Cleaved Lamin A (Asp230) Antibody detects endogenous levels of the large fragment of lamin A (and lamin C isotype) resulting from cleavage at aspartic acid 230. The antibody does not recognize full length lamin A.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to carboxy-terminal residues surrounding Asp230 in human lamin A. Antibodies are purified by protein A and peptide affinity chromatography.
Background
Lamins are nuclear membrane structural components that are important in maintaining normal cell functions such as cell cycle control, DNA replication and chromatin organization (1-3). Lamin A/C is cleaved by caspase-6 and serves as a marker for caspase-6 activation. During apoptosis, lamin A/C is specifically cleaved into a large (41-50 kDa) and a small (28 kDa) fragment (3,4). The cleavage of lamins results in nuclear disregulation and cell death (5,6).