05-298 | Anti-α-Dystroglycan Antibody, clone VIA4-1

WB: Rabbit skeletal muscle lysate was probed with anti-α Dystroglycan (1:2000).
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      Key Spec Table

      Species Reactivity Key Applications Host Format Antibody Type
      Rb, Ca, Gp, H, M, RWB, IHCMCulture SupernatantMonoclonal Antibody
      Catalogue Number 05-298
      Brand Family Upstate
      Trade Name
      • Upstate
      Description Anti-α-Dystroglycan Antibody, clone VIA4-1
      Overview Note: This product may be used for research purposes only. Diagnostic use of this product requires a license from the University of Iowa Research Foundation, 214 Technology Innovation Center, Iowa City, IA 52242.
      Background Information Dystroglycan is one of the dystrophin-associated glycoproteins, which is encoded by a 5.5 kb transcript in Homo sapiens by chromosome 3. There are two exons that are separated by a large intron. The spliced exons codes for a protein product is finally cleaved into two non-covalently associated subunits, α (N-terminal) and β (C-terminal). In skeletal muscle the dystroglycan complex works as a transmembrane linkage between the extracellular matrix and the cytoskeleton. α-dystroglycan is extracellular and binds to merosin (α-2 laminin) in the basement membrane, while β-dystroglycan is a transmembrane protein and binds to dystrophin, which is a large rod-like cytoskeletal protein, absent in Duchenne muscular dystrophy patients. Dystrophin binds to intracellular actin cables. In this way, the dystroglycan complex, which links the extracellular matrix to the intracellular actin cables, is thought to provide structural integrity in muscle tissues. The dystroglycan complex is also known to serve as an agrin receptor in muscle, where it may regulate agrin-induced acetylcholine receptor clustering at the neuromuscular junction. There is also evidence that suggests the function of dystroglycan as a part of the signal transduction pathway because it is shown that Grb2, a mediator of the Ras-related signal pathway, can interact with the cytoplasmic domain of dystroglycan. In general, aberrant expression of dystrophin-associated protein complex underlies the pathogenesis of Duchenne muscular dystrophy, Becker muscular dystrophy and severe childhood autosomal recessive muscular dystrophy. Interestingly, no genetic disease has been described for either α- or β-dystroglycan.
      Dystroglycan is widely distributed in non-muscle tissues as well as in muscle tissues. During epithelial morphogenesis of kidney, the dystroglycan complex is shown to act as a receptor for the basement membrane. Dystroglycan expression in Mus musculus brain and neural retina has also been reported. However, the physiological role of dystroglycan in non-muscle tissues has remained unclear.
      Product Information
      Format Culture Supernatant
      Specificity Recognizes α-dystroglycan/LARGE-glycan.
      • Mouse, rat and human skeletal muscle tissue extracts or DU 145 (human prostate carcinoma tumor) cell lysate
      Presentation Culture supernatant containing 0.05% sodium azide.
      Application Detect α-Dystroglycan using this Anti-α-Dystroglycan Antibody, clone VIA4-1 validated for use in IH & WB.
      Key Applications
      • Western Blotting
      • Immunohistochemistry
      Biological Information
      Immunogen Rabbit skeletal muscle membrane preparation
      Clone VIA4-1
      Concentration Please refer to the Certificate of Analysis for the lot-specific concentration.
      Host Mouse
      Specificity Recognizes α-dystroglycan/LARGE-glycan.
      Isotype IgG1
      Species Reactivity Rabbit Canine Guinea Pig Human Mouse Rat
      Antibody Type Monoclonal Antibody
      Entrez Gene Number
      Entrez Gene Summary Dystroglycan is a laminin binding component of the dystrophin-glycoprotein complex which provides a linkage between the subsarcolemmal cytoskeleton and the extracellular matrix. Dystroglycan 1 is a candidate gene for the site of the mutation in autosomal recessive muscular dystrophies. The dramatic reduction of dystroglycan 1 in Duchenne muscular dystrophy leads to a loss of linkage between the sarcolemma and extracellular matrix, rendering muscle fibers more susceptible to necrosis. Dystroglycan also functions as dual receptor for agrin and laminin-2 in the Schwann cell membrane. The muscle and nonmuscle isoforms of dystroglycan differ by carbohydrate moieties but not protein sequence.
      Gene Symbol
      • 156DAG
      • DAG1
      • A3a
      • DAG
      • beta-dystroglycan
      • alpha-dystroglycan
      • AGRNR
      Purification Method Unpurified
      UniProt Number
      UniProt Summary FUNCTION: SwissProt: Q14118 # Forms part of the dystrophin-associated protein complex (DAPC) which may link the cytoskeleton to the extracellular matrix. Alpha-dystroglycan functions as a laminin receptor. Binds to several types of arenaviruses. Is a target for the entry of Mycobacterium leprae into peripheral nerve Schwann cells.
      SIZE: 895 amino acids; 97581 Da
      SUBUNIT: Interacts with SGCD (By similarity). Interacts with AGR2 and AGR3.
      SUBCELLULAR LOCATION: Alpha-dystroglycan: Secreted, extracellular space. & Beta-dystroglycan: Cell membrane; Single- pass type I membrane protein.
      TISSUE SPECIFICITY: Expressed in a variety of fetal and adult tissues.
      Physicochemical Information
      Materials Information
      Toxicological Information
      Safety Information according to GHS
      Safety Information
      Product Usage Statements
      Quality Assurance routinely evaluated on rabbit skeletal muscle in a western blot.
      Usage Statement
      • Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
      Storage and Shipping Information
      Storage Conditions Maintain for 2 years at -20°C from date of shipment. Aliquot to avoid repeated freezing and thawing. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
      Packaging Information
      Material Size 200 µL
      Transport Information
      Supplemental Information




      Certificates of Analysis

      TitleLot Number
      Anti-#945;-Dystroglycan, clone VIA4-1 - 2150158 2150158
      Anti-#945;-Dystroglycan, clone VIA4-1 - DAM1834934 DAM1834934
      Anti--Dystroglycan, clone VIA4-1 - 1951974 1951974
      Anti--Dystroglycan, clone VIA4-1 - 1993896 1993896
      Anti--Dystroglycan, clone VIA4-1 - 2089509 2089509
      Anti--Dystroglycan, clone VIA4-1 - DAM1408802 DAM1408802
      Anti--Dystroglycan, clone VIA4-1 - DAM1632063 DAM1632063
      Anti--Dystroglycan, clone VIA4-1 - DAM1764385 DAM1764385
      Anti--Dystroglycan, clone VIA4-1 - DAM179797926 DAM179797926
      Anti--Dystroglycan, clone VIA4-1 - JBC1863401 JBC1863401
      Anti--Dystroglycan, clone VIA4-1 - JBC1925515 JBC1925515
      Anti-a-Dystroglycan, clone VIA4-1 - DAM1467543 DAM1467543
      Anti-alpha-Dystroglycan, clone VIA4-1 - DAM1543693 DAM1543693
      Anti-alpha;-Dystroglycan, clone VIA4-1 - 15571 15571
      Anti-alpha;-Dystroglycan, clone VIA4-1 - 16753 16753
      Anti-alpha;-Dystroglycan, clone VIA4-1 - 18428 18428
      Anti-alpha;-Dystroglycan, clone VIA4-1 - 20824 20824
      Anti-alpha;-Dystroglycan, clone VIA4-1 - 22705 22705
      Anti-alpha;-Dystroglycan, clone VIA4-1 - 24147 24147
      Anti-alpha;-Dystroglycan, clone VIA4-1 - 25133 25133
      Anti-alpha;-Dystroglycan, clone VIA4-1 - 29490 29490
      Anti-alpha;-Dystroglycan, clone VIA4-1 - 30002 30002
      Anti-alpha;-Dystroglycan, clone VIA4-1 - 31718 31718
      Anti-alpha;-Dystroglycan, clone VIA4-1 - 32533 32533
      Anti-alpha;-Dystroglycan, clone VIA4-1 - 32685 32685
      Anti-α-Dystroglycan/LARGE-glycan, clone VIA4-1 2470899
      Anti-α-Dystroglycan/LARGE-glycan, clone VIA4-1 - 2384724 2384724
      Anti-α-Dystroglycan/LARGE-glycan, clone VIA4-1 -2500624 2500624
      Anti-α-Dystroglycan/LARGE-glycan, clone VIA4-1 -2552275 2552275


      Reference overviewApplicationSpeciesPub Med ID
      Quiescence and activation of stem and precursor cell populations in the subependymal zone of the mammalian brain are associated with distinct cellular and extracellular matrix signals.
      Kazanis, Ilias, et al.
      J. Neurosci., 30: 9771-81 (2010) 2010

      Show Abstract
      Synapse formation and clustering of neuroligin-2 in the absence of GABAA receptors.
      Patrizi, Annarita, et al.
      Proc. Natl. Acad. Sci. U.S.A., 105: 13151-6 (2008) 2008

      Show Abstract
      Worldwide distribution and broader clinical spectrum of muscle-eye-brain disease.
      Taniguchi, Kiyomi, et al.
      Hum. Mol. Genet., 12: 527-34 (2003) 2003

      Show Abstract
      Immunohistochemistry (Tissue)12588800
      Dystroglycan is present in rat thyroid and rat thyroid cells and responds to thyrotropin.
      Collins, B J, et al.
      Endocrinology, 142: 3152-62 (2001) 2001

      Show Abstract
      Immunocytochemistry, Immunoblotting (Western)11416038
      A stoichiometric complex of neurexins and dystroglycan in brain
      Sugita, S., et al
      J Cell Biol, 154:435-45 (2001) 2001

      Immunocytochemistry, Immunoblotting (Western)11470830
      Dystrophic phenotype induced in vitro by antibody blockade of muscle alpha-dystroglycan-laminin interaction
      Brown, S. C., et al
      J Cell Sci, 112 ( Pt 2):209-16 (1999) 1999

      MEK kinase 1, a substrate for DEVD-directed caspases, is involved in genotoxin-induced apoptosis.
      Widmann, C, et al.
      Mol. Cell. Biol., 18: 2416-29 (1998) 1998

      Show Abstract
      Immunoblotting (Western)9528810
      Membrane organization of the dystrophin-glycoprotein complex.
      Ervasti, J M and Campbell, K P
      Cell, 66: 1121-31 (1991) 1991

      Show Abstract
      Dystrophin constitutes 5% of membrane cytoskeleton in skeletal muscle.
      Ohlendieck, K and Campbell, K P
      FEBS Lett., 283: 230-4 (1991) 1991

      Show Abstract
      Deficiency of a glycoprotein component of the dystrophin complex in dystrophic muscle.
      Ervasti, J M, et al.
      Nature, 345: 315-9 (1990) 1990

      Show Abstract