Dystroglycan was originally isolated from skeletal muscle as an integral membrane component of the dystrophin-glycoprotein complex. In addition to skeletal muscle, dystroglycan is strongly expressed in heart and smooth muscle, as well as many non-muscle tissues including brain and peripheral nerve. The dystroglycan 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. Dystroglycan consists of two subunits – alpha and beta, which are translated from a single mRNA as a propeptide that is proteolytically cleaved into two noncovalently associated proteins. Alpha-dystroglycan is a 156 kDa extracellular peripheral glycoprotein, while beta-dystroglycan is a 43 kDa transmembrane protein. The 43 kDa beta-dystroglycan can be cleaved into a 30 kDa form.
Clone
2B1G12
Isotype
IgG1
Host species
Mouse
Species Reactivity
Human, mouse, rat, pig
Cellular Localization
secreted, membrane
Positive Control
heart tissue, skeletal muscle tissue lysate
Applications
ELISA, Flow Cyt., IHC, WB
Intended Use
Research Use Only