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Phospho-DAG1 (Tyr892) Rabbit Polyclonal Antibody#abs140045

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Description

Catalog-specification	Delivery time	USD price
abs140045-100ug	1-2 Weeks	301.0
abs140045-50ug	1-2 Weeks	201.0

Overview
catalog	abs140045
Other names	Dystroglycan 1 (dystrophin-associated glycoprotein 1), also known as Agrin receptor or AGRNR, is a crucial protein involved in various cellular processes. It is encoded by the DAG1 gene and exists in two isoforms, alpha-DG and beta-DG, which are denoted as alpha-DG-N and Beta-dystroglycan, respectively. Alpha-DG and Beta-DG play distinct roles in cell signaling and adhesion. Alpha-DG is predominantly found in the extracellular matrix and interacts with agrin, a protein that regulates synapse formation and the development of neuromuscular junctions. On the other hand, Beta-DG is a transmembrane protein that connects the extracellular matrix to the cytoskeleton, providing structural support for cells. Dystroglycan is implicated in various biological processes, including muscle development, neuronal migration, and tissue integrity. Mutations in the DAG1 gene have been associated with several muscular dystrophies, such as Limb-girdle muscular dystrophy type 2 and congenital muscular dystrophy. In scientific research, Dystroglycan is often referred to by its alternative names, such as MDDGC7, MDDGC9, OTTHUMP00000210857, or OTTHUMP00000210858. These names may be used interchangeably to describe the same protein. In summary, Dystroglycan, or Agrin receptor, is a critical component in cellular functions and is encoded by the DAG1 gene. Its isoforms, alpha-DG and beta-DG, play distinct roles in cellular signaling and adhesion. Understanding the functions and regulation of Dystroglycan is essential for unraveling the mechanisms underlying various genetic disorders and muscular dystrophies.
Source	Rabbit
Specificity	The DAG1 (Phospho-Tyr892) Antibody is specifically designed to detect the presence of phospho-Tyr892 in the endogenous levels of DAG1. This antibody can accurately identify DAG1 only when it is phosphorylated at this particular site. Its high specificity and sensitivity make it an important tool in analyzing a variety of biological processes involving DAG1, including signal transduction pathways and cellular communication. Overall, the DAG1 (Phospho-Tyr892) Antibody is a valuable reagent for researchers studying protein phosphorylation and its role in disease and development.
Species Reactivity	Human;Mouse
Predictive reaction species	Zebrafish;Chicken;Rabbit;Xenopus;Dog;Horse;Bovine;Sheep;Pig
Antigen	DAG1
Application	：WB1：1000-3000，IHC1：50-1：200，ELISA（）1：20000-1：40000。
Immunogen	A newly developed peptide has been derived from human DAG1, specifically targeting the phosphorylated Tyr892. By utilizing the original text information, this synthesized peptide displays a high degree of similarity to the original protein.
MW	98KD
Properties
Concentration	1mg/ml
purification	The affinity-purified antibody, derived from purified rabbit serum, was obtained through sequential chromatography on affinity columns loaded with phospho- and non-phospho peptides.
Clonality	Polyclonal Antibody
Stability & Storage	Ensure that the storage temperature remains at -20 °C for a duration of one year, and it is crucial to avoid subjecting the stored items to repeated freeze/thaw cycles. It is recommended to strictly adhere to these instructions in order to maintain the quality and integrity of the stored items.
Storage buffer	Rabbit IgG in phosphate buffered saline , pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.Store at -20 °C.Stable for 12 months from date of receipt.
Target
Background	The dystroglycan complex is involved in a number of processes including laminin and basement membrane assembly, sarcolemmal stability, cell survival, peripheral nerve myelination, nodal structure, cell migration, and epithelial polarization.
Tissue specificity	Expressed in a variety of fetal and adult tissues. In epidermal tissue, located to the basement membrane. Also expressed in keratinocytes and fibroblasts.
Posttranslational modification	O- and N-glycosylated. Alpha-dystroglycan is heavily O-glycosylated comprising of up to two thirds of its mass and the carbohydrate composition differs depending on tissue type. Mucin-type O-glycosylation is important for ligand binding activity. O-mannosylation of alpha-DAG1 is found in high abundance in both brain and muscle where the most abundant glycan is Sia-alpha-2-3-Gal-beta-1-4-Glc-NAc-beta-1-2-Man. In muscle, glycosylation on Thr-317, Thr-319 and Thr-379 by a phosphorylated O-mannosyl glycan with the structure 2-(N-acetylamido)-2-deoxygalactosyl-beta-1,3-2-(N-acetylamido)-2-deoxyglucosyl-beta-1,4-6-phosphomannose is mediated by like-acetylglucosaminyltransferase (LARGE1) protein and is required for laminin binding (PubMed:20044576, PubMed:21987822, PubMed:24256719). O-mannosylation is also required for binding lymphocytic choriomeningitis virus, Old World Lassa fever virus, and clade C New World arenaviruses. The O-glycosyl hexose on Thr-367, Thr-369, Thr-372, Thr-381 and Thr-388 is probably mannose. O-glycosylated in the N-terminal region with a core 1 or possibly core 8 glycan. The beta subunit is N-glycosylated.Autolytic cleavage produces the alpha and beta subunits. In cutaneous cells, as well as in certain pathological conditions, shedding of beta-dystroglcan can occur releasing a peptide of about 30 kDa.SRC-mediated phosphorylation of the PPXY motif of the beta subunit recruits SH2 domain-containing proteins, but inhibits binding to WWW domain-containing proteins, DMD and UTRN. This phosphorylation also inhibits nuclear entry.
Celluar localization	Cytoskeleton;Cytosol;Endoplasmic reticulum;Extracellular region or secreted;Golgi apparatus;Nucleus;Plasma Membrane;
UniPort	Q14118