|Application ||WB, IHC-P, FC, E|
|Calculated MW||50685 Da|
|Antigen Region||198-226 aa|
|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||This CASP2 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 198-226 amino acids from the Central region of human CASP2.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||CASP2 Antibody (Center) is for research use only and 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.|
|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 press
Shi,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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