Anti-Lamin A/C antibody (STJ24412)

SKU:
STJ24412
Current Stock:
Host: Rabbit
Applications: WB, IHC, IF, IP
Reactivity: Human, Mouse, Rat
Short Description: Rabbit polyclonal primary antibody against LMNA.
Note: FOR RESEARCH USE ONLY (RUO).
Clonality: Polyclonal
Conjugation: Unconjugated
Formulation: PBS with 0.02% sodium azide, 50% glycerol, pH7.3.
Purification: Affinity purification
Storage Instruction: Store at-20°C. Avoid freeze/thaw cycles.
Isotype: IgG
Dilution Range: WB: 1:500-1:2000
IHC: 1:50-1:200
IF: 1:50-1:200
IP: 1:50-1:200
Gene ID: 4000
Immunogen: Recombinant fusion protein containing a sequence corresponding to amino acids 403-572 of human Lamin C (NP_005563.1).
Background The nuclear lamina consists of a two-dimensional matrix of proteins located next to the inner nuclear membrane. The lamin family of proteins make up the matrix and are highly conserved in evolution. During mitosis, the lamina matrix is reversibly disassembled as the lamin proteins are phosphorylated. Lamin proteins are thought to be involved in nuclear stability, chromatin structure and gene expression. Vertebrate lamins consist of two types, A and B. Alternative splicing results in multiple transcript variants. Mutations in this gene lead to several diseases: Emery-Dreifuss muscular dystrophy, familial partial lipodystrophy, limb girdle muscular dystrophy, dilated cardiomyopathy, Charcot-Marie-Tooth disease, and Hutchinson-Gilford progeria syndrome.
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. 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.
Database Links Reactome: R-HSA-1221632 P02545-2
Cellular Localisation Nucleus
Nucleus Envelope
Nucleus Lamina
Nucleoplasm
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
Emd Is Required For Proper Localization Of Non-Farnesylated Prelamin-A/C
Isoform C: Nucleus Speckle
Protein Name Prelamin-A/C Cleaved Into - Lamin-A/C
70 Kda Lamin
Renal Carcinoma Antigen Ny-Ren-32
6 months standard