DAG1 Antibody
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Description
Structure and Function of DAG1
Dystroglycan exists as two subunits:
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α-Dystroglycan: Extracellular, binds laminin and agrin in the ECM.
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β-Dystroglycan: Transmembrane, connects α-dystroglycan to dystrophin intracellularly .
Post-translational modifications, including O-glycosylation, are essential for α-dystroglycan’s ligand-binding activity . Mutations in DAG1 disrupt these functions, leading to muscular dystrophies and dystroglycanopathies .
DAG1 Antibody Overview
DAG1 antibodies target specific epitopes or post-translational modifications of dystroglycan. Key features include:
3.1. Protein Expression Analysis
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Western Blot: Detects β-dystroglycan (~43 kDa) and α-dystroglycan (~97 kDa) . For example, Proteintech’s #66735-1-Ig identifies β-dystroglycan in muscle lysates .
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Immunohistochemistry: Localizes dystroglycan to the sarcolemma and basement membrane in muscle tissues .
3.2. Disease Diagnostics
DAG1 antibodies aid in diagnosing dystroglycanopathies:
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Reduced α-dystroglycan levels in muscle biopsies correlate with DAG1 mutations .
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Truncating DAG1 variants (e.g., c.931del) linked to hyperCKemia show diminished β-dystroglycan expression via WB .
3.3. Glycosylation Studies
Antibodies like VIA41 (DSHB) recognize glycosylated α-dystroglycan, critical for assessing congenital muscular dystrophies caused by glycosylation defects .
4.1. DAG1 Haploinsufficiency
Heterozygous truncating DAG1 variants (e.g., c.220G>A) cause isolated hyperCKemia, with histopathology revealing dystroglycan deficiency in muscle .
4.2. Novel Mutations
A homozygous DAG1 missense variant (c.2326C>T) was identified in a Chinese family with late-onset limb-girdle muscular dystrophy, confirmed by α-dystroglycan reduction on WB .
4.3. Therapeutic Insights
Restoring dystroglycan expression via gene therapy or glycosylation-enhancing drugs is under investigation for dystroglycanopathies .
Validation and Specificity
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Knockout Validation: Abcam’s ab234587 shows no signal in DAG1 knockout HAP1 cells, confirming specificity .
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Epitope Mapping: Antibodies like DAG-6F4 target α-dystroglycan’s laminin-binding domain (aa 312–653) .
Future Directions
Advancements in glycosylation-specific antibodies (e.g., VIA41 ) will enhance the precision of dystroglycanopathy subtyping. Additionally, multiplex assays combining DAG1 antibodies with other DGC markers could improve diagnostic workflows .
Product Specs
Buffer
Preservative: 0.03% Proclin 300
Constituents: 50% Glycerol, 0.01M PBS, pH 7.4
Constituents: 50% Glycerol, 0.01M PBS, pH 7.4
Form
Liquid
Lead Time
Typically, we can ship your orders within 1-3 business days of receipt. Delivery times may vary based on the chosen purchasing method or location. Please consult your local distributor for specific delivery timeframes.
Synonyms
156DAG antibody; A3a antibody; AGRNR antibody; Alpha dystroglycan antibody; Alpha-DG antibody; Beta-DG antibody; Beta-dystroglycan antibody; DAG antibody; Dag1 antibody; DAG1_HUMAN antibody; Dystroglycan 1 (dystrophin associated glycoprotein 1) antibody; Dystroglycan antibody; Dystrophin associated glycoprotein 1 antibody; Dystrophin-associated glycoprotein 1 antibody; OTTHUMP00000210857 antibody; OTTHUMP00000210858 antibody
Target Names
Uniprot No.
Target Background
Function
The dystroglycan complex plays a vital role in various cellular processes, including:
- Laminin and basement membrane assembly
- Sarcolemmal stability
- Cell survival
- Peripheral nerve myelination
- Nodal structure
- Cell migration
- Epithelial polarization.
Dystroglycan is an extracellular peripheral glycoprotein that acts as a receptor for extracellular matrix proteins containing laminin-G domains. It serves as a receptor for laminin-2 (LAMA2) and agrin in peripheral nerve Schwann cells. Additionally, it functions as a receptor for laminin LAMA5.
Dystroglycan is a transmembrane protein with critical roles in connecting the extracellular matrix to the cytoskeleton. It acts as a cell adhesion receptor in both muscle and non-muscle tissues. It interacts with both DMD and UTRN, and through these interactions, scaffolds axin to the cytoskeleton. Furthermore, dystroglycan is involved in cell adhesion-mediated signaling and plays a role in cell polarity.
In the context of microbial infections, dystroglycan acts as a receptor for Lassa virus and lymphocytic choriomeningitis virus glycoprotein, as well as class C new-world arenaviruses. It also serves as a Schwann cell receptor for Mycobacterium leprae, the causative organism of leprosy, but only in the presence of the G-domain of LAMA2.
- Laminin and basement membrane assembly
- Sarcolemmal stability
- Cell survival
- Peripheral nerve myelination
- Nodal structure
- Cell migration
- Epithelial polarization.
Dystroglycan is an extracellular peripheral glycoprotein that acts as a receptor for extracellular matrix proteins containing laminin-G domains. It serves as a receptor for laminin-2 (LAMA2) and agrin in peripheral nerve Schwann cells. Additionally, it functions as a receptor for laminin LAMA5.
Dystroglycan is a transmembrane protein with critical roles in connecting the extracellular matrix to the cytoskeleton. It acts as a cell adhesion receptor in both muscle and non-muscle tissues. It interacts with both DMD and UTRN, and through these interactions, scaffolds axin to the cytoskeleton. Furthermore, dystroglycan is involved in cell adhesion-mediated signaling and plays a role in cell polarity.
In the context of microbial infections, dystroglycan acts as a receptor for Lassa virus and lymphocytic choriomeningitis virus glycoprotein, as well as class C new-world arenaviruses. It also serves as a Schwann cell receptor for Mycobacterium leprae, the causative organism of leprosy, but only in the presence of the G-domain of LAMA2.
Gene References Into Functions
- A study identified beta-dystroglycan as a substrate of WWP1 and found that the muscular dystrophy-causing mutation of WWP1 renders the enzyme hyperactive by relieving autoinhibition. PMID: 29635000
- ISPD and FKTN are essential for the incorporation of ribitol into alpha-dystroglycan. PMID: 27194101
- N-terminal alpha Dystroglycan ELISA signals were significantly reduced in Duchenne muscular dystrophy serum relative to serum from otherwise normal controls. PMID: 27854211
- TMEM5 is a UDP-xylosyl transferase that elaborates the O-mannose glycan structure on alpha-dystroglycan. The authors demonstrate in a zebrafish model as well as in a human patient that defects in TMEM5 result in muscular dystrophy in combination with abnormal brain development. PMID: 27130732
- Research indicates that the balance and integrity between the dystroglycan alpha and beta subunits are indispensable for cell differentiation and proliferation in acute leukemia cells. PMID: 28591567
- The interaction of DG with laminin and dynamin is involved in the regulation of AQP4 internalization. PMID: 27788222
- The Muscular Dystrophy Gene TMEM5 Encodes a Ribitol beta1,4-Xylosyltransferase Required for the Functional Glycosylation of Dystroglycan. PMID: 27733679
- Data show that CD93 antigen is phosphorylated on tyrosine 628 and 644 following cell adhesion on laminin through dystroglycan. PMID: 26848865
- Removal of the alpha-DG-N terminal domain serves as an important posttranslational control of endometrial receptivity. Additionally, uterine fluid alpha-DG-N may serve as a potential biomarker for receptivity in women. PMID: 26077903
- Phosphorylation within the cysteine-rich region of dystrophin enhances its association with beta-dystroglycan. This finding identifies a potential novel therapeutic target for skeletal muscle wasting. PMID: 25082828
- Novel mutations in DAG1 are associated with asymptomatic hyperCKemia with hypoglycosylation of alpha-dystroglycan. PMID: 25503980
- Reduced alpha-dystroglycan expression is correlated with glioma. PMID: 25139094
- Depletion of DAG resulted in altered morphology and reduced properties of differentiated HL-60 cells, including chemotaxis, respiratory burst, phagocytic activities, and markers of differentiation, implicating DAG as a protein involved in differentiation. PMID: 24792180
- A report details a homozygous novel DAG1 missense mutation c.2006G>T in the beta-subunit of dystroglycan in two Libyan siblings presenting with a novel muscle-eye-brain disease-like phenotype with multicystic leucodystrophy. PMID: 24052401
- Research provides evidence for at least three separate pools of dystroglycan complexes within myofibers that differ in composition and are differentially affected by loss of dystrophin. PMID: 23951345
- Findings suggest that proteolysis, tyrosine phosphorylation, and translocation of dystroglycan to the nucleus, resulting in altered gene transcription, could be significant mechanisms in the progression of prostate cancer. PMID: 24077328
- The T192M point-mutation in dystroglycan leads to weaker interactions with laminin-1, resulting in hypoglycosylation and ultimately contributing to limb girdle disease. PMID: 24361964
- GTDC2 generates CTD110.6 antibody-reactive N-acetylglucosamine epitopes on the O-mannosylated alpha-dystroglycan. PMID: 24041696
- Dystroglycan-mediated cortical microtubule anchoring is crucial, and its disruption initiates gastrulation EMT. PMID: 23940118
- Loss of alpha-dystroglycan and increased CD133 expression are frequent occurrences in human colon cancer. Assessment of CD133 expression could aid in identifying high-risk colon cancer patients. PMID: 22964035
- Loss of LARGE2 disrupts functional glycosylation of alpha-dystroglycan in prostate cancer. PMID: 23223448
- The loss of dystroglycan during tumorigenesis leads to an increased capacity for tumor growth. PMID: 22996647
- Research highlights a novel role for HNK-1ST as a tumor suppressor controlling the functional glycans on alpha-DG. This emphasizes the importance of sulfate transfer in the glycosylation of alpha-DG. PMID: 22801424
- The study examines the dynamics of expression patterns of dystroglycan in human glioblastoma. PMID: 22307776
- The virus-induced perturbation of alpha6beta1 integrin signaling critically depended on high-affinity Lassa virus binding to dystroglycan and dystroglycan's cytoplasmic domain. PMID: 22405130
- Data suggest that throughout pregnancy, changes occur in the expression and distribution of DAG1 and dystroglycan subunits in placental tissues undergoing placentation. PMID: 22138543
- Research describes a mechanism by which Large competes with galactosyltransferase to target GlcNAc terminals to induce the functional glycans on alpha-DG. PMID: 21347376
- Reduced expression and altered localization of dystroglycan are common in pancreatic cancer, potentially contributing to the aggressive behavior of this disease. PMID: 20338590
- The ligand-binding activity of alpha-dystroglycan is primarily conferred by LARGE modification at Thr-317 and -319, within the highly conserved first 18 amino acids of the mucin-like domain. PMID: 21987822
- These observations suggest that secreted alpha-DG-N may be transported via CSF and have yet unidentified effects on the nervous system. PMID: 21741360
- LARGE plays a role in inducing alpha-dystroglycan hyperglycosylation in skeletal and cardiac muscle. PMID: 21203384
- Ameloblastoma cells proliferate and differentiate by capturing perlecan differentially with alpha-dystroglycan and integrin beta1, respectively. PMID: 21255062
- Data indicate that loss of nuclear p27(kip1) is a frequent event in human RCCs and is a strong predictor of poor outcome. In combination with low DG expression, this could help identify high-risk patients with clear cell RCC. PMID: 20626751
- Beta-Dystroglycan interaction with caveolin-1 in smooth muscle is required for receptor-mediated Ca2+ release. PMID: 20736308
- Twenty-five glycopeptides were characterized from human alpha-dystroglycan, providing insights into the complex in vivo O-glycosylation of alpha-dystroglycan. PMID: 20507882
- This review examines the biological role of dystroglycan in Schwann cell function, particularly myelination, and its implications in diseases. PMID: 20625412
- Beta-dystroglycan follows a conventional Importin alpha/beta-dependent nuclear import pathway. PMID: 20512930
- Loss of alpha-dystroglycan expression is a frequent event in human oral squamous cell carcinoma. PMID: 20350218
- Research analyzed the main cleavage site involved in enzymatic processing of beta-dystroglycan recombinant ectodomain by MMP-9. PMID: 19946898
- A study identified phosphorylated O-mannosyl glycan on the mucin-like domain of alpha-DG, which was required for laminin binding. Patients with muscular dystrophy exhibit defects in a postphosphoryl modification of this phosphorylated O-linked mannose. PMID: 20044576
- Post-translational disruption of dystroglycan-ligand interactions is observed in congenital muscular dystrophies. PMID: 12140558
- Glomeruli contain substantial amounts of a specifically composed complex. This complex may undergo changes in human glomerular disease, and flattening of foot processes is directly associated with dissociation of laminin-dystroglycan complexes. PMID: 12386278
- hAG-2 and hAG-3, human homologues of genes involved in differentiation, are associated with estrogen receptor-positive breast tumors and interact with metastasis gene C4.4a and dystroglycan. PMID: 12592373
- Expression of dystroglycan is frequently reduced in human breast and colon cancers and is associated with tumor progression. PMID: 12598319
- In human coxsackievirus B myocarditis, focal disruption of the DAG can primarily occur and may contribute to the pathogenesis of human enterovirus-induced dilated cardiomyopathy. PMID: 12920582
- Mutation of certain residues in dystroglycan prevents both ezrin binding and the induction of actin-rich surface protrusions. PMID: 15175275
- Cells deficient in components of the O-mannosylation pathway exhibited markedly reduced lymphocytic choriomeningitis virus infectivity. PMID: 16254364
- Alpha-DG glycosylation may differ between neurons and glial cells in congenital muscular dystrophy brains. PMID: 16466646
- Dystroglycan may be involved in the progression of primary brain tumors. PMID: 16575202
- Fukutin appears to bind to both the hypoglycosylated and fully glycosylated forms of alpha-dystroglycan and seems to bind to the core area rather than the sugar chain of alpha-dystroglycan. PMID: 17005282
Database Links
Involvement In Disease
Muscular dystrophy-dystroglycanopathy limb-girdle C9 (MDDGC9); Muscular dystrophy-dystroglycanopathy congenital with brain and eye anomalies A9 (MDDGA9)
Subcellular Location
[Alpha-dystroglycan]: Secreted, extracellular space.; [Beta-dystroglycan]: Cell membrane; Single-pass type I membrane protein. Cytoplasm, cytoskeleton. Nucleus, nucleoplasm. Cell membrane, sarcolemma. Cell junction, synapse, postsynaptic cell membrane.
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.
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