R Recombinant
Recombinant: Superior lot-to-lot consistency, continuous supply, and animal-free manufacturing.
Phospho-β-Dystroglycan (Tyr892) (E6T9O) Rabbit mAb #32248
Filter:
- WB
- IP
Supporting Data
| REACTIVITY | H M R |
| SENSITIVITY | Endogenous |
| MW (kDa) | 45 |
| Source/Isotype | Rabbit IgG |
Application Key:
- WB-Western Blotting
- IP-Immunoprecipitation
Species Cross-Reactivity Key:
- H-Human
- M-Mouse
- R-Rat
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
| Immunoprecipitation | 1:100 |
Storage
Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/mL BSA, 50% glycerol, and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the antibody.
Protocol
Specificity / Sensitivity
Phospho-β-Dystroglycan (Tyr892) (E6T9O) Rabbit mAb recognizes endogenous levels of β-dystroglycan protein only when phosphorylated at Tyr892. By western blot, this antibody detects bands of unknown origin at approximately 80 and 140 kDa.
Species Reactivity:
Human, Mouse, Rat
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Tyr892 of human β-dystroglycan protein.
Background
Dystroglycan 1 (DAG1) is a ubiquitously expressed glycoprotein that is post-translationally processed into two protein subunits. α-dystroglycan is secreted and localizes to the outer plasma membrane, where it binds to the transmembrane subunit, β-dystroglycan. The two proteins form a complex that connects the cytoskeleton with the extracellular matrix and plays essential roles in various cellular processes, including neuromuscular junction function and adhesion-driven cell signaling (1,2).
Phosphorylation of β-dystroglycan at Tyr892 regulates protein-protein interaction and subcellular localization (3-5). β-dystroglycan interacts with nuclear envelope proteins emerin and lamin B1 to regulate nuclear architecture and function (6).
Phosphorylation of β-dystroglycan at Tyr892 regulates protein-protein interaction and subcellular localization (3-5). β-dystroglycan interacts with nuclear envelope proteins emerin and lamin B1 to regulate nuclear architecture and function (6).
- Bozzi, M. et al. (2009) Matrix Biol 28, 179-87.
- Moore, C.J. and Winder, S.J. (2012) Neuromuscul Disord 22, 959-65.
- James, M. et al. (2000) J Cell Sci 113 (Pt 10), 1717-26.
- Sotgia, F. et al. (2003) Biochemistry 42, 7110-23.
- Gracida-Jiménez, V. et al. (2017) Sci Rep 7, 9906.
- Vélez-Aguilera, G. et al. (2018) Biochim Biophys Acta Mol Cell Res 1865, 406-420.
限制使用
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For Research Use Only. Not For Use In Diagnostic Procedures.
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