Product name: Anti-caspase-3 antibody
Description: Polyclonal rabbit to Caspase-3
Host species: Rabbit
Caspase-3 is a member of the interleukin-1 converting enzyme family. Caspase-3 is believed to be associated with the induction of apoptosis. Caspase-3 is synthesized as an inactive 32 kDa proenzyme and processed during apoptosis generating two subunits of 17 kDa and 12 kDa. Caspase-3 stains skin epithelial cells, proximal renal tubules, and collecting ducts. This antibody reacts with the 32 kDa proenzyme and the active 17 kDa form of caspase 3.
Suitable for: WB, IHC-P
Reacts with: Human
A synthetic peptide corresponding to Human Caspase-3 aa 167-175. Corresponding to the human caspase 3 cleavage site.
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Involved in the caspase activation cascade responsible for the execution of apoptosis. At the onset of apoptosis, it proteolytically cleaves poly (ADP-ribose) polymerase (PARP) at a ‘216-Asp-Gly-217 ‘link. It cleaves and activates the sterol regulatory element-binding proteins (SREBPs) between the basic helix-loop-helix leucine zipper domain and the membrane-binding domain. Cleavage and activate caspase-6, -7, and -9. Involved in huntingtin cleavage.
Highly expressed in the lung, spleen, heart, liver, and kidney. Moderate levels in the brain and skeletal muscle and low in testes. It is also found in many cell lines, the highest expression in the cells of the immune system.
It belongs to the C14A peptidase family.
Cleavage by granzyme B, caspase-6, caspase-8, and caspase-10 generates the two active subunits. Additional processing of the propeptides is likely due to the autocatalytic activity of the activated protease. Active heterodimers also appear between the small subunit of caspase-7 protease and the large subunit of caspase-3 and vice versa.
S-nitrosylated at its catalytic site cysteine in unstimulated human cell lines and denitrosylated after activation of the apoptotic Fas pathway, associated with an increase in intracellular caspase activity. Thus, Fas activates caspase-3 not only by inducing caspase zymogen cleavage into its active subunits but also by stimulating denitrosylation of its thiol active site.