Caspase-2 (CASP2) Antibody – Rabbit Polyclonal

This gene encodes a member of the cysteine-aspartic acid protease (caspase) family. Caspases mediate cellular apoptosis through the proteolytic cleavage of specific protein substrates. The encoded protein may function in stress-induced cell death pathways, cell cycle maintenance, and the suppression of tumorigenesis. Increased expression of this gene may play a role in neurodegenerative disorders including Alzheimer's disease, Huntington's disease and temporal lobe epilepsy. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene. [provided by RefSeq, Jan 2011]

CASP2: Involved in the activation cascade of caspases responsible for apoptosis execution. Might function by either activating some proteins required for cell death or inactivating proteins necessary for cell survival. Heterotetramer that consists of two anti-parallel arranged heterodimers, each one formed by a p18 subunit and a p12 subunit. Interacts with LRDD. Expressed at higher levels in the embryonic lung, liver and kidney than in the heart and brain. In adults, higher level expression is seen in the placenta, lung, kidney, and pancreas than in the heart, brain, liver and skeletal muscle. Belongs to the peptidase C14A family. 2 isoforms of the human protein are produced by alternative splicing.

Protein type: EC 3.4.22.55; Apoptosis; Protease

Chromosomal Location of Human Ortholog: 7q34-q35

Cellular Component: membrane; mitochondrion; cytoplasm; cytosol; nucleus

Molecular Function: protein domain specific binding; protein binding; enzyme binding; cysteine-type endopeptidase activity

Biological Process: luteolysis; nerve growth factor receptor signaling pathway; positive regulation of apoptosis; apoptosis; germ cell programmed cell death; regulation of caspase activity; proteolysis; DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; DNA damage response, signal transduction resulting in induction of apoptosis; positive regulation of neuron apoptosis; protein processing; brain development; aging