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Caspase-9 (Active) Antibody

based on 5 citations in multiple journalsCaspase-9 (Active) Antibody54.1 4
Catalog #: 3149
$425.00

Product Details

Cat # +Size 3149-100
Size 100 µg
Antibody Target Caspase-9 (Active)
Host Rabbit
Antibody Type Polyclonal
Isotype Rabbit IgG
Immunogen Synthetic peptide mapping to the N-terminus adjacent to Asp330 of human caspase-9
Accession # P55211
Gene ID 12371
Appearance Colorless liquid
Concentration 0.2 mg/ml
Formulation 100 µg (0.2 mg/ml) affinity purified rabbit polyclonal antibody in phosphate-buffered saline (PBS) containing 50% glycerol, 0.5% BSA, and 0.02% thimerosal.
Purification Affinity purified
Species Reactivity Human
Application Western blot, Immunoprecipitation
Application & Usage Western blotting (0.5-4 µg/ml) and immunoprecipitation (10-20 µg/ml). However, the optimal concentrations should be determined individually. The anti-active caspase-9 antibody recognizes only the cleaved caspase-9 (37 kDa). It does not recognize full-leng
Handling The antibody solution should be gently mixed before use.
Storage Conditions -20 °C
Shipping Conditions Gel Pack
USAGE For Research Use Only! Not For Use in Humans.

Details

Caspases are synthesized as inactive pro-enzymes that are processed to active form in cells undergoing apoptosis. Caspase-9 is an important member of the caspase family. Upon induction of apoptosis, Cytochrome c released from mitochondria associates with pro-caspase-9 (47 kDa) and Apaf-1. The complex processes pro-caspase-9 into a large subunit (37 kDa/17 kDa) and a small subunit (10 kDa). Cleaved caspase-9 further processes other caspases including caspase-3 and caspase-6, to initiate a caspase cascade leading to apoptosis. The affinity purified antibody recognizing the active forms of caspase-9 provides a new tool for identifying apoptotic cell populations in both tissue sections and cultured cells.


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Kasloff et al., Oncolytic Activity of Avian Influenza Virus in Human Pancreatic Ductal Adenocarcinoma Cell Lines. J. Virol., Aug 2014; 88: 9321 - 9334.
Schwartz, J. et al. Francisella tularensis Inhibits the Intrinsic and Extrinsic Pathways To Delay Constitutive Apoptosis and Prolong Human Neutrophil Lifespan, J. Immunol., Apr 2012; 188: 3351 - 3363.
Singh S et al (2009) Mol. Cancer Ther.; 8: 178 - 184.
Scarabelli, T.M. et al. (2004) J. Thorac. Cardiovasc. Surg. 128: 364-371.
Scarabelli, T.M. et al. (2002) Circ. Res. 90:745-748.
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