves SRF and generates a truncated SRF that appears to function as a dominant-negative transcription factor. Additionally, the caspase-3 influence on bone mineral density should be considered in any in vivo application of caspase-3 inhibitors to the treatment of human disease. In erythroid precursors undergoing terminal differentiation, Hsp70 prevents active CASP3 from cleaving GATA1 and inducing apoptosis.

E.coli-derived human Caspase-3 recombinant protein (Position: T67-D175) . Human Caspase-3 shares 86% and 90% amino acid (aa) sequence identity with mouse and rat Caspase-3, respectively.

Highly expressed in lung, spleen, heart, liver and kidney. Moderate levels in brain and skeletal muscle, and low in testis. Also found in many cell lines, highest expression in cells of the immune system.

Alzheimer's Disease, Apoptosis, Apoptotic Markers, Cancer, Caspases, Cell Biology, Cell Death, Intracellular, Invasion/Microenvironment, Neurodegenerative Disease, Neurology Process, Neuroscience

Involved in the activation cascade of caspases responsible for apoptosis execution. At the onset of apoptosis it proteolytically cleaves poly (ADP-ribose) polymerase (PARP) at a 216-Asp-|-Gly-217 bond. Cleaves and activates sterol regulatory element binding proteins (SREBPs) between the basic helix-loop-helix leucine zipper domain and the membrane attachment domain. Cleaves and activates caspase-6, -7 and -9. Involved in the cleavage of huntingtin. Triggers cell adhesion in sympathetic neurons through RET cleavage.

1.Chang, J.; Wei, L.; Otani, T.; Youker, K. A.; Entman, M. L.; Schwartz, R. J. : Inhibitory cardiac transcription factor, SRF-N, is generated by caspase 3 cleavage in human heart failure and attenuated by ventricular unloading. Circulation 108: 407-413, 2003. 2.Miura, M.; Chen, X.-D.; Allen, M. R.; Bi, Y.; Gronthos, S.; Seo, B.-M.; Lakhani, S.; Flavell, R. A.; Feng, X.-H.; Robey, P. G.; Young, M.; Shi, S. : A crucial role of caspase-3 in osteogenic differentiation of bone marrow stromal stem cells. J. Clin. Invest. 114: 1704-1713, 2004. 3.Ribeil, J.-A.; Zermati, Y.; Vandekerckhove, J.; Cathelin, S.; Kersual, J.; Dussiot, M.; Coulon, S.; Moura, I. C.; Zeuner, A.; Kirkegaard-Sorensen, T.; Varet, B.; Solary, E.; Garrido, C.; Hermine, O. : Hsp70 regulates erythropoiesis by preventing caspase-3-mediated cleavage of GATA-1. Nature 445: 102-105, 2007.

Store at -20°C for one year from date of receipt. After reconstitution, at 4°C for one month. It can also be aliquotted and stored frozen at -20°C for six months. Avoid repeated freeze-thaw cycles.