Anti-Caspase-3 CASP3 Antibody

Caspases are a family of cysteine proteases that can be divided into the apoptotic and inflammatory caspase subfamilies. Unlike the apoptotic caspases, members of the inflammatory subfamily are generally not involved in cell death but are associated with the immune response to microbial pathogens. The apoptotic subfamily can be further divided into initiator caspases, which are activated in response to death signals, and executioner caspases, which are activated by the initiator caspases and are responsible for cleavage of cellular substrates that ultimately lead to cell death. Caspase-3 is synthesized as an inactive proenzyme that undergoes proteolytic cleavage by caspases 8, 9 and 10 to produce 2 subunits, termed p20 and p11. These subunits dimerize to form the active enzyme. Caspase-3 proteolytically cleaves and activates other proteins such as caspases 6, 7 and 9.

Caspase-3 antibody was raised against a 17 amino acid synthetic peptide near the center of human Caspase-3. The immunogen is located within amino acids 70 - 120 of Caspase-3.

Highly expressed in lung, spleen, heart, liver and kidney. Moderate levels in brain and skeletal muscle, and low in testis. Also found in many cell lines, highest expression in cells of the immune system.

Involved in the activation cascade of caspases responsible for apoptosis execution. At the onset of apoptosis it proteolytically cleaves poly (ADP-ribose) polymerase (PARP) at a '216-Asp-

Caspase-3 antibody can be stored at 4°C for three months and -20°C, stable for up to one year. Avoid repeated freeze-thaw cycles. Antibodies should not be exposed to prolonged high temperatures.