Anti-Alpha Dystroglycan Antibody

Evaluated by Western Blotting in mouse brain tissue lysates.

Western Blotting Analysis: 1 ug/mL of this antibody detected Alpha Dystroglycan in mouse brain tissue lysates.

Anti-Alpha Dystroglycan, clone 3D7, Cat. No. MABN2515, is a rat monoclonal antibody that detects Dystroglycan and has been tested for use in Western Blotting.

Western Blotting Analysis: A representative lot detected Alpha Dystroglycan in Western Blotting applications (Ohtsuka, Y., et. al. (2015). Sci Rep. 5:8316; Kanagawa, M., et. al. (2010). J Biol Chem. 285(41):31208-16; Kanagawa, M., et. al. (2016). Cell Rep

Dystroglycan (UniProt: Q62165; also known as Dystrophin-associated glycoprotein 1) is encoded by the Dag1 (also known as Dag-1) gene (Gene ID: 13138) in murine species. Dystroglycan is a component of the dystrophin glycoprotein complex that links the extracellular matrix to the intracellular actin cytoskeleton. It is synthesized with a signal peptide (aa 1-27) that is subsequently cleaved off to generate the mature protein that is further autolytically cleaved (between 651-652) to produce alpha-dystroglycan (aa 28-651) and beta-dystroglycan (aa 652-893). Alpha-dystroglycan is an extracellular peripheral glycoprotein that binds to several extracellular matrix and synaptic proteins such as laminin, agrin, neurexin, and pikachurin. It is reported that its O-mannosyl glycosylation is required for its ligand-binding functions. Beta-dystroglycan is a single-pass type 1 transmembrane protein that plays important roles in connecting the extracellular matrix to the cytoskeleton and serves as a cell adhesion receptor in both muscle and non-muscle tissues. In the cell, beta-dystroglycan binds to dystrophin that is linked to actin cytoskeleton. Hence, alpha/beta dystroglycans act as a molecular axis connecting extracellular matrix with the cytoskeleton across the plasma membrane. Defects in O-mannosyl glycan have been linked to various congenital muscular dystrophies caused by aberrant alpha-dystroglycan glycosylation. (Ref.: Sudo, A., et al. (2018). Human Mol. Genetics. 27(7); 7 1174-1185; Kanagawa, M., et al. (2010). J. Biol. Chem. 285(41); 31208-31216).

Murine alpha-dystroglycan-Fc-Fusion protein.

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