α-Dystroglycan Antibody, clone VIA4-1 | EMD Millipore 05-298 product information

This webpage contains legacy information. The product is either no longer available from the supplier or has been delisted at Labome.

product summary

company name :

EMD Millipore

other brands :

Oncogene Research Products, Calbiochem, Novagen, Merck, Upstate Biotechnology, Chemicon, LINCO, Novabiochem, Guava

product type :

antibody

product name :

α-Dystroglycan Antibody, clone VIA4-1

catalog :

05-298

quantity :

200 μL

clonality :

monoclonal

host :

mouse

conjugate :

nonconjugated

clone name :

VIA4-1

The same clone is also sold as:

Santa Cruz Biotechnology: sc-53986
LifeSpan Biosciences: LS-C36215

reactivity :

human, mouse

application :

western blot, immunohistochemistry, flow cytometry, immunohistochemistry - paraffin section, immunohistochemistry - frozen section

citations: 27

Published Application/Species/Sample/Dilution	Reference
western blot; mouse; 1:200; loading ...; fig 2e	Rubio Fernández M, Uribe M, Vicente Tejedor J, Germain F, Susín Lara C, Quereda C, et al. Impairment of photoreceptor ribbon synapses in a novel Pomt1 conditional knockout mouse model of dystroglycanopathy. Sci Rep. 2018;8:8543 pubmed publisher
immunohistochemistry - paraffin section; human; 1:50	Rickelt S, Hynes R. Antibodies and methods for immunohistochemistry of extracellular matrix proteins. Matrix Biol. 2018;71-72:10-27 pubmed publisher
immunohistochemistry - frozen section; human; loading ...; fig 7fs2i	Praissman J, Willer T, Sheikh M, Toi A, Chitayat D, Lin Y, et al. The functional O-mannose glycan on ?-dystroglycan contains a phospho-ribitol primed for matriglycan addition. elife. 2016;5: pubmed publisher
immunohistochemistry; mouse western blot; mouse	Domi T, Porrello E, Velardo D, Capotondo A, Biffi A, Tonlorenzi R, et al. Mesoangioblast delivery of miniagrin ameliorates murine model of merosin-deficient congenital muscular dystrophy type 1A. Skelet Muscle. 2015;5:30 pubmed publisher
flow cytometry; human immunohistochemistry; human	Stevens E, Torelli S, Feng L, Phadke R, Walter M, Schneiderat P, et al. Flow cytometry for the analysis of ?-dystroglycan glycosylation in fibroblasts from patients with dystroglycanopathies. PLoS ONE. 2013;8:e68958 pubmed publisher
western blot; mouse; fig 7	Lien C, Mohanta S, Frontczak Baniewicz M, Swinny J, Zablocka B, Gorecki D. Absence of glial ?-dystrobrevin causes abnormalities of the blood-brain barrier and progressive brain edema. J Biol Chem. 2012;287:41374-85 pubmed publisher
	Balci Hayta B, Talim B, Kale G, Dincer P. LARGE expression in different types of muscular dystrophies other than dystroglycanopathy. BMC Neurol. 2018;18:207 pubmed publisher
	. 15th International Congress on Neuromuscular Diseases, July 6 - 10, 2018 Vienna, Austria. J Neuromuscul Dis. 2018;5:S1-S408 pubmed publisher
	El Battrawy I, Zhao Z, Lan H, Li X, YÃ¼cel G, Lang S, et al. Ion Channel Dysfunctions in Dilated Cardiomyopathy in Limb-Girdle Muscular Dystrophy. Circ Genom Precis Med. 2018;11:e001893 pubmed publisher
	Osborn D, Pond H, Mazaheri N, Dejardin J, Munn C, Mushref K, et al. Mutations in INPP5K Cause a Form of Congenital Muscular Dystrophy Overlapping Marinesco-Sjögren Syndrome and Dystroglycanopathy. Am J Hum Genet. 2017;100:537-545 pubmed publisher
	Jensen L, Andersen L, SchrÃ¸der H, Frandsen U, SjÃ¸gaard G. Neuronal nitric oxide synthase is dislocated in type I fibers of myalgic muscle but can recover with physical exercise training. Biomed Res Int. 2015;2015:265278 pubmed publisher
	Dong M, Noguchi S, Endo Y, Hayashi Y, Yoshida S, Nonaka I, et al. DAG1 mutations associated with asymptomatic hyperCKemia and hypoglycosylation of Î±-dystroglycan. Neurology. 2015;84:273-9 pubmed publisher
	Martínez Zárate A, Martínez Vieyra I, Alonso Rangel L, Cisneros B, Winder S, Cerecedo D. Dystroglycan depletion inhibits the functions of differentiated HL-60 cells. Biochem Biophys Res Commun. 2014;448:274-80 pubmed publisher
	Raphael A, Couthouis J, Sakamuri S, Siskind C, Vogel H, Day J, et al. Congenital muscular dystrophy and generalized epilepsy caused by GMPPB mutations. Brain Res. 2014;1575:66-71 pubmed publisher
	Hafner P, Bonati U, Fischmann A, Schneider J, Frank S, Morris Rosendahl D, et al. Skeletal muscle MRI of the lower limbs in congenital muscular dystrophy patients with novel POMT1 and POMT2 mutations. Neuromuscul Disord. 2014;24:321-4 pubmed publisher
	Riisager M, Duno M, Hansen F, Krag T, Vissing C, Vissing J. A new mutation of the fukutin gene causing late-onset limb girdle muscular dystrophy. Neuromuscul Disord. 2013;23:562-7 pubmed publisher
	Blaeser A, Keramaris E, Chan Y, Sparks S, Cowley D, Xiao X, et al. Mouse models of fukutin-related protein mutations show a wide range of disease phenotypes. Hum Genet. 2013;132:923-34 pubmed publisher
	Yu M, He Y, Wang K, Zhang P, Zhang S, Hu H. Adeno-associated viral-mediated LARGE gene therapy rescues the muscular dystrophic phenotype in mouse models of dystroglycanopathy. Hum Gene Ther. 2013;24:317-30 pubmed publisher
	Cirak S, Foley A, Herrmann R, Willer T, Yau S, Stevens E, et al. ISPD gene mutations are a common cause of congenital and limb-girdle muscular dystrophies. Brain. 2013;136:269-81 pubmed publisher
	Bangratz M, Sarrazin N, Devaux J, Zambroni D, Echaniz Laguna A, Rene F, et al. A mouse model of Schwartz-Jampel syndrome reveals myelinating Schwann cell dysfunction with persistent axonal depolarization in vitro and distal peripheral nerve hyperexcitability when perlecan is lacking. Am J Pathol. 2012;180:2040-55 pubmed publisher
	Street R, Mucowski S, Urrabaz Garza R, O Boyle K, Snyder R, Theiler R. Dystroglycan expression in human placenta: basement membrane localization and subunit distribution change between the first and third trimester. Reprod Sci. 2012;19:282-9 pubmed publisher
	Zhang Z, Zhang P, Hu H. LARGE expression augments the glycosylation of glycoproteins in addition to ?-dystroglycan conferring laminin binding. PLoS ONE. 2011;6:e19080 pubmed publisher
	Clarke N, Maugenre S, Vandebrouck A, Urtizberea J, Willer T, Peat R, et al. Congenital muscular dystrophy type 1D (MDC1D) due to a large intragenic insertion/deletion, involving intron 10 of the LARGE gene. Eur J Hum Genet. 2011;19:452-7 pubmed publisher
	Edwards M, Mammadova Bach E, Alpy F, Klein A, Hicks W, Roux M, et al. Mutations in Lama1 disrupt retinal vascular development and inner limiting membrane formation. J Biol Chem. 2010;285:7697-711 pubmed publisher
	Lathia J, Patton B, Eckley D, Magnus T, Mughal M, Sasaki T, et al. Patterns of laminins and integrins in the embryonic ventricular zone of the CNS. J Comp Neurol. 2007;505:630-43 pubmed
	Yang D, Bierman J, Tarumi Y, Zhong Y, Rangwala R, Proctor T, et al. Coordinate control of axon defasciculation and myelination by laminin-2 and -8. J Cell Biol. 2005;168:655-66 pubmed
	Sugita S, Saito F, Tang J, Satz J, Campbell K, Sudhof T. A stoichiometric complex of neurexins and dystroglycan in brain. J Cell Biol. 2001;154:435-45 pubmed

product information

Catalog Number :

05-298

Subcategory :

Cell Structure

Product Name :

Anti-α-Dystroglycan Antibody, clone VIA4-1

Product Type :

Antibodies

Clonality :

Monoclonal Antibody

Gene ID :

Q14118

Host Name :

Mouse

Antigen :

α-Dystroglycan

Clone :

VIA4-1

Conjugate :

Culture Supernatant

Isotype :

IgG1

Product Description :

Anti-α-Dystroglycan Antibody, clone VIA4-1

Cross Reactivity :

Canine;Guinea Pig;Human;Mouse;Rat;Rabbit

Background :

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.

Immunogen :

Rabbit skeletal muscle membrane preparation

Specificity :

Recognizes α-dystroglycan/LARGE-glycan.

Package Size :

200 μL

Uses :

Immunohistochemistry;Western Blotting

Storage :

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.