Caspase 3 is a cytosolic protein present as a 32 kDa proenzyme in cells. It is activated by proteolytic cleavage into the 20 kDa (p20) and 11 kDa (p11) active subunits when cells undergo apoptosis.
synthetic peptide corresponding to the N-terminal of human caspase 3 (amino acids 29-43 with C-terminally added lysine) conjugated to KLH. This sequence, unique to caspase 3, corresponds to N-terminal of the enzyme p20 subunit and is highly conserved in rat and mouse caspase 3.
Anti-Caspase 3 antibody produced in rabbit is suitable for microarray and western blotting at a working dilution of 1:3000 using Jurkat human T-cell leukemia cell extract. It was used as a primary antibody for western blotting in a study to establish the biomolecular basis for the role of PCMT1 (isoaspartyl protein carboxyl-O-methyltransferase) as a part of a novel apoptosis regulatory mechanism. It was used to examine activation of caspase-3 via immunoblotting in a study to confirm the apoptosis of tumor cells mediated by AAV-ISN-T (recombinant adeno-associated virus vector with signal peptides of human insulin) administration. It was used as a primary antibody at 1:300 dilution for immunohistochemistry of deparaffinized sections of squamous cell carcinoma of the tongue containing surrounding normal tissue. It was used at a dilution of 1:1000 to detect caspase-3 and its cleaved form P20 in a study.
Caspase 3 is one of the key executioners of apoptosis downstream in the apoptotic pathway, as it is activated in cells by various death signals. In some neurodegenerative diseases, such as Huntington disease (HD) and Alzheimer′s disease (AD), specific neuronal caspase substrates have been identified. In Huntington disease (HD), caspase 3 specifically cleaves the HD gene product, Huntingtin.
Caspase 3 cleaves many key proteins including poly(ADP-ribose) polymerase (PARP), sterol-regulatory element-binding proteins (SREBPs), DNA-dependent protein kinase (DNA-PK), α-fodrin, gelsolin, PKCd and DFF45/ICAD during apoptosis. High levels of this enzyme in lymphocytes suggest that it is an important mediator of apoptosis in the immune system. Deletion of CASP-3 gene in mice results in hyperplasia and cell abnormalities, indicating that caspase 3 is essential for morphogenetic cell death during normal brain development.
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.
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