|Other Names||Prelamin-A/C, Lamin-A/C, 70 kDa lamin, Renal carcinoma antigen NY-REN-32, LMNA, LMN1|
|Format||Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Function||Lamins are components of the nuclear lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear membrane, which is thought to provide a framework for the nuclear envelope and may also interact with chromatin. Lamin A and C are present in equal amounts in the lamina of mammals. Plays an important role in nuclear assembly, chromatin organization, nuclear membrane and telomere dynamics. Required for normal development of peripheral nervous system and skeletal muscle and for muscle satellite cell proliferation. Required for osteoblastogenesis and bone formation. Also prevents fat infiltration of muscle and bone marrow, helping to maintain the volume and strength of skeletal muscle and bone.|
|Cellular Location||Nucleus. Nucleus envelope. Nucleus lamina. Nucleus, nucleoplasm. Note=Farnesylation of prelamin-A/C facilitates nuclear envelope targeting and subsequent cleaveage by ZMPSTE24/FACE1 to remove the farnesyl group produces mature lamin- A/C, which can then be inserted into the nuclear lamina. EMD is required for proper localization of non-farnesylated prelamin-A/C|
|Tissue Location||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.|
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The nuclear lamina consists of a two-dimensional matrix ofproteins located next to the inner nuclear membrane. The laminfamily of proteins make up the matrix and are highly conserved inevolution. During mitosis, the lamina matrix is reversiblydisassembled as the lamin proteins are phosphorylated. Laminproteins are thought to be involved in nuclear stability, chromatinstructure and gene expression. Vertebrate lamins consist of twotypes, A and B. Through alternate splicing, this gene encodes threetype A lamin isoforms. Mutations in this gene lead to severaldiseases: Emery-Dreifuss muscular dystrophy, familial partiallipodystrophy, limb girdle muscular dystrophy, dilatedcardiomyopathy, Charcot-Marie-Tooth disease, and Hutchinson-Gilfordprogeria syndrome.
Bailey, S.D., et al. Diabetes Care 33(10):2250-2253(2010)Wegner, L., et al. J. Clin. Endocrinol. Metab. 95(8):3884-3892(2010)Drac, H., et al. Neurol. Neurochir. Pol. 44(3):291-296(2010)Liu, Q., et al. PLoS ONE 5 (5), E10874 (2010) :Chaturvedi, P., et al. PLoS ONE 5 (5), E10620 (2010) :
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