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Overview

  • Product nameDAG1 protein
  • Protein descriptionRecombinant fragment (aa 31-140) of Human DAG1 with proprietary tag. (M. Wt 37.73kDa, UniProt Q14118).
  • Uniprot accessionQ14118
  • Molecular weight37.730kDa inclusive of tags
  • Protein length110 amino acids
  • Expression hostWheat germ

    • Properties

  • Biological activityuseful for Antibody Production and Protein Array
  • FormLiquid
  • Storage instructionsShipped on dry ice. Upon delivery aliquot and store at -80ºC. Avoid freeze / thaw cycles.
  • Storage bufferpH: 8.00
    Constituents: 0.79% Tris HCl, 0.31% Glutathione
    Note: Reduced glutathione
  • Concentration information loading...
  • Additional notesBest use within three months from the date of receipt of this protein.
  • Research Areas

    • Applications

    Our Abpromise guarantee covers the use of ab112278 in the following tested applications.

    The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.

    Application Notes
    WB WB: Use at an assay dependent concentration. Predicted molecular weight: 37.73 kDa. This antibody has only been tested in WB against the recombinant fragment used as immunogen. We have no data on the detection of endogenous protein.
    PepArr PepArr: Use at an assay dependent concentration.
    SDS-PAGE SDS-PAGE: Use at an assay dependent concentration.
    ELISA ELISA: Use at an assay dependent concentration.

    Protein info

    • Alternative names
        156DAGA3aAGRNR
        Alpha-DGBeta-DGBeta-dystroglycanDAGDag1DAG1_HUMANDystroglycanDystroglycan 1 (dystrophin-associated glycoprotein 1)Dystrophin-associated glycoprotein 1OTTHUMP00000210857OTTHUMP00000210858
      see all
  • FunctionThe dystroglycan complex is involved in a number of processes including laminin and basement membrane assembly, sarcolemmal stability, cell survival, peripheral nerve myelination, nodal structure, cell migration, and epithelial polarization.
    Alpha-dystroglycan is an extracellular peripheral glycoprotein that acts as a receptor for both extracellular matrix proteins containing laminin-G domains, and for certain adenoviruses. Receptor for laminin-2 (LAMA2) and agrin in peripheral nerve Schwann cells. Also acts as a receptor for M.leprae in peripheral nerve Schwann cells but only in the presence of the G-domain of LAMA2, and for lymphocytic choriomeningitis virus, Old World Lassa fever virus, and clade C New World arenaviruses.
    Beta-dystroglycan is a transmembrane protein that plays important roles in connecting the extracellular matrix to the cytoskeleton. Acts as a cell adhesion receptor in both muscle and non-muscle tissues. Receptor for both DMD and UTRN and, through these interactions, scaffolds axin to the cytoskeleton. Also functions in cell adhesion-mediated signaling and implicated in cell polarity.
  • Tissue specificityExpressed in a variety of fetal and adult tissues. In epidermal tissue, located to the basement membrane. Also expressed in keratinocytes and fibroblasts.
  • Involvement in diseaseDefects in DAG1 are the cause of muscular dystrophy-dystroglycanopathy limb-girdle type C7 (MDDGC7) [MIM:613818]. An autosomal recessive muscular dystrophy showing onset in early childhood, and associated with mental retardation without structural brain anomalies. Note=MDDGC7 is caused by DAG1 mutations that interfere with normal post-translational processing, resulting in defective DAG1 glycosylation and impaired interactions with extracellular-matrix components. Other muscular dystrophy-dystroglycanopathies are caused by defects in enzymes involved in protein O-glycosylation.
  • Sequence similaritiesContains 1 peptidase S72 domain.
  • Post-translational
    modifications    O- and N-glycosylated. Alpha-dystroglycan is heavily O-glycosylated comprising of up to two thirds of its mass and the carbohydrate composition differs depending on tissue type. Mucin-type O-glycosylation is important for ligand binding activity. O-mannosylation of alpha-DAG1 is found in high abundance in both brain and muscle where the most abundant glycan is Sia-alpha-2-3-Gal-beta-1-4-Glc-NAc-beta-1-2-Man. In muscle, glycosylation on Thr-379 by a phosphorylated O-mannosyl glycan with the structure 2-(N-acetylamido)-2-deoxygalactosyl-beta-1,3-2-(N-acetylamido)-2-deoxyglucosyl-beta-1,4-6-phosphomannose is mediated by like-acetylglucosaminyltransferase (LARGE) protein and is required for laminin binding. O-mannosylation is also required for binding lymphocytic choriomeningitis virus, Old World Lassa fever virus, and clade C New World arenaviruses. The O-glycosyl hexose on Thr-367, Thr-369, Thr-372, Thr-381 and Thr-388 is probably mannose. O-glycosylated in the N-terminal region with a core 1 or possibly core 8 glycan. The beta subunit is N-glycosylated.
    Autolytic cleavage produces the alpha and beta subunits. In cutaneous cells, as well as in certain pathological conditions, shedding of beta-dystroglcan can occur releasing a peptide of about 30 kDa.
    SRC-mediated phosphorylation of the PPXY motif of the beta subunit recruits SH2 domain-containing proteins, but inhibits binding to WWW domain-containing proteins, DMD and UTRN. This phosphorylation also inhibits nuclear entry.
  • Cellular localizationSecreted > extracellular space and Cell membrane. Cytoplasm > cytoskeleton. Nucleus > nucleoplasm. The monomeric form translocates to the nucleus via the action of importins and depends on RAN. Nuclear transport is inhibited by Tyr-892 phosphorylation. In skeletal muscle, this phosphorylated form locates to a vesicular internal membrane compartment. In peripheral nerves, localizes to the Schwann cell membrane. Colocalizes with ERM proteins in Schwann-cell microvilli.

    • Target information above from: UniProt accession Q14118 The UniProt Consortium
    The Universal Protein Resource (UniProt) in 2010
    Nucleic Acids Res. 38:D142-D148 (2010) .

    Information by UniProt

    DAG1 protein images

    • SDS-PAGE - DAG1 protein (ab112278)
      SDS-PAGE - DAG1 protein (ab112278)
      12.5% SDS-PAGE Stained with Coomassie Blue with recombinant protein.

    References for DAG1 protein (ab112278)

    ab112278 has not yet been referenced specifically in any publications.

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