Human Dystroglycan Alexa Fluor™ Plus 488‑conjugated Antibody

Dystroglycan, also DAG-1 (Dystrophin-associated glycoprotein 1) is a 180-200 kDa heterodimeric adhesion molecule that links the cell cytoskeleton to the extracellular matrix. It is found on skeletal muscle, cardiac muscle, fibroblasts, smooth muscle and keratinocytes. DAG-1 binds multiple matrix molecules, including laminin-1 and -2, agrin, and perlecan. Intracellularly, the cytoplasmic tail of DAG-1 contributes to a large 400 kDa complex that interacts with the cytoskeleton. The human DAG-1 preprocursor is a type I transmembrane protein 895 amino acids (aa) in length. It contains a 27 aa signal sequence plus an 868 aa proform that undergoes autocatalysis to generate a 626 aa alpha -chain (aa 28-653), and a 242 aa beta -chain. Mature DAG-1 is a heterodimer composed of noncovalently linked alpha ‑ and beta ‑chains. The alpha -chain possesses one potential Ig-like domain (aa 64-162), a mucin-like region (aa 316-485), and a peptidase S72 domain (aa 500-733). It is O‑glycosylated and runs from 100-160 kDa in SDS-PAGE. The beta -chain is N-glycosylated and runs at 42-44 kDa in SDS-Page. It possesses a short 95 aa extracellular region (aa 654-749) plus a 120 aa cytoplasmic domain (aa 776-895). Membrane cleavage of the beta -chain causes dissociation of the heterodimer and generates a 30 kDa truncated form. Over aa 28-749, human DAG-1 shares 93% aa identity with mouse DAG-1.