Lamin A/C Recombinant Rabbit Monoclonal Antibody [JE51-60] (ET7110-12)

UNIPROT #

P02545

PROTEIN NAME

Lamin A/C

SYNONYMS

70 kDa lamin antibody;Cardiomyopathy dilated 1A (autosomal dominant) antibody;CDCD1 antibody;CDDC antibody;CMD1A antibody;CMT2B1 antibody;EMD2 antibody;FPL antibody;FPLD antibody;FPLD2 antibody;HGPS antibody;IDC antibody;Lamin A antibody;Lamin A/C antibody;Lamin A/C like 1 antibody;Lamin antibody;Lamin C antibody;Lamin-A/C antibody;LDP1 antibody;LFP antibody;LGMD1B antibody;Limb girdle muscular dystrophy 1B (autosomal dominant) antibody;LMN 1 antibody;LMN A antibody;LMN C antibody;LMN1 antibody;LMNA antibody;LMNA_HUMAN antibody;LMNC antibody;LMNL1 antibody;Prelamin A/C antibody;PRO1 antibody;Renal carcinoma antigen NY REN 32 antibody;Renal carcinoma antigen NY-REN-32 antibody;Renal carcinoma antigen NYREN32 antibody

SEQUENCE SIMILARITIES

Belongs to the intermediate filament family.

TISSUE SPECIFICITY

In the arteries, prelamin-A/C accumulation is not observed in young healthy vessels but is prevalent in medial vascular smooth muscle cells (VSMCs) from aged individuals and in atherosclerotic lesions, where it often colocalizes with senescent and degenerate VSMCs. Prelamin-A/C expression increases with age and disease. In normal aging, the accumulation of prelamin-A/C is caused in part by the down-regulation of ZMPSTE24/FACE1 in response to oxidative stress.

POST-TRANSLATIONAL MODIFICATION

Increased phosphorylation of the lamins occurs before envelope disintegration and probably plays a role in regulating lamin associations.; Proteolytic cleavage of the C-terminal of 18 residues of prelamin-A/C results in the production of lamin-A/C. The prelamin-A/C maturation pathway includes farnesylation of CAAX motif, ZMPSTE24/FACE1 mediated cleavage of the last three amino acids, methylation of the C-terminal cysteine and endoproteolytic removal of the last 15 C-terminal amino acids. Proteolytic cleavage requires prior farnesylation and methylation, and absence of these blocks cleavage.; Sumoylation is necessary for the localization to the nuclear envelope.; Farnesylation of prelamin-A/C facilitates nuclear envelope targeting.

SUBCELLULAR LOCATION

Intermediate filament, Nucleus.

FUNCTION

A unique family of cysteine proteases has been described that differs in sequence, structure and substrate specificity from any previously described protease family. This family, termed Ced-3/ICE, is comprised of ICE, CPP32, ICH-1/Nedd-2, Tx, Mch2, Mch3 (ICE-LAP3 or CMH-1), Mch4 and ICE-LAP6. Ced-3/ICE family members function as key components of the apoptotic machinery and act to destroy specific target proteins which are critical to cellular longevity. Nuclear lamins are critical to maintaining the integrity of the nuclear envelope and cellular morphology. The nuclear Lamin A is cleaved by Mch2, but not CPP32. Nuclear Lamin B is fragmented as a consequence of apoptosis by an unidentified member of the ICE family. Lamin C is a splice variant of Lamin A, differing only at the carboxy-terminus. Lamins A and C are identical for the first 566 amino acids, with Lamin C differing only in six unique carboxy-terminal amino acids.