05-298
Anti-α-Dystroglycan Antibody, clone VIA4-1
culture supernatant, clone VIA4-1, Upstate®
Szinonimák:
Anti-156DAG, Anti-A3a, Anti-AGRNR, Anti-DAG, Anti-LGMDR16, Anti-MDDGA9, Anti-MDDGC7, Anti-MDDGC9
Bejelentkezésa Szervezeti és Szerződéses árazás megtekintéséhez
Összes fotó(1)
About This Item
UNSPSC kód:
12352203
eCl@ss:
32160702
NACRES:
NA.41
Javasolt termékek
biológiai forrás
mouse
Minőségi szint
antitest forma
culture supernatant
antitest terméktípus
primary antibodies
klón
VIA4-1, monoclonal
faj reaktivitás
guinea pig, rabbit, rat, human, mouse, canine
gyártó/kereskedő neve
Upstate®
technika/technikák
immunohistochemistry: suitable
western blot: suitable
izotípus
IgG1
NCBI elérési szám
UniProt elérési szám
kiszállítva
wet ice
célzott transzláció utáni módosítás
unmodified
Géninformáció
human ... DAG1(1605)
Általános leírás
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.
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.
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.
Egyediség
Recognizes α-dystroglycan/LARGE-glycan.
Immunogén
Rabbit skeletal muscle membrane preparation
Alkalmazás
Detect α-Dystroglycan using this Anti-α-Dystroglycan Antibody, clone VIA4-1. This antibody has been published and validated for use in IH and WB.
Research Category
Cell Structure
Cell Structure
Research Sub Category
Cytoskeleton
Cytoskeleton
Minőség
routinely evaluated on rabbit skeletal muscle in a western blot.
Cél megnevezése
156 kDa
Fizikai forma
Culture supernatant containing 0.05% sodium azide.
Unpurified
Tárolás és stabilitás
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.
Analízis megjegyzés
Control
Mouse, rat and human skeletal muscle tissue extracts or DU 145 (human prostate carcinoma tumor) cell lysate
Mouse, rat and human skeletal muscle tissue extracts or DU 145 (human prostate carcinoma tumor) cell lysate
Egyéb megjegyzések
Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.
Jogi információk
UPSTATE is a registered trademark of Merck KGaA, Darmstadt, Germany
Jogi nyilatkozat
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.
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Tárolási osztály kódja
12 - Non Combustible Liquids
WGK
WGK 2
Analitikai tanúsítványok (COA)
Analitikai tanúsítványok (COA) keresése a termék sarzs-/tételszámának megadásával. A sarzs- és tételszámok a termék címkéjén találhatók, a „Lot” vagy „Batch” szavak után.
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Mechanistic distinctions between agrin and laminin-1 induced aggregation of acetylcholine receptors.
Lara K Lee et al.
BMC neuroscience, 3, 10-10 (2002-08-17)
One of the earliest steps in synaptogenesis at the neuromuscular junction is the aggregation of nicotinic acetylcholine receptors at the postsynaptic membrane. This study presents quantitative analyses of receptor and alpha-Dystroglycan aggregation in response to agrin and laminin-1, alone or
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.
The Journal of Neuroscience, 30, 9771-9781 (2010)
Dystrophin constitutes 5% of membrane cytoskeleton in skeletal muscle.
Ohlendieck, K and Campbell, K P
Febs Letters, 283, 230-234 (1991)
Genri Kawahara et al.
Human molecular genetics, 19(4), 623-633 (2009-12-04)
Various muscular dystrophies are associated with the defective glycosylation of alpha-dystroglycan and are known to result from mutations in genes encoding glycosyltransferases. Fukutin-related protein (FKRP) was identified as a homolog of fukutin, the defective protein in Fukuyama-type congenital muscular dystrophy
S Sugita et al.
The Journal of cell biology, 154(2), 435-445 (2001-07-27)
In nonneuronal cells, the cell surface protein dystroglycan links the intracellular cytoskeleton (via dystrophin or utrophin) to the extracellular matrix (via laminin, agrin, or perlecan). Impairment of this linkage is instrumental in the pathogenesis of muscular dystrophies. In brain, dystroglycan
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