Lane 1: SkBr3 cell lysate
Lane 2: Mouse placenta tissue lysate
Lane3: Siha cell lysate
Rabbit polyclonal primary
Alpha-dystroglycan Rabbit Polyclonal Antibody (ER1901-72)
Synthetic peptide within human alpha-dystroglycan aa 20-55.
SkBr3 cell lysate, mouse placenta tissue lysate, SkBr3, Rat skeletal muscle tissue, human placenta tissue, Mouse heart tissue, A431.
Store at +4C after thawing. Aliquot store at -20C. Avoid repeated freeze / thaw cycles.
1*PBS (pH7.4), 0.2% BSA, 50% Glycerol. Preservative: 0.05% Sodium Azide.
Peptide affinity purified.
Predicted band size 97 kDa.
156DAG antibody; A3a antibody; AGRNR antibody; Alpha dystroglycan antibody; Alpha-DG antibody; Beta-DG antibody; Beta-dystroglycan antibody; DAG antibody; Dag1 antibody; DAG1_HUMAN antibody; Dystroglycan 1 (dystrophin associated glycoprotein 1) antibody; Dystroglycan antibody; Dystrophin associated glycoprotein 1 antibody; Dystrophin-associated glycoprotein 1 antibody; OTTHUMP00000210857 antibody; OTTHUMP00000210858 antibody
Expressed in a variety of fetal and adult tissues. In epidermal tissue, located to the basement membrane. Also expressed in keratinocytes and fibroblasts.
O-glycosylated. POMGNT1 catalyzes the initial addition of N-acetylglucosamine, giving rise to the GlcNAc(beta1-2)Man(alpha1-)O-Ser/Thr moiety and thus providing the necessary basis for the addition of further carbohydrate moieties. 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-317, Thr-319 and 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 (LARGE1) 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.
Cell junction. Cytoplasm. Cytoskeleton. Membrane. Secreted. Synapse. Nucleus.
Dystroglycan (DG) is a cell surface receptor for several extracellular matrix molecules including laminins, Agrin and Perlecan. Dystroglycan function is required for the formation of basement membranes in early development and the organization of Laminin on the cell surface. α-dystroglycan is a membrane- associated, extracellular glycoprotein that is anchored to the cell-membrane by binding to the transmembrane glycoprotein α-dystroglycan to form an α/β-dystroglycan-complex. Additionally, dystroglycan is part of a multimolecular complex, where it associates with dystrophin, at the sarcolemma, to form the dystrophin-associated protein complex, or with utrophin, at the neuromuscular junction, to form the utrophin-associated protein complex. Dystroglycan is also thought to participate in the clustering of nicotinic acetylcholine receptors at the neuromuscular junction.