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MAB3211 | Anti-Lamin A/C Antibody, clone JoL2

1 mL  
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      Key Specifications Table

      Species ReactivityKey ApplicationsHostFormatAntibody Type
      H, Ht, Mk, Xn ICC, IF, IHC, IP, WB M Culture Supernatant Monoclonal Antibody
      Catalogue NumberMAB3211
      Brand Family Chemicon®
      Trade Name
      • Chemicon
      DescriptionAnti-Lamin A/C Antibody, clone JoL2
      Product Information
      FormatCulture Supernatant
      • Mammalian Cardiac tissue
      PresentationUnPurified mouse tissue culture supernatant containing 0.2M Tris/HCl pH 7.4 and 5-10% fetal calf Serum with 0.09% sodium azide as a preservative
      ApplicationAnti-Lamin A/C Antibody, clone JoL2 is an antibody against Lamin A/C for use in IC, IF, IH, IP & WB.
      Key Applications
      • Immunocytochemistry
      • Immunofluorescence
      • Immunohistochemistry
      • Immunoprecipitation
      • Western Blotting
      Application NotesImmunohistochemistry: overnight incubation is recommended. Frozen tissue sections Neat-1:5; paraffin embedded tissue sections 1:30-1:50 (requires pretreatment with trypsin prior to staining)

      Immunoprecipitation: Neat

      Western Blotting: 1:150-1:200

      Optimal working dilutions must be determined by the end user.
      Biological Information
      ImmunogenRecombinant human lamin A
      SpecificityRecognizes human lamins A and C. The antibody reacts with both recombinant and native lamin A and C. The antibody has been shown to bind to an epitope between amino acids 464-572.
      Species Reactivity
      • Human
      • Hamster
      • Monkey
      • Xenopus
      Antibody TypeMonoclonal Antibody
      Entrez Gene Number
      Entrez Gene SummaryThe 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. Through alternate splicing, this gene encodes three type A lamin isoforms. 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.
      Gene Symbol
      • LMNA
      • HGPS
      • EMD2
      • FPLD
      • CDCD1
      • LDP1
      • LGMD1B
      • IDC
      • CMT2B1
      • FPL
      • LMNC
      • PRO1
      • Lamin-A/C
      • LMN1
      • CMD1A
      • LFP
      • CDDC
      Purification MethodUnpurified
      UniProt Number
      UniProt SummaryFUNCTION: SwissProt: P02545 # 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.
      SIZE: 664 amino acids; 74139 Da
      SUBUNIT: Homodimer of lamin A and lamin C. Interacts with lamin- associated polypeptides IA, IB and TMPO-alpha, RB1 and with emerin. Proteolytically processed isoform A interacts with NARF.
      PTM: Increased phosphorylation of the lamins occurs before envelope disintegration and probably plays a role in regulating lamin associations. & The C-terminal 18 residues are removed by proteolytic cleavage in isoform A. Proteolytic cleavage requires prior farnesylation and absence of farnesylation blocks cleavage (By similarity).
      DISEASE: SwissProt: P02545 # Defects in LMNA are a cause of Emery-Dreifuss muscular dystrophy type 2 (EDMD2) [MIM:181350]. EDMD2 is an autosomal dominant disorder characterized by slowly progressive muscle wasting and weakness, early contractures of the elbows Achilles tendons and spine, and cardiomyopathy associated with cardiac conduction defects. & Defects in LMNA are a cause of Emery-Dreifuss muscular dystrophy type 3 (EDMD3) [MIM:604929]. EDMD3 is an autosomal recessive disorder characterized by early contractures, muscle wasting and weakness and cardiomyopathy. & Defects in LMNA are a cause of dilated cardiomyopathy 1A (CMD1A) [MIM:115200]. Dilated cardiomyopathy, a disorder characterized by cardiac dilation and reduced systolic function, represents an outcome of a heterogeneous group of inherited and acquired disorders. & Defects in LMNA are a cause of CMD1A with quadriceps myopathy [MIM:607920]. Inheritance is autosomal dominant and the phenotype severe. & Defects in LMNA are a cause of generalized lipoatrophy associated with diabetes, hepatic steatosis, hypertrophic cardiomyopathy and leukomelanodermic papules (LDHCP) [MIM:608056]. LDHCP is a disorder characterized by acquired generalized lipoatrophy with metabolic alterations, massive liver steatosis, distinctive cutaneous manifestations, and cardiac abnormalities involving both endocardium and myocardium. & Defects in LMNA are a cause of familial partial lipodystrophy (FPLD) [MIM:151660]; also known as familial partial lipodystrophy Dunnigan type. FPLD is an autosomal dominant disorder characterized by marked loss of subcutaneous adipose tissue from the extremities and trunk but by excess fat deposition in the head and neck. Frequently associated with profound insulin resistance, dyslipidemia, and diabetes. & Defects in LMNA are the cause of limb-girdle muscular dystrophy type 1B (LGMD1B) [MIM:159001]. LGMD1B is an autosomal dominantly inherited slowly progressive limb girdle muscular dystrophy, with age-related atrioventricular cardiac conduction disturbances and the absence of early contractures. & 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. & Defects in LMNA are a cause of familial atrial fibrillation (ATFB) [MIM:607554]. Atrial fibrillation is a cardiac arrhythmia characterized by rapid and irregular activation of the atrium. It causes thromboembolism, tachycardia-mediated cardiomyopathy and heart failure. & Defects in LMNA are a cause of Werner syndrome (WRN) [MIM:277700]. WRN is an autosomal, recessively inherited, segmental progeroid syndrome, in which multiple aspects (or segments) of aging phenotypes seem to be entailed. The features of Werner syndrome are scleroderma-like skin changes, especially in the extremities, cataract, subcutaneous calcification, premature arteriosclerosis, diabetes mellitus, and a wizened and prematurely aged facies. & Defects in LMNA are the cause of mandibuloacral dysplasia with type A lipodystrophy (MADA) [MIM:248370]. Mandibuloacral dysplasia (MAD) is a rare autosomal recessive disorder characterized by mandibular and clavicular hypoplasia, acroosteolysis, delayed closure of the cranial suture, joint contractures, and types A or B patterns of lipodystrophy. Type A lipodystrophy observed in MADA, is characterized by fat loss restricted to the extremities. & Defects in LMNA are a cause of lethal tight skin contracture syndrome [MIM:275210]; also called 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.
      SIMILARITY: SwissProt: P02545 ## Belongs to the intermediate filament family.
      MISCELLANEOUS: There are three types of lamins in human cells: A, B, and C. & The structural integrity of the lamina is strictly controlled by the cell cycle, as seen by the disintegration and formation of the nuclear envelope in prophase and telophase, respectively.
      Molecular Weight70 & 60 kDa
      Physicochemical Information
      Materials Information
      Toxicological Information
      Safety Information according to GHS
      Safety Information
      Product Usage Statements
      Usage Statement
      • Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
      Storage and Shipping Information
      Storage ConditionsMaintain for 1 year at -20°C from date of shipment. Aliquot to avoid repeated freezing and thawing. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
      Packaging Information
      Material Size1 mL
      Transport Information
      Supplemental Information




      Safety Data Sheet (SDS) 

      Certificates of Analysis

      TitleLot Number
      MOUSE ANTI-HUMAN LAMIN A+C - 2506321 2506321
      MOUSE ANTI-HUMAN LAMIN A+C -2548173 2548173
      MOUSE ANTI-HUMAN LAMIN A+C -2576359 2576359
      MOUSE ANTI-HUMAN LAMIN A+C -2624217 2624217
      MOUSE ANTI-HUMAN LAMIN A+C -2661400 2661400
      MOUSE ANTI-HUMAN LAMIN A+C -2685217 2685217
      MOUSE ANTI-HUMAN LAMIN A+C -2718314 2718314
      MOUSE ANTI-HUMAN LAMIN A+C -2739494 2739494
      MOUSE ANTI-HUMAN LAMIN A+C -2757197 2757197
      MOUSE ANTI-HUMAN LAMIN A+C -2804225 2804225

      References | 40 Available | See All References

      Reference overviewApplicationSpeciesPub Med ID
      Progerin reduces LAP2α-telomere association in Hutchinson-Gilford progeria.
      Chojnowski, A; Ong, PF; Wong, ES; Lim, JS; Mutalif, RA; Navasankari, R; Dutta, B; Yang, H; Liow, YY; Sze, SK; Boudier, T; Wright, GD; Colman, A; Burke, B; Stewart, CL; Dreesen, O
      eLife 4 2015

      Show Abstract
      26312502 26312502
      Expression of progerin in aging mouse brains reveals structural nuclear abnormalities without detectible significant alterations in gene expression, hippocampal stem cells or behavior.
      Baek, JH; Schmidt, E; Viceconte, N; Strandgren, C; Pernold, K; Richard, TJ; Van Leeuwen, FW; Dantuma, NP; Damberg, P; Hultenby, K; Ulfhake, B; Mugnaini, E; Rozell, B; Eriksson, M
      Human molecular genetics 24 1305-21 2015

      Show Abstract
      25343989 25343989
      Mechanisms controlling the smooth muscle cell death in progeria via down-regulation of poly(ADP-ribose) polymerase 1.
      Zhang, H; Xiong, ZM; Cao, K
      Proceedings of the National Academy of Sciences of the United States of America 111 E2261-70 2014

      Show Abstract
      24843141 24843141
      Depletion of the protein kinase VRK1 disrupts nuclear envelope morphology and leads to BAF retention on mitotic chromosomes.
      Molitor, TP; Traktman, P
      Molecular biology of the cell 25 891-903 2014

      Show Abstract
      24430874 24430874
      FHL2 prevents cardiac hypertrophy in mice with cardiac-specific deletion of ROCK2.
      Okamoto, R; Li, Y; Noma, K; Hiroi, Y; Liu, PY; Taniguchi, M; Ito, M; Liao, JK
      FASEB journal : official publication of the Federation of American Societies for Experimental Biology 27 1439-49 2013

      Show Abstract
      23271052 23271052
      Lamin B1 fluctuations have differential effects on cellular proliferation and senescence.
      Dreesen, O; Chojnowski, A; Ong, PF; Zhao, TY; Common, JE; Lunny, D; Lane, EB; Lee, SJ; Vardy, LA; Stewart, CL; Colman, A
      The Journal of cell biology 200 605-17 2013

      Show Abstract
      23439683 23439683
      LMNA-associated cardiocutaneous progeria: an inherited autosomal dominant premature aging syndrome with late onset.
      Kane, MS; Lindsay, ME; Judge, DP; Barrowman, J; Ap Rhys, C; Simonson, L; Dietz, HC; Michaelis, S
      American journal of medical genetics. Part A 161A 1599-611 2013

      Show Abstract
      23666920 23666920
      Partial lipodystrophy with severe insulin resistance and adult progeria Werner syndrome.
      Donadille, B; D'Anella, P; Auclair, M; Uhrhammer, N; Sorel, M; Grigorescu, R; Ouzounian, S; Cambonie, G; Boulot, P; Laforêt, P; Carbonne, B; Christin-Maitre, S; Bignon, YJ; Vigouroux, C
      Orphanet journal of rare diseases 8 106 2013

      Show Abstract
      23849162 23849162
      Correlated alterations in genome organization, histone methylation, and DNA-lamin A/C interactions in Hutchinson-Gilford progeria syndrome.
      McCord, RP; Nazario-Toole, A; Zhang, H; Chines, PS; Zhan, Y; Erdos, MR; Collins, FS; Dekker, J; Cao, K
      Genome research 23 260-9 2013

      Show Abstract
      23152449 23152449
      Expression of the Hutchinson-Gilford Progeria Mutation during Osteoblast Development Results in Loss of Osteocytes, Irregular Mineralization, and Poor Biomechanical Properties.
      Eva Schmidt,Ola Nilsson,Antti Koskela,Juha Tuukkanen,Claes Ohlsson,Bj Rozell,Maria Eriksson,Björn Rozell
      The Journal of biological chemistry 287 2012

      Show Abstract
      22893709 22893709

      Data Sheet


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