Anti-Lamin A antibody (ab26300)

Overview

• Product nameAnti-Lamin A antibodySee all Lamin A primary antibodies ...
• Description
  Rabbit polyclonal to Lamin A
• Tested applicationsIHC-P, ICC/IF, WB more details
• Species reactivity
  Reacts with: Mouse, Rat, Human
  Predicted to work with: Chicken, Pig
• Immunogen

  Synthetic peptide conjugated to KLH derived from within residues 550 to the C-terminus of Human Lamin A.

  Read Abcam's proprietary immunogen policy

  (Peptide available as ab27812.)

• Positive controlab26300 gave a positive result in the following Whole Cell Lysates A431 NIH 3T3 PC12

Properties

• FormLiquid
• 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: 0.02% Sodium Azide
  Constituents: 1% BSA, PBS. pH 7.4
• Concentration information loading...
• PurityImmunogen affinity purified
• Clonality Polyclonal
• IsotypeIgG
• Research Areas
  • Signal Transduction
  • Cytoskeleton / ECM
  • Cytoskeleton
  • Intermediate Filaments
  • Class V
  • Lamins

  • Tags & Cell Markers
  • Subcellular Markers
  • Nucleus
  • Nuclear Envelope

Applications

Target

• 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.
• Post-translational
  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.

Target information above from: UniProt accession P02545 The UniProt Consortium
The Universal Protein Resource (UniProt) in 2010
Nucleic Acids Res. 38:D142-D148 (2010) .

Information by UniProt
• Database links
  • Entrez Gene: 396224 Chicken
  • Entrez Gene: 4000 Human
  • Entrez Gene: 16905 Mouse
  • Entrez Gene: 100126859 Pig
  • Entrez Gene: 60374 Rat
  • Omim: 150330 Human
  • SwissProt: P13648 Chicken
  • SwissProt: P02545 Human

  • SwissProt: P48678 Mouse
  • SwissProt: Q3ZD69 Pig
  • SwissProt: P48679 Rat
  • Unigene: 715 Chicken
  • Unigene: 594444 Human
  • Unigene: 243014 Mouse
  • Unigene: 471227 Mouse
  • Unigene: 944 Pig
  • Unigene: 44161 Rat

  see all

• Alternative names
  70 kDa lamin antibodyCDCD1 antibodyCDDC antibody

  CMD1A antibodyCMT2B1 antibodyEMD2 antibodyFPL antibodyFPLD antibodyHGPS antibodyIDC antibodyLAMIN A antibodylamin A/C antibodyLAMIN C antibodyLamin-A/C antibodyLDP1 antibodyLFP antibodyLGMD1B antibodyLMN 1 antibodyLMN A antibodyLMN C antibodyLMN1 antibodyLMNA antibodyLMNA_HUMAN antibodyLMNC antibodyNY REN 32 antigen antibodyPRO1 antibodyRenal carcinoma antigen NY-REN-32 antibody

  see all

Anti-Lamin A antibody images

• 

  Western blot - Lamin A antibody (ab26300)
  Anti-Lamin A antibody (ab26300) at 1 µg/ml + A431 (Human epithelial carcinoma cell line) Whole Cell Lysate (ab7909) at 20 µg
  
  Secondary
  IRDye 680 Conjugated Goat Anti-Rabbit IgG (H+L) at 1/15000 dilution
  
  Performed under reducing conditions.
  
  Predicted band size : 74 kDa
  Observed band size : 76 kDa (why is the actual band size different from the predicted?)
  Additional bands at : 68 kDa (possible degradation product).
• 

  Western blot - Lamin A antibody (ab26300)
  All lanes : Anti-Lamin A antibody (ab26300) at 1 µg/ml
  
  Lane 1 : Lamin A protein (Human) (ab83472) at 0.1 µg
  Lane 2 : Lamin A protein (Human) (ab83472) at 0.01 µg
  
  Secondary
  Goat polyclonal Secondary Antibody to Rabbit IgG - H&L (HRP), pre-adsorbed (ab97080) at 1/5000 dilution
  developed using the ECL technique
  
  Performed under reducing conditions.
  
  Exposure time : 10 seconds
• 

  Immunocytochemistry/ Immunofluorescence - Lamin A antibody (ab26300)This image is part of an Abreview submmited by Dr Kirk McManus.
   ab26300 (1/2000) staining Lamin A in assynchronous HeLa Cells, by Immunocytochemistry/ Immunofluorescence. Secondary antibody: goat anti-rabbit conjugated to Cy3 ^® (1/200). Cells counterstained with DAPI in order to highlight the nucleus.

  See Abreview

• 

  Immunocytochemistry/ Immunofluorescence - Lamin A antibody (ab26300)This image is courtesy of an Abreview submitted by Dr Chi W Tang
  ab26300 at 1/1000 staining human HeLa cells by ICC/IF. The cells were paraformaldehyde fixed, permeabilized with Triton X100 and blocked with BSA before incubation with the antibody. A Cy3 ® conjugated donkey anti-rabbit IgG was used as the secondary.

  See Abreview

• 

  Western blot - Lamin A antibody (ab26300)
  All lanes : Anti-Lamin A antibody (ab26300) at 1 µg/ml
  
  Lane 1 : NIH 3T3 (Mouse embryonic fibroblast cell line) Whole Cell Lysate (ab7179)
  Lane 2 : PC12 (Rat adrenal pheochromocytoma cell line) Whole Cell Lysate
  
  Lysates/proteins at 10 µg per lane.
  
  Secondary
  IRDye 680 Conjugated Goat Anti-Rabbit IgG (H+L) at 1/10000 dilution
  
  Performed under reducing conditions.
  
  Predicted band size : 74 kDa
  Observed band size : 74 kDa
  Additional bands at : 100 kDa,45 kDa,70 kDa (possible degradation product). We are unsure as to the identity of these extra bands.
• 

  Immunocytochemistry/ Immunofluorescence - Lamin A antibody (ab26300)
  ICC/IF image of ab26300 stained HeLa cells. The cells were fixed with 4% PFA (10 min) and then incubated in 1%BSA / 10% normal Goat serum / 0.3M glycine in 0.1% PBS-Tween for 1h to permeabilise the cells and block non-specific protein-protein interactions. The cells were then incubated with the antibody (ab26300 at 1µg/ml) overnight at +4°C. The secondary antibody (green) was Alexa Fluor® 488 Goat anti-Rabbit IgG (H+L) used at a 1/1000 dilution for 1h. Alexa Fluor® 594 WGA was used to label plasma membranes (red) at a 1/200 dilution for 1h. DAPI was used to stain the cell nuclei (blue). This antibody also gave a positive result in 4% PFA fixed (10 min)HepG2 and MCF7 cells at 1µg/ml, and in 100% methanol fixed (5 min) HeLa, HepG2 and MCF7 cells at 1µg/ml.