||WB, IHC, IF, IP
||Human, Mouse, Rat
||Rabbit polyclonal anti-Lamin A/C antibody is suitable for use in Western Blot, Immunohistochemistry, Immunofluorescence and Immunoprecipitation.
||FOR RESEARCH USE ONLY (RUO).
||PBS with 0.02% sodium azide, 50% glycerol, pH7.3.
||Store at-20°C. Avoid freeze/thaw cycles.
||WB: 1:500-1:2000IHC: 1:50-1:200IF: 1:50-1:200IP: 1:50-1:200
||Recombinant fusion protein containing a sequence corresponding to amino acids 403-572 of human Lamin C (NP_005563.1).
| 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 Modifications || Increased phosphorylation of the lamins occurs before envelope disintegration and probably plays a role in regulating lamin associations. Phosphorylation status of S-22 determines its localization between double-strand break (DSB) sites and the nuclear matrix. 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. |
| 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. Recruited by DNA repair proteins XRCC4 and IFFO1 to the DNA double-strand breaks (DSBs) to prevent chromosome translocation by immobilizing broken DNA ends. 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. Required for cardiac homeostasis. Prelamin-A/C can accelerate smooth muscle cell senescence. It acts to disrupt mitosis and induce DNA damage in vascular smooth muscle cells (VSMCs), leading to mitotic failure, genomic instability, and premature senescence. |
| Protein Name || Prelamin-A/C Cleaved Into - Lamin-A/C70 Kda LaminRenal Carcinoma Antigen Ny-Ren-32 |
| Database Links || Reactome: R-HSA-1221632 P02545-2Reactome: R-HSA-2980766Reactome: R-HSA-2995383Reactome: R-HSA-352238 P02545-1Reactome: R-HSA-381038Reactome: R-HSA-4419969Reactome: R-HSA-6802952Reactome: R-HSA-8862803 P02545-1 |
| Cellular Localisation || NucleusNucleus EnvelopeNucleus LaminaNucleoplasmNucleus MatrixFarnesylation Of Prelamin-A/C Facilitates Nuclear Envelope Targeting And Subsequent Cleavage By Zmpste24/Face1 To Remove The Farnesyl Group Produces Mature Lamin-A/CWhich Can Then Be Inserted Into The Nuclear LaminaEmd Is Required For Proper Localization Of Non-Farnesylated Prelamin-A/CIsoform C: Nucleus Speckle |
| Alternative Antibody Names || Anti-Prelamin-A/C Cleaved Into - Lamin-A/C antibodyAnti-70 Kda Lamin antibodyAnti-Renal Carcinoma Antigen Ny-Ren-32 antibodyAnti-LMNA antibodyAnti-LMN1 antibody |
Information sourced from Uniprot.org
12 months for antibodies. 6 months for ELISA Kits. Please see website T&Cs for further guidance