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MAB1678 Anti-Filamin A Antibody, clone PM6/317

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MAB1678
100 µL  
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      Overview

      Replacement Information

      Key Spec Table

      Species ReactivityKey ApplicationsHostFormatAntibody Type
      Ch, Gp, H, M, R, RbIF, IHC, IH(P), IP, WBMAscitesMonoclonal Antibody
      Description
      Catalogue NumberMAB1678
      Brand Family Chemicon®
      Trade Name
      • Chemicon
      DescriptionAnti-Filamin A Antibody, clone PM6/317
      Alternate Names
      • Alpha-Filamin
      • Filamin I
      • Endothelial Actin-binding Protein
      • ABP-280
      • Nonmuscle Filamin
      Background InformationFilamin is a structural protein that forms flexible cross-links between two actin filaments. Filamin is a homodimer of polypeptide chains each joined to the other at one end with an actin binding site ath the other. It is present in smooth muscle, fibroblasts, platelets and lymphocytes.
      References
      Product Information
      FormatAscites
      Control
      • Positive control tisse: skin, jurkat cell lysate.
      PresentationMouse monoclonal ascites IgG1 in buffer containing 0.1% sodium azide.
      Quality LevelMQ100
      Applications
      ApplicationThis Anti-Filamin A Antibody, clone PM6/317 is validated for use in IF, IH, IH(P), IP, WB for the detection of Filamin A.
      Key Applications
      • Immunofluorescence
      • Immunohistochemistry
      • Immunohistochemistry (Paraffin)
      • Immunoprecipitation
      • Western Blotting
      Application NotesImmunoblotting:
      1:1000-1:4000. Because of the large size of the unprocessed forms of filamin, 4-7% PAGE gels and proteinase inhibitors are recommended.

      Immunofluorescence:
      1:50-1:200 dilution from a previous lot was used. Suitable for staining both frozen and paraffin embedded tissues (at lower dilutions). Microwave-citrate buffer antigen retrieval method recommended for paraffin sections.

      Immunoprecipitation:
      A previous lot was used on immunoprecipitation. Suggested lysis buffer is PBS with 0.5% triton X-100 with proteinase inhibitors (note for full length filamin include calpain inhibitors). 5 microliters of antibody for every 300-500 μL of cell lysate (200-500 μg/mL total protein is suggested. Incubation is 1 hour RT or overnight 4C; Protein A/G agarose beads or rabbit anti-mouse secondary capture antibody is recommended for best recovery. 4-8% acrylamide gels are recommended for full length filamin or the 190 kDa fragement visualization.

      Optimal working dilutions must be determined by end user.
      Biological Information
      ImmunogenHuman platelet protein.
      ClonePM6/317
      ConcentrationPlease refer to the Certificate of Analysis for the lot-specific concentration.
      HostMouse
      SpecificityRecognizes unprocessed, full length Human filamin (actin-binding protein; 270-280 kDa) as well as the 190 kDa N-terminal calpain cleavage fragment of filamin (Aakhus, 1992). Following induction of apoptosis in U937 cells, the antibody recognizes 170, 150, and 120 kDa N-terminal cleavage fragments of the full-length form presumably resulting from cleavage by activated caspase-3 (Umeda, 2001).
      IsotypeIgG1
      Species Reactivity
      • Chicken
      • Guinea Pig
      • Human
      • Mouse
      • Rat
      • Rabbit
      Species Reactivity NoteHuman, mouse, and rat. Expected to cross-react with chicken, guinea pig and rabbit.
      Antibody TypeMonoclonal Antibody
      Entrez Gene Number
      Entrez Gene SummaryActin-binding protein, or filamin, is a 280-kD protein that crosslinks actin filaments into orthogonal networks in cortical cytoplasm and participates in the anchoring of membrane proteins for the actin cytoskeleton. Remodeling of the cytoskeleton is central to the modulation of cell shape and migration. Filamin A, encoded by the FLNA gene, is a widely expressed protein that regulates reorganization of the actin cytoskeleton by interacting with integrins, transmembrane receptor complexes, and second messengers.[supplied by OMIM]
      Gene Symbol
      • FLNA
      • Alpha-filamin
      • OPD2
      • Filamin-A
      • MNS
      • FLN
      • FMD
      • OPD1
      • FLN1
      • NHBP
      • ABP-280
      • ABPX
      • OPD
      • Filamin-1
      • DKFZp434P031
      Purification MethodUnpurified
      UniProt Number
      UniProt SummaryFUNCTION: SwissProt: P21333 # Promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. Anchors various transmembrane proteins to the actin cytoskeleton and serves as a scaffold for a wide range of cytoplasmic signaling proteins. Interaction with FLNA may allow neuroblast migration from the ventricular zone into the cortical plate. Tethers cell surface- localized furin, modulates its rate of internalization and directs its intracellular trafficking (By similarity).
      SIZE: 2647 amino acids; 280739 Da
      SUBUNIT: Interacts with PDLIM2 (By similarity). Homodimer. Interacts with FLNB, FURIN, HSPB7, INPPL1, KCND2, MYOT, MYOZ1, ARHGAP24, PSEN1 and PSEN2. Interacts also with various other binding partners in addition to filamentous actin.
      SUBCELLULAR LOCATION: Cytoplasm, cell cortex.
      TISSUE SPECIFICITY: Ubiquitous.
      DOMAIN: SwissProt: P21333 Comprised of a NH2-terminal actin-binding domain, 24 internally homologous repeats and two hinge regions. Repeat 24 and the second hinge domain are important for dimer formation.
      PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By similarity). Phosphorylation extent changes in response to cell activation. & The N-terminus is blocked.
      DISEASE: SwissProt: P21333 # Defects in FLNA are the cause of periventricular nodular heterotopia 1 (PVNH1) [MIM:300049]; also called nodular heterotopia, bilateral periventricular (NHBP or BPNH). PVNH1 is an X-linked developmental dominant disorder in which many neurons fail to migrate into the cerebral cortex. They remain as nodules lining the ventricular surface. In heterozygous females these neurons presumably represent those cells that, after X-chromosome inactivation, contain the active X chromosome with the filamin mutation. Most hemizygous affected males die early during embryogenesis, whereas heterozygous females have normal intelligence but suffer from seizures and various manifestations outside the central nervous system, especially related to the vascular system. This implies that essential embryonic cell migration can only occur in FLNA-expressing cells. & Defects in FLNA are the cause of periventricular nodular heterotopia 4 (PVNH4) [MIM:300537]; also known as periventricular heterotopia Ehlers-Danlos variant. PVNH4 is characterized by nodular brain heterotopia, joint hypermobility and development of aortic dilatation in early adulthood. & Defects in FLNA are the cause of otopalatodigital syndrome type 1 (OPD1) [MIM:311300]. OPD1 is an X-linked dominant multiple congenital anomalies disease mainly characterized by a generalized skeletal dysplasia, mild mental retardation, hearing loss, cleft palate, and typical facial anomalies. OPD1 belongs to a group of X-linked skeletal dysplasias known as oto-palato- digital syndrome spectrum disorders that also include OPD2, Melnick-Needles syndrome (MNS), and frontometaphyseal dysplasia (FMD). Remodeling of the cytoskeleton is central to the modulation of cell shape and migration. FLNA is a widely expressed protein that regulates re-organization of the actin cytoskeleton by interacting with integrins, transmembrane receptor complexes and second messengers. Males with OPD1 have cleft palate, malformations of the ossicles causing deafness and milder bone and limb defects than those associated with OPD2. Obligate female carriers of mutations causing both OPD1 and OPD2 have variable (often milder) expression of a similar phenotypic spectrum. & Defects in FLNA are the cause of otopalatodigital syndrome type 2 (OPD2) [MIM:304120]; also known as cranioorodigital syndrome. OPD2 is a congenital bone disorder that is characterized by abnormally modeled, bowed bones, small or absent first digits and, more variably, cleft palate, posterior fossa brain anomalies, omphalocele and cardiac defects. & Defects in FLNA are the cause of frontometaphyseal dysplasia (FMD) [MIM:305620]. FMD is a congenital bone disease characterized by supraorbital hyperostosis, deafness and digital anomalies. & Defects in FLNA are the cause of Melnick-Needles syndrome (MNS) [MIM:309350]. MNS is a severe congenital bone disorder characterized by typical facies (exophthalmos, full cheeks, micrognathia and malalignment of teeth), flaring of the metaphyses of long bones, s-like curvature of bones of legs, irregular constrictions in the ribs, and sclerosis of base of skull. & Defects in FLNA are associated with cerebrofrontofacial syndrome [MIM:608578]. This syndrome consists of a phenotype of male PVNH, with relatively normal development, no epilepsy or other neurological abnormality, severe constipation, and facial dysmorphism and without a discernible skeletal phenotype. & Defects in FLNA are a cause of X-linked congenital idiopathic intestinal pseudoobstruction (CIIPX) [MIM:300048]. CIIPX is caused by severe abnormality of gastrointestinal motility either due to primary qualitative defects of enteric ganglia and nerve fibers, or secondary to a variety of conditions, such as myopathies, inflammatory or autoimmune diseases, drug toxicity, ischemia, or viral infections. CIIPX is diagnosed by radiological, surgical, or manometric evidence of abnormal bowel motility causing intestinal obstruction in the absence of any mechanical occlusion.
      SIMILARITY: Belongs to the filamin family. & Contains 1 actin-binding domain. & Contains 2 CH (calponin-homology) domains. & Contains 24 filamin repeats.
      Molecular Weight270-280 kDa & 190 kDa
      Physicochemical Information
      Dimensions
      Materials Information
      Toxicological Information
      Safety Information according to GHS
      Safety Information
      Product Usage Statements
      Quality AssuranceRoutinely evaluated by Western Blot on Jurkat lysates.

      Western Blot Analysis:
      1:500-1:4000 dilution of this lot detected Filamin A on 10 μg of Jurkat lysates. Because of the large size of the unprocessed forms of filamin, 4-7% PAGE gels and proteinase inhibitors are recommended.
      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 ConditionsStable for 1 year at -20°C in undiluted aliquots from date of receipt.
      Handling Recommendations: Upon first thaw, and prior to removing the cap, centrifuge the vial and gently mix the solution. Aliquot into microcentrifuge tubes and store at -20°C. Avoid repeated freeze/thaw cycles, which may damage IgG and affect product performance.
      Packaging Information
      Material Size100 µL
      Transport Information
      Supplemental Information
      Specifications
      Global Trade Item Number
      Catalogue Number GTIN
      MAB1678 08436037124563

      Documentation

      Anti-Filamin A Antibody, clone PM6/317 SDS

      Title

      Safety Data Sheet (SDS) 

      Anti-Filamin A Antibody, clone PM6/317 Certificates of Analysis

      TitleLot Number
      Anti-Filamin A, clone PM6/317 - 2345005 2345005
      Anti-Filamin A, clone PM6/317 - 2446767 2446767
      Anti-Filamin A, clone PM6/317 - 1994375 1994375
      Anti-Filamin A, clone PM6/317 - 2025991 2025991
      Anti-Filamin A, clone PM6/317 - 2041573 2041573
      Anti-Filamin A, clone PM6/317 - 2062306 2062306
      Anti-Filamin A, clone PM6/317 - 2112542 2112542
      Anti-Filamin A, clone PM6/317 - 2161126 2161126
      Anti-Filamin A, clone PM6/317 - 2293839 2293839
      Anti-Filamin A, clone PM6/317 - 3172118 3172118

      References

      Reference overviewPub Med ID
      Documentation and localization of force-mediated filamin A domain perturbations in moving cells.
      Nakamura, F; Song, M; Hartwig, JH; Stossel, TP
      Nature communications  5  4656  2014

      Show Abstract
      25120197 25120197
      Vascular and connective tissue anomalies associated with X-linked periventricular heterotopia due to mutations in Filamin A.
      Reinstein, E; Frentz, S; Morgan, T; García-Miñaúr, S; Leventer, RJ; McGillivray, G; Pariani, M; van der Steen, A; Pope, M; Holder-Espinasse, M; Scott, R; Thompson, EM; Robertson, T; Coppin, B; Siegel, R; Bret Zurita, M; Rodríguez, JI; Morales, C; Rodrigues, Y; Arcas, J; Saggar, A; Horton, M; Zackai, E; Graham, JM; Rimoin, DL; Robertson, SP
      European journal of human genetics : EJHG  21  494-502  2013

      Show Abstract
      23032111 23032111
      HCN1 and HCN2 proteins are expressed in cochlear hair cells: HCN1 can form a ternary complex with protocadherin 15 CD3 and F-actin-binding filamin A or can interact with HCN2.
      Ramakrishnan, NA; Drescher, MJ; Khan, KM; Hatfield, JS; Drescher, DG
      The Journal of biological chemistry  287  37628-46  2012

      Show Abstract
      22948144 22948144
      A Monoclonal Antibody SZ-117 That Recognizes Filamin A Derived from Tumor Cells.
      Zibin Bu,Ruifang Liu,Bingxue Shang,Zhifei Cao,Yanyan Pan,Quansheng Zhou,Changgeng Ruan
      Hybridoma (2005)  31  2012

      Show Abstract
      22741587 22741587
      A switch of G protein-coupled receptor binding preference from phosphoinositide 3-kinase (PI3K)-p85 to filamin A negatively controls the PI3K pathway.
      Najib, S; Saint-Laurent, N; Estève, JP; Schulz, S; Boutet-Robinet, E; Fourmy, D; Lättig, J; Mollereau, C; Pyronnet, S; Susini, C; Bousquet, C
      Molecular and cellular biology  32  1004-16  2012

      Show Abstract
      22203038 22203038
      Disease-associated mutations in the actin-binding domain of filamin B cause cytoplasmic focal accumulations correlating with disease severity.
      Philip B Daniel,Tim Morgan,Yasemin Alanay,Emilia Bijlsma,Tae-Joon Cho,Trevor Cole,Felicity Collins,Albert David,Koen Devriendt,Laurence Faivre,Shiro Ikegawa,Sebastien Jacquemont,Milos Jesic,Deborah Krakow,Daniela Liebrecht,Silvia Maitz,Sandrine Marlin,Gilles Morin,Toshiya Nishikubo,Gen Nishimura,Trine Prescott,Gioacchino Scarano,Yousef Shafeghati,Flemming Skovby,Seiji Tsutsumi,Margo Whiteford,Martin Zenker,Stephen P Robertson
      Human mutation  33  2012

      Show Abstract
      22190451 22190451
      Cytoskeletal protein filamin A is a nucleolar protein that suppresses ribosomal RNA gene transcription.
      Deng, W; Lopez-Camacho, C; Tang, JY; Mendoza-Villanueva, D; Maya-Mendoza, A; Jackson, DA; Shore, P
      Proceedings of the National Academy of Sciences of the United States of America  109  1524-9  2012

      Show Abstract
      22307607 22307607
      Alzheimer's disease-linked presenilin mutation (PS1M146L) induces filamin expression and γ-secretase independent redistribution.
      Lu, Q; Ding, K; Frosch, MP; Jones, S; Wolfe, M; Xia, W; Lanford, GW
      Journal of Alzheimer's disease : JAD  22  235-45  2010

      Show Abstract
      20847418 20847418
      Characterization of cytoskeleton-enriched protein fraction of the trabecular meshwork and ciliary muscle cells.
      Inoue, T; Pecen, P; Maddala, R; Skiba, NP; Pattabiraman, PP; Epstein, DL; Rao, PV
      Investigative ophthalmology & visual science  51  6461-71  2010

      Show Abstract
      20631233 20631233
      LL5beta directs the translocation of filamin A and SHIP2 to sites of phosphatidylinositol 3,4,5-triphosphate (PtdIns(3,4,5)P3) accumulation, and PtdIns(3,4,5)P3 localization is mutually modified by co-recruited SHIP2.
      Tetsuji Takabayashi,Min-Jue Xie,Seiji Takeuchi,Motomi Kawasaki,Hideshi Yagi,Masayuki Okamoto,Rahman M Tariqur,Fawzia Malik,Kazuki Kuroda,Chikara Kubota,Shigeharu Fujieda,Takashi Nagano,Makoto Sato
      The Journal of biological chemistry  285  2010

      Show Abstract Full Text Article
      20236936 20236936

      Data Sheet

      Title
      Anti-Filamin A, clone PM6/317 - Data Sheet

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      Categories

      Life Science Research > Antibodies and Assays > Primary Antibodies