Each lot of this antibody is quality control tested by Western blotting. Western blotting, suggested working dilution(s): Use 5 μg antibody per 5 ml antibody dilution buffer for each mini-gel. It is recommended that the reagent be titrated for optimal performance for each application.
A431 cell extract was resolved by electrophoresis, transferred to nitrocellulose and probed with monoclonal anti-caspase 9 antibody. Proteins were visualized using a goat anti-mouse secondary antibody conjugated to HRP and a chemiluminescence system.
Description:
Caspase 9 (also known as ICE-like apoptotic protease 6 (ICE-LAP6), apoptotic protease Mch-6, and apoptotic protease activating factor 3 (Apaf-3)) is a member of the peptidase family C14 that contains a CARD domain. This caspase is active as a heterotetramer and has been reported to have two isoforms. Pro-Caspase 9 has been reported to be approximately 47 kD. This caspase is present in the cytosol and, upon activation, translocates to the mitochondria. Caspase 9 is involved in the caspase activation cascade responsible for apoptosis execution and cleaves/activates Caspase 3 and Caspase 6. Caspase 9 is inhibited by the dominant negative isoform, Bcl-XL, c-IAP1, c-IAP2, XIAP, and Livin. This caspase becomes activated when recruited to Apaf-1/cytochrome c complex, and following cleavage by Apaf-1, granzyme B, Caspase 3, possibly Caspase 8 and Caspase 10 into large p37 and small p10 subunits. Caspase 9 interacts with BIRC7 and has been shown to cleave PARP and vimentin. The 96-2-22 monoclonal antibody has been shown to be useful for Western blotting of human caspase 9 (46 kD pro-caspase 9 as well as the 34 kD cleaved caspase 9).
Peptidase family C14, CARD domain. Heterotetramer, two isoforms, pro-Casp9 47 kD, active cleaved from Casp9 37 kD
Distribution:
Cytoplasm, when activated mitochondrial
Function:
Involved in caspase activation cascade responsible for apoptosis execution; cleaves/activates Casp3, Casp6
Regulation:
Inhibited by dominant negative isoform, Bcl-XL, c-IAP1, c-IAP2, XIAP, Livin. Activated when recruited to Apaf-1/cytochrome c complex, cleaved by Apaf-1, granzyme B, Casp3, possibly Casp8 and -10 into large p37 and small p10 subunits
Interaction:
BIRC7; cleaves PARP, vimentin
Antigen References:
1. Srinivasula, S., et al., 1996. J. Biol. Chem. 271:27099. 2. Hu, Y., et al., 1998. PNAS 95:4386. 3. Sitailo, L., et al., 2002. J. Biol. Chem. 277:19346. 4. Potokar, M., et al., 2003. FEBS Lett. 544:153.
*These products may be covered by one or more Limited Use Label Licenses (see the BioLegend Catalog or our website, www.biolegend.com/ordering/). BioLegend products may not be transferred to third parties, resold, modified for resale, or used to manufacture commercial products or to provide a service to third parties without written approval of BioLegend. By use of these products you accept the terms and conditions of all applicable Limited Use Label Licenses. Unless otherwise indicated, these products are for research use only and are not intended for human or animal diagnostic, therapeutic or commercial use.
