Lamin A is a member of the intermediate filament family that contains a farnesyl binding domain and forms dimers. Three isoforms of Lamin A have been reported designated A, AD10, C, with molecular weights of approximately 70 kD, 66 kD, and 61 kD, respectively. Lamin A is localized to the nucleoplasmic side of inner nuclear membrane. Lamin A is thought to function as a fibrous component of the nuclear lamina, providing a framework for the nuclear envelope, and possibly interacting with chromatin. Expression of lamin A is strictly under cell cycle control as seen by disintegration/formation of nuclear envelope in prophase/telophase. Lamin A is modified by phosphorylation, methylation, and farnesylation; phosphorylation regulates disassembly. Lamin A forms a homodimer with Lamin C and has also been shown to interact with the LAPs 1A-1C, emerin, Narf, hsMOK2, PKC, SREBP1a, and SREBP 1c. The Poly6135 antibody recognizes the C-terminal region of human and mouse Lamin A and has been shown to be useful for Western blotting and immunofluorescence staining.