Product: Lamin A/C Antibody
Catalog: AF6056
Description: Rabbit polyclonal antibody to Lamin A/C
Application: WB IHC IF/ICC
Reactivity: Human, Mouse, Rat
Prediction: Pig, Zebrafish, Bovine, Horse, Rabbit, Chicken, Xenopus
Mol.Wt.: 74,65kDa; 74kD(Calculated).
Uniprot: P02545
RRID: AB_2834975

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 100ul $280 In stock
 200ul $350 In stock

Lead Time: Same day delivery

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Product Info

WB 1:500-1:2000, IHC 1:50-1:200, IF/ICC 1:100-1:500
*The optimal dilutions should be determined by the end user.

WB: For western blot detection of denatured protein samples. IHC: For immunohistochemical detection of paraffin sections (IHC-p) or frozen sections (IHC-f) of tissue samples. IF/ICC: For immunofluorescence detection of cell samples. ELISA(peptide): For ELISA detection of antigenic peptide.

Pig(100%), Zebrafish(100%), Bovine(100%), Horse(100%), Rabbit(100%), Chicken(91%), Xenopus(82%)
Lamin A/C Antibody detects endogenous levels of total Lamin A/C.
Cite Format: Affinity Biosciences Cat# AF6056, RRID:AB_2834975.
The antiserum was purified by peptide affinity chromatography using SulfoLink™ Coupling Resin (Thermo Fisher Scientific).
Rabbit IgG in phosphate buffered saline , pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol. Store at -20 °C. Stable for 12 months from date of receipt.


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



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.

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.



Score>80(red) has high confidence and is suggested to be used for WB detection. *The prediction model is mainly based on the alignment of immunogen sequences, the results are for reference only, not as the basis of quality assurance.

Model Confidence:
High(score>80) Medium(80>score>50) Low(score<50) No confidence

PTMs - P02545 As Substrate

Site PTM Type Enzyme
M1 Acetylation
T3 Phosphorylation
S5 Phosphorylation
T10 Phosphorylation
S12 Phosphorylation
S17 Phosphorylation
S18 Phosphorylation
T19 Phosphorylation P06493 (CDK1)
S22 Phosphorylation P28482 (MAPK1) , P06493 (CDK1)
T24 Phosphorylation
T27 Phosphorylation
K32 Ubiquitination
R41 Methylation
Y45 Phosphorylation
R48 Methylation
S51 Phosphorylation
T64 Phosphorylation
S66 Phosphorylation
S71 Phosphorylation
S75 Phosphorylation
K78 Ubiquitination
Y81 Phosphorylation
K90 Ubiquitination
S94 Phosphorylation
K97 Acetylation
K97 Sumoylation
K97 Ubiquitination
S107 Phosphorylation
K108 Acetylation
K108 Ubiquitination
K114 Acetylation
K114 Ubiquitination
K117 Ubiquitination
K123 Ubiquitination
K135 Acetylation
K135 Ubiquitination
S143 Phosphorylation
K144 Acetylation
K144 Ubiquitination
S149 Phosphorylation
T150 Phosphorylation
S153 Phosphorylation
K155 Acetylation
K155 Ubiquitination
T157 Phosphorylation
R166 Methylation
K171 Acetylation
K171 Ubiquitination
K180 Acetylation
K180 Ubiquitination
K181 Ubiquitination
R189 Methylation
T199 Phosphorylation
K201 Acetylation
K201 Sumoylation
K201 Ubiquitination
K208 Acetylation
K208 Sumoylation
K208 Ubiquitination
Y211 Phosphorylation
S212 Phosphorylation
T218 Phosphorylation
K219 Sumoylation
K219 Ubiquitination
T224 Phosphorylation
K233 Acetylation
K233 Sumoylation
K233 Ubiquitination
K260 Acetylation
K260 Sumoylation
K260 Ubiquitination
K261 Acetylation
K261 Ubiquitination
K265 Acetylation
K265 Sumoylation
K265 Ubiquitination
K270 Acetylation
K270 Sumoylation
K270 Ubiquitination
S277 Phosphorylation
S282 Phosphorylation
S295 Phosphorylation
S301 Phosphorylation P31749 (AKT1)
S303 Phosphorylation
S307 Phosphorylation O14757 (CHEK1)
K311 Acetylation
K311 Sumoylation
K311 Ubiquitination
K316 Ubiquitination
K319 Ubiquitination
S326 Phosphorylation
Y359 Phosphorylation
Y376 Phosphorylation
K378 Acetylation
K378 Sumoylation
K378 Ubiquitination
R386 Methylation
S390 Phosphorylation P06493 (CDK1)
S392 Phosphorylation P06493 (CDK1)
T394 Phosphorylation
S395 Phosphorylation
S398 Phosphorylation
S403 Phosphorylation
S404 Phosphorylation P31749 (AKT1)
S406 Phosphorylation
S407 Phosphorylation
T409 Phosphorylation
S414 Phosphorylation
T416 Phosphorylation
K417 Acetylation
K417 Sumoylation
K417 Ubiquitination
K418 Acetylation
K418 Ubiquitination
K420 Sumoylation
K420 Ubiquitination
S423 Phosphorylation
T424 Phosphorylation
S426 Phosphorylation
S429 Phosphorylation
S431 Phosphorylation
S437 Phosphorylation
K450 Acetylation
K450 Sumoylation
K450 Ubiquitination
K457 Acetylation
K457 Ubiquitination
S458 Phosphorylation
S463 Phosphorylation
K470 Acetylation
K470 Methylation
K470 Ubiquitination
T480 Phosphorylation
Y481 Phosphorylation
K486 Sumoylation
K486 Ubiquitination
T488 Phosphorylation
T505 Phosphorylation
S507 Phosphorylation
T510 Phosphorylation
K515 Acetylation
C522 S-Nitrosylation
S525 Phosphorylation
T528 Phosphorylation
S533 Phosphorylation
T534 Phosphorylation
S546 Phosphorylation
T548 Phosphorylation
S568 Phosphorylation
S583 Phosphorylation
T585 Phosphorylation
T590 Phosphorylation
K597 Acetylation
K597 Sumoylation
K597 Ubiquitination
S599 Phosphorylation
S601 Phosphorylation
S603 Phosphorylation
S612 O-Glycosylation
S612 Phosphorylation
S613 Phosphorylation
S615 Phosphorylation
S616 Phosphorylation
S618 Phosphorylation
S619 Phosphorylation
T621 Phosphorylation
T623 Phosphorylation
S625 Phosphorylation
S628 Phosphorylation
S632 Phosphorylation
S636 Phosphorylation
T643 O-Glycosylation
T643 Phosphorylation
R644 Methylation
S651 Phosphorylation
S652 Phosphorylation
T655 Phosphorylation
S657 Phosphorylation

Research Backgrounds


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. 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.


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:

Nucleus. Nucleus envelope. Nucleus lamina. Nucleus>Nucleoplasm.
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. EMD is required for proper localization of non-farnesylated prelamin-A/C.

Nucleus speckle.

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionSubcellular location
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.

Subunit Structure:

Homodimer of lamin A and lamin C. Interacts with lamin-associated polypeptides IA, IB and TMPO-alpha, RB1 and with emerin. Interacts with SREBF1, SREBF2, SUN2 and TMEM43. Interacts with TMEM201 (By similarity). Proteolytically processed isoform A interacts with NARF. Interacts with SUN1. Prelamin-A/C interacts with EMD. Interacts with MLIP. Interacts with DMPK; may regulate nuclear envelope stability. Interacts with SUV39H1; the interaction increases stability of SUV39H1. Interacts with SYNE2. Interacts with ITSN1 isoform 2.


Belongs to the intermediate filament family.

Research Fields

· Cellular Processes > Cell growth and death > Apoptosis.   (View pathway)

· Human Diseases > Cardiovascular diseases > Hypertrophic cardiomyopathy (HCM).

· Human Diseases > Cardiovascular diseases > Arrhythmogenic right ventricular cardiomyopathy (ARVC).

· Human Diseases > Cardiovascular diseases > Dilated cardiomyopathy (DCM).


1). Metabolic regulation of homologous recombination repair by MRE11 lactylation. Cell, 2024 (PubMed: 38128537) [IF=64.5]

Application: WB    Species: Human    Sample: MDA-MB-231 cells

Figure S3. MRE11 lactylation enhances its chromatin loading, DNA binding, and DNA end resection, related to Figures 3 and 4. (F–H) Western blots of soluble fractions from the indicated cells. These figures are related to Figures 3I, 3J, and 3L.

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