|Other Names||Caspase-2, CASP-2, Neural precursor cell expressed developmentally down-regulated protein 2, NEDD-2, Protease ICH-1, Caspase-2 subunit p18, Caspase-2 subunit p13, Caspase-2 subunit p12, CASP2, ICH1, NEDD2|
|Target/Specificity||The synthetic peptide sequence used to generate the antibody AP1327c was selected from the Center region of human CASP2. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.|
|Format||Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Function||Involved in the activation cascade of caspases responsible for apoptosis execution. Might function by either activating some proteins required for cell death or inactivating proteins necessary for cell survival (PubMed:15073321). Associates with PIDD1 and CRADD to form the PIDDosome, a complex that activates CASP2 and triggers apoptosis in response to genotoxic stress (PubMed:15073321).|
|Tissue Location||Expressed at higher levels in the embryonic lung, liver and kidney than in the heart and brain. In adults, higher level expression is seen in the placenta, lung, kidney, and pancreas than in the heart, brain, liver and skeletal muscle|
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Provided below are standard protocols that you may find useful for product applications.
CASP2 is a protein which 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. The protein exist as inactive proenzymes which undergo proteolytic processing at conserved aspartic residues to produce two subunits, large and small, that dimerize to form the active enzyme. The proteolytic cleavage of this protein is induced by a variety of apoptotic stimuli.
Lan,Q., Morton,L.M. Blood (2009) In pressShi,M., Vivian,C.J. Cell 136 (3), 508-520 (2009)Paroni,G., Henderson,C. J. Biol. Chem. 276 (24), 21907-21915 (2001)Tiso,N., Pallavicini,A. Biochem. Biophys. Res. Commun. 225 (3), 983-989 (1996)
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