α-dystroglycan Antibody (VIA41): sc-53986

α-dystroglycan Antibody (VIA41) is a mouse monoclonal IgG1 antibody that detects α-dystroglycan in mouse, rat, human, bovine, rabbit, and canine samples through applications such as western blotting (WB) and immunoprecipitation (IP). α-dystroglycan is a crucial membrane-associated glycoprotein that plays a significant role in the formation of the dystrophin-associated protein complex, which is essential for maintaining the structural integrity of muscle cells. α-dystroglycan (VIA41) antibody recognizes a protein primarily located on the cell surface, where α-dystroglycan interacts with various extracellular matrix components, including laminins, Agrin, and Perlecan, facilitating the organization of these molecules into functional structures. The proper localization of α-dystroglycan is vital for the clustering of nicotinic acetylcholine receptors at the neuromuscular junction, which is critical for effective synaptic transmission and muscle contraction. Disruptions in α-dystroglycan function or its interactions can lead to severe muscular dystrophies and other neuromuscular disorders, highlighting the importance of α-dystroglycan in both development and muscle physiology. α-dystroglycan (VIA41) monoclonal antibody serves as an invaluable tool for researchers studying this protein in various biological processes and disease states.

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α-dystroglycan Antibody (VIA41) References:

1. The multiple affinities of α-dystroglycan.  |  Sciandra, F., et al. 2013. Curr Protein Pept Sci. 14: 626-34. PMID: 24206164
2. Glycobiology of α-dystroglycan and muscular dystrophy.  |  Endo, T. 2015. J Biochem. 157: 1-12. PMID: 25381372
3. Structural flexibility of human α-dystroglycan.  |  Covaceuszach, S., et al. 2017. FEBS Open Bio. 7: 1064-1077. PMID: 28781947
4. Analysis of α-Dystroglycan/LG Domain Binding Modes: Investigating Protein Motifs That Regulate the Affinity of Isolated LG Domains.  |  Dempsey, CE., et al. 2019. Front Mol Biosci. 6: 18. PMID: 30984766
5. Lassa Fever Virus Binds Matriglycan-A Polymer of Alternating Xylose and Glucuronate-On α-Dystroglycan.  |  Joseph, S. and Campbell, KP. 2021. Viruses. 13: PMID: 34578260
6. Sarcospan increases laminin-binding capacity of α-dystroglycan to ameliorate DMD independent of Galgt2.  |  Mamsa, H., et al. 2022. Hum Mol Genet. 31: 718-732. PMID: 34581784
7. Deficiency of Glycosylated α-Dystroglycan in Ventral Hippocampus Bridges the Destabilization of Gamma-Aminobutyric Acid Type A Receptors With the Depressive-like Behaviors of Male Mice.  |  Xie, WL., et al. 2022. Biol Psychiatry. 91: 593-603. PMID: 35063187
8. N-terminal domain on dystroglycan enables LARGE1 to extend matriglycan on α-dystroglycan and prevents muscular dystrophy.  |  Okuma, H., et al. 2023. Elife. 12: PMID: 36723429
9. Broad spectrum of phenotype and genotype in Korean α-dystroglycan related muscular dystrophy presenting to a tertiary pediatric neuromuscular center.  |  Ko, YJ., et al. 2023. Neuromuscul Disord. 33: 425-431. PMID: 37087885
10. The α-dystroglycan N-terminus is a broad-spectrum antiviral agent against SARS-CoV-2 and enveloped viruses.  |  Bigotti, MG., et al. 2024. Antiviral Res. 224: 105837. PMID: 38387750

The preferred α-dystroglycan antibody is α-dystroglycan Antibody (IIH6): sc-53987.