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LMNA Antibody (Center) Blocking Peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
| Primary Accession | P02545 |
|---|---|
| Clone Names | 90625006 |
| Gene ID | 4000 |
|---|---|
| Other Names | Prelamin-A/C, Lamin-A/C, 70 kDa lamin, Renal carcinoma antigen NY-REN-32, LMNA, LMN1 |
| Format | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
| 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. |
| Name | LMNA |
|---|---|
| Synonyms | LMN1 |
| Function | [Lamin-A/C]: Lamins are intermediate filament proteins that assemble into a filamentous meshwork, and which constitute the major components of the nuclear lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear membrane (PubMed:2344612, PubMed:2188730, PubMed:24741066, PubMed:10080180, PubMed:10580070, PubMed:10587585, PubMed:10814726, PubMed:11799477, PubMed:12075506, PubMed:12927431, PubMed:15317753, PubMed:18551513, PubMed:18611980, PubMed:22431096, PubMed:23666920, PubMed:31434876, PubMed:31548606, PubMed:37788673, PubMed:37832547). Lamins provide a framework for the nuclear envelope, bridging the nuclear envelope and chromatin, thereby playing an important role in nuclear assembly, chromatin organization, nuclear membrane and telomere dynamics (PubMed:24741066, PubMed:10080180, PubMed:10580070, PubMed:10587585, PubMed:10814726, PubMed:11799477, PubMed:12075506, PubMed:12927431, PubMed:15317753, PubMed:18551513, PubMed:18611980, PubMed:22431096, PubMed:23666920, PubMed:31548606, PubMed:37788673, PubMed:37832547). Lamin A and C also regulate matrix stiffness by conferring nuclear mechanical properties (PubMed:25127216, PubMed:23990565). The structural integrity of the lamina is strictly controlled by the cell cycle, as seen by the disintegration and formation of the nuclear envelope in prophase and telophase, respectively (PubMed:2344612, PubMed:2188730). Lamin A and C are present in equal amounts in the lamina of mammals (PubMed:10080180, PubMed:10580070, PubMed:10587585, PubMed:10814726, PubMed:11799477, PubMed:12075506, PubMed:12927431, PubMed:15317753, PubMed:18551513, PubMed:18611980, PubMed:22431096, PubMed:23666920, PubMed:31548606). Also invoved in DNA repair: recruited by DNA repair proteins XRCC4 and IFFO1 to the DNA double-strand breaks (DSBs) to prevent chromosome translocation by immobilizing broken DNA ends (PubMed:31548606). Required for normal development of peripheral nervous system and skeletal muscle and for muscle satellite cell proliferation (PubMed:10080180, PubMed:10814726, PubMed:11799477, PubMed:18551513, PubMed:22431096). Required for osteoblastogenesis and bone formation (PubMed:12075506, PubMed:15317753, PubMed:18611980). Also prevents fat infiltration of muscle and bone marrow, helping to maintain the volume and strength of skeletal muscle and bone (PubMed:10587585). Required for cardiac homeostasis (PubMed:10580070, PubMed:12927431, PubMed:23666920, PubMed:18611980). |
| Cellular Location | Nucleus lamina. Nucleus envelope. Nucleus, nucleoplasm. Nucleus matrix. Note=Farnesylation of prelamin-A/C facilitates nuclear envelope targeting and subsequent cleavage by ZMPSTE24/FACE1 to remove the farnesyl group produces mature lamin-A/C, which can then be inserted into the nuclear lamina (PubMed:15317753) EMD is required for proper localization of non-farnesylated prelamin- A/C (PubMed:19323649). Also localizes to the micronuclear envelope in response to response to genome instability (PubMed:37788673) |
| 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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Provided below are standard protocols that you may find useful for product applications.
Background
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.
References
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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