This purified rabbit CASP3 [D175] monoclonal antibody is specific for the cleaved (active) form of caspase 3. CASP3 [D175] is encoded by the 836 gene, also known as caspase 3, apoptosis-related cysteine peptidase, CPP32, SCA-1, CPP32B. Rabbit anti-CASP3 [D175] monoclonal antibody is used in western blotting, flow cytometry, immunohistochemistry, and immunofluorescence.

Antibody Specifications:

Applications: Validated applications for anti-CASP3 [D175] monoclonal antibody are western blotting, flow cytometry, immunofluorescence, and immunohistochemistry.
Host Species and Isotype: The host species and isotype of the antibody is rabbit IgG.
Clone ID of Monoclonal Antibody (mAb): The anti-CASP3 [D175] monoclonal antibody clone is 9H19L2.
Reactivity: Reacts with human CASP3 [D175].
Product Size: Rabbit anti-CASP3 [D175] monoclonal antibody is available in a 100 µg size.

Caspases are a family of cysteine proteases that centrally controls apoptotic machinery (1). Caspases can be grouped according to their substrate specificities that are largely determined by the amino acids preceding the cleavage site. One group of caspases that include -6, -8, (MACH/FLICE), and -9(V/LEXD) is specific for the substrate V/LEXD. This substrate is a site similar to those found in caspase proenzymes. This group of caspases may function as initiators of a proteolytic cascade by activating pro-caspases to amplify a death signal. A second group of caspases (-2, -3 and -7) is specific for the substrate DEXD that is related to sites found on target proteins cleaved during apoptosis.

Caspase-3 (also known as CPP32, Yama or Apopain) is a member of the interleukin-1β converting enzyme (ICE) family of cysteine proteases. Caspase-3 exists in cells as an inactive 32 kDa proenzyme, called pro-Caspase-3. Pro-Caspase-3 is cleaved into active 17 and 12 kDa subunits by upstream proteases such as Caspase-6 (Mch2), Caspase-8 (FLICE) and Granzyme B during apoptosis. The downstream substrates of Caspase-3 include poly-ADP ribose polymerase (PARP), sterol regulatory element binding proteins (SREBPs), nuclear lamins and others. The overexpression of Caspase-3 can result in apoptosis. Likewise, the inhibition of Caspase-3 or other caspases can prevent cells from entering the apoptotic pathway. Recent evidence has revealed a link between plasma caspase-3 and atherosclerosis, and its role in activation of apoptosis in breast cancer mediated by siRNA-mediated Apollon silencing. This antibody is specific for the cleaved (active) form of caspase-3.