|Calculated MW||97441 Da|
|Other Names||Dystroglycan, Dystrophin-associated glycoprotein 1, Alpha-dystroglycan, Alpha-DG, Beta-dystroglycan, Beta-DG, DAG1|
|Target/Specificity||A synthetic peptide corresponding o residues near the C-terminus of human Beta-Dystroglycan was used as an immunogen.|
|Format||50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||Beta-Dystroglycan Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||The 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. 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.|
|Cellular Location||Alpha-dystroglycan: Secreted, extracellular space|
|Tissue Location||Expressed in a variety of fetal and adult tissues. In epidermal tissue, located to the basement membrane Also expressed in keratinocytes and fibroblasts|
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Provided below are standard protocols that you may find useful for product applications.
The dystroglycan complex is a membrane-spanning complex composed of two subunits, alpha- and beta-dystroglycan. Alpha-dystroglycan is a cell surface peripheral membrane protein which binds to the extracellular matrix (ECM), whereas beta-dystroglycan is an integral membrane protein which anchors alpha-dystroglycan to the cell membrane. The dystroglycan complex provides a tight link between the ECM and cell membrane. Dysfunction of the dystroglycan complex has commonly been implicated in the molecular pathogenesis of severe forms of hereditary neuromuscular diseases, including Duchenne muscular dystrophy, Fukuyama-type congenital muscular dystrophy and sarcoglycanopathy (1). Human dystroglycan is expressed in a variety of fetal and adult tissues. Data suggest that muscle and non-muscle isoforms of dystroglycan differ by carbohydrate moieties but not protein sequence. Therefore variable glycosylation of the conserved protein core might modulate laminin binding (2). beta-dystroglycan has been localized to microvilli structures in a number of cell types where it associates with the cytoskeletal adaptor ezrin, through which it is able to modulate the actin cytoskeleton and induce peripheral filopodia and microvilli (3).
1. Yamada H, et al. Hum Mol Genet 10(15):1563-9, 2001
2. Ibraghimov-Beskrovnaya O, et al. Human Mol Genet 2(10) 1651-7,1993
3. Spence HJ, et al. Hum Mol Genet 13(15):1657-68, 200
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