Polyclonal antibody to Caspase-9

Apoptosis is related to many diseases and induced by a family of cell death receptors and their ligands. Cell death signals are transduced by death domain containing adapter molecules and members of the caspase family of proteases. A novel member in the caspase family was recently identified and designated ICE-LAP6, Mch6, and Apaf-3. Caspase-9 and Apaf-1 bind to each other, which leads to caspase-9 activation. Caspase-9 is also activated by granzyme B and CPP32. Activated caspase-9 cleaves and activates caspase-3 that is one of the key proteases, being responsible for the proteolytic cleavage of many key proteins in apoptosis. Caspase-9 play a central role in cell death induced by a wide variety of apoptosis activators including TNFalpha, TRAIL, anti-CD-95, FADD, and TRADD. Caspase-9 is expressed in a variety of human tissues. The Cleaved Caspase-9 polyclonal antibody preferntially recognizes (active) cleaved Caspase-9. Whereas the antibody has a strong preference for (active) cleaved Caspase-9, in some cell or tissue systems or techniques the antibody may also recognize the pro form of Caspase-9.

WB: 1:1000-1:2000, IHC (paraffin): 1:1000-1:5000, IHC (frozen): Users should optimize, IP: 1:50-1:200

For Research Use Only. Not for use in diagnostic/therapeutics procedures.

Post transnational modification:	Phosphorylated at Thr-125 by MAPK1/ERK2. Phosphorylation at Thr-125 is sufficient to block caspase-9 processing and subsequent caspase-3 activation. Phosphorylation on Tyr-153 by ABL1/c-Abl; occurs in the response of cells to DNA damage.
Tissue Specificity:	Ubiquitous, with highest expression in the heart, moderate expression in liver, skeletal muscle, and pancreas. Low levels in all other tissues. Within the heart, specifically expressed in myocytes.
BioGrid:	107292. 37 interactions.

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