Caspase-3

GWB-64E687

A synthetic peptide corresponding to residues in p17 subunit of human Caspase-3 was used as immunogen. The antibody should recognize both pro-form (35kDa) and p17 cleaved-form of Caspase-3.

WB: 1:5 000IHC: 1:25-1:50ICC: 1:25IP: 1:10. Caspases are a family of cytosolic aspartate-specific cysteine proteases involved in the initiation and execution of apoptosis. Caspase-3 (apopain SCA-1 Yama and CPP32) is a member of the apoptosis execution functional group of caspases and is either partially or totally responsible for the proteolytic cleavage of many key proteins during apoptosis such as poly (ADP-ribose) polymerase (PARP) (1 2 3). Caspase-3 is a cytosolic protein found in cells as an inactive 32 kDa proenzyme. It is activated by proteolytic cleavage into two active subunits only when cells undergo apoptosis (3). 1. Zhao Y Herdegen T Cerebral ischemia provokes a profound exchange of activated JNK isoforms in brain mitochondria Mol Cell Neurosci 41 (2009) 186-195[Application: WB IP]2. Tanaka K Hashimoto H Tachibana T et al Apoptosis in the small intestine of neonatal rat using blue light-emitting diode devices and conventional halogen-quartz devices in phototherapy Pediatr Surg Int 24 (2008) 837-842[Application: IHC]1. Fernandes-Alnemri T. et al. CPP32 a novel human apoptotic protein with homology to Caenorhabditis elegans cell death protein Ced-3 and mammalian interleukin-1 beta-converting enzyme. J. Biol. Chem. 269:307612. Tewari M. et al. Yama/CPP32 beta a mammalian homolog of CED-3 is a CrmA-inhibitable protease that cleaves the death substrate poly(ADP-ribose) polymerase. Cell 81: 8013. Nicholson D. W. et al. Identification and inhibition of the ICE/CED-3 protease necessary for mammalian apoptosis. Nature 376: 374. Manufactured under U. S. Patents No. 5 675 063 and 7 429 487