Anti-ACP3 | Activated Caspase 3 (p20/p17 subunit)

Anti-ACP3 | Activated Caspase 3 (p20/p17 subunit)

• Background: Caspasesare a family of cysteine proteases which play essential roles in apoptosis. Among them, Caspase 3 is a frequently activated death protease, catalyzing the specific cleavage of many key cellular proteins. Caspase 3 is synthesized as an inactive 32 kDa pro-enzyme which undergo proteolytic processing in response to apoptotic stimulation to produce the active form which consists of the p20/p17, and p12 subunits. Caspase 3 is the predominant caspase involved in the cleavage of Alzheimer amyloid precursor protein (APP), which is associated with neuronal death in Alzheimer ‘s disease. An antibody (named ACP3) against activated caspase 3 was raised in rabbit. This antibody recognizes the active form of human caspase 3, p20/p17 subunit but does not recognize the proenzyme p32.
• CAS Number: 9007-83-4
• Host: Rabbit
• Reactivity: Human, Mouse and Rat
• Immunogen: KLH-conjugated synthetic peptide corresponding to the human caspase 3 cleavage site, 6 aa (CGIETD) UniProt:P42574
• Applications: ELISA (ELISA), Immunolocalisation (IL), Western blot (WB)
• Dilution: 1: 500 - 1: 1000 (IL), 1:3000-1:1000 (WB)
• Purity: Serum. Contains 0.05% sodium azide.
• Format: Liquid
• Molecular Weight: 31.6 | 17 and 19 kDa
• Precautions: The antibody does not react with the proenzyme p32
• References & Citations: Nishimuraet al (2003). Upregulation and antiapoptotic role of endogenous Alzheimer amyloid precursor protein in dorsal root ganglion neurons. Exp Cell Res. 2003 Jun 10;286(2):241-51. doi: 10.1016/s0014-4827(03)00066-1. PMID: 12749853.Nishimuraet al. (2002) Cell death induced by a caspase-cleaved transmembrane fragment of the Alzheimer amyloid precursor protein. Cell Death Differ. 2002 Feb;9(2):199-208. doi: 10.1038/sj.cdd.4400931. PMID: 11840170.
• Storage Conditions: Store at -20°C; make aliquots to avoid repeated freeze-thaw cycles. Please remember to spin the tubes briefly prior to opening them to avoid any losses that might occur from material adhering to the cap or sides of the tube.