Anti-Lamin A + C antibody [131C3] - Nuclear Envelope Marker (ab8984)
- Product nameAnti-Lamin A + C antibody [131C3] - Nuclear Envelope MarkerSee all Lamin A + C primary antibodies ...
- DescriptionMouse monoclonal [131C3] to Lamin A + C - Nuclear Envelope Marker
- Specificityab8984 reacts with lamins A and C. Lamins do not appear to be universally distributed among different cell and tissue types. ab8984 has been shown to react with HT1080 cells in Western blot. Other cell/tissue types have not been tested. Customer feedback seems to indicate that ab8984 does not detect Lamin A+C in rat brain lysates (please see AbReviews).
- Tested applicationsIP, Flow Cyt, ICC, IHC-Fr, WB, ICC/IF more details
- Species reactivityReacts with: Mouse, Rat, Sheep, Hamster, Cow, Dog, Human, Indian Muntjac
Purified rat liver lamins.
- EpitopeBetween residues 319-566.
- Positive control
- IHC: human colon WB: Human fibroblast, HT1080 cells
- Storage instructionsStore at +4°C short term (1-2 weeks). Aliquot and store at -20°C or -80°C. Avoid repeated freeze / thaw cycles.
- Storage bufferPreservative: 0.09% Sodium Azide
- Concentration information loading...
- PurityProtein G purified
- Clonality Monoclonal
- Clone number131C3
- Light chain typekappa
- Research Areas
Our Abpromise guarantee covers the use of ab8984 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
|IP||IP: Use at an assay dependent dilution. PubMed: 16126733|
|Flow Cyt||Flow Cyt: 1/100 - 1/200.|
|ICC||ICC: Use at an assay dependent dilution. Fix cells in precold (- 20°C) 1:1 methanol/acetone for 20 minutes at - 20°C.|
|IHC-Fr||IHC-Fr: Use at an assay dependent dilution. Recommended range is 1/100 - 1/200 for Immunohistochemistry with avidin-biotinylated horseradish peroxidase complex (ABC) as detection reagent.|
|WB||WB: 1/100 - 1/1000. Predicted molecular weight: 70 kDa. Use nuclear extracts, incubate primary antibody overnight. Predicted molecular weight: 65-70 kDa depending on the species and preparation.|
|ICC/IF||ICC/IF: Use at an assay dependent concentration. Used at an a dilution of 1/200 (for 16 hrs incubation) on HeLa cells (see Abreview for further information).|
- FunctionLamins 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. Play an important role in nuclear assembly, chromatin organization, nuclear membrane and telomere dynamics.
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.
- Tissue specificityIn the arteries, prelamin-A/C accumulation is not observed in young healthy vessels but is prevalent in medial vascular smooth muscle celle (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.
- Involvement in diseaseDefects in LMNA are the cause of Emery-Dreifuss muscular dystrophy type 2 (EDMD2) [MIM:181350]. A degenerative myopathy characterized by weakness and atrophy of muscle without involvement of the nervous system, early contractures of the elbows, Achilles tendons and spine, and cardiomyopathy associated with cardiac conduction defects.
Defects in LMNA are the cause of cardiomyopathy dilated type 1A (CMD1A) [MIM:115200]. Dilated cardiomyopathy is a disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death.
Defects in LMNA are the cause of familial partial lipodystrophy type 2 (FPLD2) [MIM:151660]; also known as familial partial lipodystrophy Dunnigan type. A disorder characterized by the loss of subcutaneous adipose tissue in the lower parts of the body (limbs, buttocks, trunk). It is accompanied by an accumulation of adipose tissue in the face and neck causing a double chin, fat neck, or cushingoid appearance. Adipose tissue may also accumulate in the axillae, back, labia majora, and intraabdominal region. Affected patients are insulin-resistant and may develop glucose intolerance and diabetes mellitus after age 20 years, hypertriglyceridemia, and low levels of high density lipoprotein cholesterol.
Defects in LMNA are the cause of limb-girdle muscular dystrophy type 1B (LGMD1B) [MIM:159001]. LGMD1B is an autosomal dominant degenerative myopathy with age-related atrioventricular cardiac conduction disturbances, dilated cardiomyopathy, and the absence of early contractures. LGMD1B is characterized by slowly progressive skeletal muscle weakness of the hip and shoulder girdles. Muscle biopsy shows mild dystrophic changes.
Defects in LMNA are the cause of Charcot-Marie-Tooth disease type 2B1 (CMT2B1) [MIM:605588]. CMT2B1 is a form of Charcot-Marie-Tooth disease, the most common inherited disorder of the peripheral nervous system. Charcot-Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathy or CMT1, and primary peripheral axonal neuropathy or CMT2. Neuropathies of the CMT2 group are characterized by signs of axonal regeneration in the absence of obvious myelin alterations, normal or slightly reduced nerve conduction velocities, and progressive distal muscle weakness and atrophy. CMT2B1 inheritance is autosomal recessive.
Defects in LMNA are the cause of Hutchinson-Gilford progeria syndrome (HGPS) [MIM:176670]. HGPS is a rare genetic disorder characterized by features reminiscent of marked premature aging. Note=HGPS is caused by the toxic accumulation of a mutant form of lamin-A/C. This mutant protein, called progerin, acts to deregulate mitosis and DNA damage signaling, leading to premature cell death and senescence. Progerin lacks the conserved ZMPSTE24/FACE1 cleavage site and therefore remains permanently farnesylated. Thus, although it can enter the nucleus and associate with the nuclear envelope, it cannot incorporate normally into the nuclear lamina.
Defects in LMNA are the cause of cardiomyopathy dilated with hypergonadotropic hypogonadism (CMDHH) [MIM:212112]. A disorder characterized by the association of genital anomalies, hypergonadotropic hypogonadism and dilated cardiomyopathy. Patients can present other variable clinical manifestations including mental retardation, skeletal anomalies, scleroderma-like skin, graying and thinning of hair, osteoporosis. Dilated cardiomyopathy is characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia.
Defects in LMNA are the cause of mandibuloacral dysplasia with type A lipodystrophy (MADA) [MIM:248370]. A disorder characterized by mandibular and clavicular hypoplasia, acroosteolysis, delayed closure of the cranial suture, progeroide appearance, partial alopecia, soft tissue calcinosis, joint contractures, and partial lipodystrophy with loss of subcutaneous fat from the extremities. Adipose tissue in the face, neck and trunk is normal or increased.
Defects in LMNA are a cause of lethal tight skin contracture syndrome (LTSCS) [MIM:275210]; also known as restrictive dermopathy (RD). Lethal tight skin contracture syndrome is a rare disorder mainly characterized by intrauterine growth retardation, tight and rigid skin with erosions, prominent superficial vasculature and epidermal hyperkeratosis, facial features (small mouth, small pinched nose and micrognathia), sparse/absent eyelashes and eyebrows, mineralization defects of the skull, thin dysplastic clavicles, pulmonary hypoplasia, multiple joint contractures and an early neonatal lethal course. Liveborn children usually die within the first week of life. The overall prevalence of consanguineous cases suggested an autosomal recessive inheritance.
Defects in LMNA are the cause of heart-hand syndrome Slovenian type (HHS-Slovenian) [MIM:610140]. Heart-hand syndrome (HHS) is a clinically and genetically heterogeneous disorder characterized by the co-occurrence of a congenital cardiac disease and limb malformations.
Defects in LMNA are the cause of muscular dystrophy congenital LMNA-related (CMD-LMNA) [MIM:613205]. It is a form of congenital muscular dystrophy. Patients present at birth, or within the first few months of life, with hypotonia, muscle weakness and often with joint contractures.
- Sequence similaritiesBelongs to the intermediate filament family.
modificationsIncreased 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.
- Cellular localizationNucleus. Nucleus envelope. 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.
- 70 kDa Lamin antibody
- Cardiomyopathy dilated 1A (autosomal dominant) antibody
- CDCD1 antibody
- CDDC antibody
- Charcot Marie Tooth Disease Axonal Type 2B1 antibody
- CMD1A antibody
- CMT2B1 antibody
- EMD2 antibody
- FPL antibody
- FPLD antibody
- FPLD2 antibody
- HGPS antibody
- IDC antibody
- Lamin A/C antibody
- Lamin A/C Isoform 1 Precursor antibody
- Lamin A/C Isoform 2 antibody
- Lamin A/C Isoform 3 antibody
- Lamin A/C like 1 antibody
- Lamin-A/C antibody
- LDP1 antibody
- LFP antibody
- LGMD1B antibody
- Limb girdle muscular dystrophy 1B (autosomal dominant) antibody
- LMN 1 antibody
- LMN A antibody
- LMN C antibody
- LMN1 antibody
- LMNA antibody
- LMNA_HUMAN antibody
- LMNC antibody
- LMNC antibody
- NY REN 32 antigen antibody
- Prelamin A/C antibody
- PRO1 antibody
- Progeria 1 (Hutchinson Gilford Type) antibody
- Renal carcinoma antigen NY REN 32 antibody
- Renal carcinoma antigen NY-REN-32 antibody
- Renal carcinoma antigen NYREN32 antibody
Anti-Lamin A + C antibody [131C3] - Nuclear Envelope Marker images
Predicted band size : 70 kDa
A. HT1080 cells + siRNA control sequence
B. HT1080 cells + siRNA Lamin
This picture was submitted by Andrea Robertson as part of a review of ab8984
ab8984 at a 1/200 dilution staining Asynchronous and paraformaldehyde-fixed (4%) HeLa cells by immunocytochemistry. The antibody was incubated with the cells overnight and then detected using a Cy3 conjugated Goat Anti-Mouse IgG (H+L) antibody. The image shows faint, but distinct, nuclear membrane staining.
This image is courtesy of an Abreview by Kirk McManus submitted on 27 February 2006.
All lanes : Anti-Lamin A + C antibody [131C3] - Nuclear Envelope Marker (ab8984) at 1/1000 dilution
Lane 1 : 10ug HeLa whole cell lysate
Lane 2 : 50ug HeLa whole cell lysate
Lane 3 : 100ug HeLa whole cell lysate
HRP conjugated goat anti-mouse antibody
developed using the ECL technique
Predicted band size : 70 kDa
Observed band size : 70 kDa
Exposure time : 30 seconds
This image is courtesy of an Abreview submitted by Ms Aarti Jagannath
ab8984 staining dog skeletal muscle tissue cells by ICC/IF. Cells were fixed in methanol and incubated with ab8984, diluted 1/200, for 12 hours at 4°C. A FITC conjugated goat anti-mouse antibody, diluted 1/200, was used as the secondary antibody.
Anti-Lamin A + C antibody [131C3] - Nuclear Envelope Marker (ab8984) at 1/100 dilution + human fibroblast at 15 µl
developed using the ECL technique
Performed under reducing conditions.
Predicted band size : 70 kDa
Lysates were prepared in RIPA buffer on ice for 30 min. They were sonicated 4 times for 5 sec prior to mixing with loading buffer.
Overlay histogram showing HeLA cells stained with ab8984 (red line). The cells were fixed with 100% methanol (5 min) and then permeabilized with 0.1% PBS-Tween for 20 min. The cells were then incubated in 1x PBS / 10% normal goat serum / 0.3M glycine to block non-specific protein-protein interactions followed by the antibody (ab8984, 1µg/1x106 cells) for 30 min at 22°C. The secondary antibody used was DyLight® 488 goat anti-mouse IgG (H+L) (ab96879) at 1/500 dilution for 30 min at 22°C. Isotype control antibody (black line) was Mouse IgG1 [ICIGG1] (ab91353, 2µg/1x106 cells) used under the same conditions. Acquisition of >5,000 events was performed.
References for Anti-Lamin A + C antibody [131C3] - Nuclear Envelope Marker (ab8984)
This product has been referenced in:
- Umlauf D et al. The human TREX-2 complex is stably associated with the nuclear pore basket. J Cell Sci 126:2656-67 (2013). Human . Read more (PubMed: 23591820) »
- Benfield CT et al. Vaccinia virus protein K7 is a virulence factor that alters the acute immune response to infection. J Gen Virol 94:1647-57 (2013). Read more (PubMed: 23580427) »