Clone: MCH3-5
Background: Caspases are key effectors of programmed cell death. Caspase-7 along with caspase 3 and 6 form the group of effector caspases that are responsible for the cleavage of multiple substrates including the cytokeratins, PARP, alpha fodrin, NuMA and others. Caspase-7 is a 303 amino acid protein with high similarity to caspase-3. Caspase-7 occurs in three varient forms. Granzyme B activates pro-caspase-7 to a form which can cleave poly(ADP-ribose) polymerase (PARP) to its signature fragment of ~85 kDa. Also, in vivo caspase-7 appears to be a better substrate for granzyme B than caspase-3. Pro-caspase-7 has been shown to exist as dimers or high order oligomers. Caspase-7 may be an important intracellular effector of granzyme B-mediated apoptosis and cytotoxic T-lymophocyte-induced cell killing in vivo.
Positive Control: MCF-7 cell line
Immunogen: Hybridoma produced by the fusion of splenocytes from mice immunized with recombinant human caspase-7 protein and mouse myeloma cells.
Purification Method: Ammonium Sulfate Precipitation
Concentration: See vial for concentration
Formulation: Provided as solution in phosphate buffered saline with 0.08% sodium azide
References: 1. Cohen, G.M., et al. Caspases: the executioners of apoptosis. Biochem. J. 1997, 326, 1-162. Chandler, J.M., et al. Different subcellular distribution of Caspase-3 and Caspase-7 following Fas-induced apoptosis in mouse liver. J. Bio. Chem. 1998, 273, 10815-108183. Behrensdorf, H.A., et al. The endothelial monocyte-activating polypeptide II (EMAP II) is a substrate for caspase-7. FEBS Lett. 2000, 466, 143-147
UniProt: P55210
Caution: This product is intended FOR RESEARCH USE ONLY, and FOR TESTS IN VITRO, not for use in diagnostic or therapeutic procedures involving humans or animals.
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