Recombinant Human DAG1 protein (ab175460)
Key features and details
- Expression system: Escherichia coli
- Purity: > 90% Densitometry
- Endotoxin level: < 1.000 Eu/µg
- Tags: His tag N-Terminus
- Suitable for: WB, MS, ELISA, SDS-PAGE
Description
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Product name
Recombinant Human DAG1 protein -
Purity
> 90 % Densitometry.
ab175460 is purifed using Ni-NTA chromatography and filtered (0.4 µm). -
Endotoxin level
< 1.000 Eu/µg -
Expression system
Escherichia coli -
Accession
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Protein length
Protein fragment -
Animal free
No -
Nature
Recombinant -
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Species
Human -
Sequence
MKHHHHHHASHWPSEPSEAVRDWENQLEASMHSVLSDLHEAVPTVVGIPD GTAVVGRSFRVTIPTDLIASSGDIIKVSAAGKEALPSWLHWDSQSHTLEG LPLDTDKGVHYISVSATRLGANGSHIPQTSSVFSIEVYPEDHSELQSVRT ASPDPGEVVSSACAADEPVTVLTVILDADLTKMTPKQRIDLLHRMRSFSE VELHNMKLVPVVNNRLFDMSAFMAGPGNAKKVVENGALLSWKLGCSLNQN SVPDIHGVEAPAREGAMSAQLGYPVVGWHIANKKPPLPKRVRR -
Predicted molecular weight
32 kDa including tags -
Amino acids
30 to 312 -
Tags
His tag N-Terminus
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Associated products
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Related Products
Specifications
Our Abpromise guarantee covers the use of ab175460 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
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Applications
Western blot
Mass Spectrometry
ELISA
SDS-PAGE
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Mass spectrometry
LC-MS/MS -
Form
Lyophilized -
Concentration information loading...
Preparation and Storage
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Stability and Storage
Shipped at 4°C. Store at -80°C. Avoid freeze / thaw cycle.
Constituents: 0.44% Sodium chloride, 99% Phosphate Buffer
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ReconstitutionAdd 200ul of deionized water to prepare a working stock solution of 0.5 mg/mL and let the lyophilized pellet dissolve completely.
General Info
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Alternative names
- 156DAG
- A3a
- Agrin receptor
see all -
Function
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.
Alpha-dystroglycan is an extracellular peripheral glycoprotein that acts as a receptor for both extracellular matrix proteins containing laminin-G domains, and for certain adenoviruses. Receptor for laminin-2 (LAMA2) and agrin in peripheral nerve Schwann cells. Also acts as a receptor for M.leprae in peripheral nerve Schwann cells but only in the presence of the G-domain of LAMA2, and for lymphocytic choriomeningitis virus, Old World Lassa fever virus, and clade C New World arenaviruses.
Beta-dystroglycan is a transmembrane protein that plays important roles in connecting the extracellular matrix to the cytoskeleton. Acts as a cell adhesion receptor in both muscle and non-muscle tissues. Receptor for both DMD and UTRN and, through these interactions, scaffolds axin to the cytoskeleton. Also functions in cell adhesion-mediated signaling and implicated in cell polarity. -
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. -
Involvement in disease
Defects in DAG1 are the cause of muscular dystrophy-dystroglycanopathy limb-girdle type C7 (MDDGC7) [MIM:613818]. An autosomal recessive muscular dystrophy showing onset in early childhood, and associated with mental retardation without structural brain anomalies. Note=MDDGC7 is caused by DAG1 mutations that interfere with normal post-translational processing, resulting in defective DAG1 glycosylation and impaired interactions with extracellular-matrix components. Other muscular dystrophy-dystroglycanopathies are caused by defects in enzymes involved in protein O-glycosylation. -
Sequence similarities
Contains 1 peptidase S72 domain. -
Post-translational
modificationsO- 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-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 (LARGE) protein and is required for laminin binding. 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. -
Cellular localization
Secreted > extracellular space and Cell membrane. Cytoplasm > cytoskeleton. Nucleus > nucleoplasm. The monomeric form translocates to the nucleus via the action of importins and depends on RAN. Nuclear transport is inhibited by Tyr-892 phosphorylation. In skeletal muscle, this phosphorylated form locates to a vesicular internal membrane compartment. In peripheral nerves, localizes to the Schwann cell membrane. Colocalizes with ERM proteins in Schwann-cell microvilli. - Information by UniProt
Images
Protocols
To our knowledge, customised protocols are not required for this product. Please try the standard protocols listed below and let us know how you get on.
Datasheets and documents
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Datasheet download
References (0)
ab175460 has not yet been referenced specifically in any publications.