Recombinant Human Dystroglycan (DAG1) Protein (His&Myc)

Name: Recombinant Human Dystroglycan (DAG1) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-07848P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Dystroglycan (DAG1) Protein (His&Myc) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	Q14118
Target Symbol	DAG1
Synonyms	Dystrophin-associated glycoprotein 1
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-10His&C-Myc
Target Protein Sequence	HWPSEPSEAVRDWENQLEASMHSVLSDLHEAVPTVVGIPDGTAVVGRSFRVTIPTDLIASSGDIIKVSAAGKEALPSWLHWDSQSHTLEGLPLDTDKGVHYISVSATRLGANGSHIPQTSSVFSIEVYPEDHSELQSVRTASPDPGEVVSSACAADEPVTVLTVILDADLTKMTPKQRIDLLHRMRSFSEVELHNMKLVPVVNNRLFDMSAFMAGPGNAKKVVENGALLSWKLGCSLNQNSVPDIHGVEAPAREGAMSAQLGYPVVGWHIANKKPPLPKRVRRQIHATPTPVTAIGPPTTAIQEPPSRIVPTPTSPAIAPPTETMAPPVRDPVPGKPTVTIRTRGAIIQTPTLGPIQPTRVSEAGTTVPGQIRPTMTIPGYVEPTAVATPPTTTTKKPRVSTPKPATPSTDSTTTTTRRPTKKPRTPRPVPRVTTKVSITRLETASPPTRIRTTTSGVPRGGEPNQRPELKNHIDRVDAWVGTYFEVKIPSDTFYDHEDTTTDKLKLTLKLREQQLVGEKSWVQFNSNSQLMYGLPDSSHVGKHEYFMHATDKGGLSAVDAFEIHVHRRPQGDRAPARFKAKFVGDPALVLNDIHKKIALVKKLAFAFGDRNCSTITLQNITRG
Expression Range	30-653aa
Protein Length	Partial
Mol. Weight	75.2 kDa
Research Area	Neuroscience
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target 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.; Extracellular peripheral glycoprotein that acts as a receptor for extracellular matrix proteins containing laminin-G domains. Receptor for laminin-2 (LAMA2) and agrin in peripheral nerve Schwann cells. Also acts as a receptor for laminin LAMA5.; 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.; (Microbial infection) Acts as a receptor for lassa virus and lymphocytic choriomeningitis virus glycoprotein and class C new-world arenaviruses. Acts as a Schwann cell receptor for Mycobacterium leprae, the causative organism of leprosy, but only in the presence of the G-domain of LAMA2.
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.
Database References	HGNC: 2666 OMIM: 128239 KEGG: hsa:1605 STRING: 9606.ENSP00000312435 UniGene: 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 Our results strongly suggest that the balance and integrity between the dystroglycan alpha and beta subunits are indispensable and responsible for the cell differentiation and proliferation in acute leukemia cells. PMID: 28591567 interation 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 proved to be phosphorylated on tyrosine 628 and 644 following cell adhesion on laminin through dystroglycan. PMID: 26848865 alpha-DG-N removal as an important posttranslational control of endometrial receptivity and uterine fluid alpha-DG-N as a potential biomarker for receptivity in women. PMID: 26077903 Phosphorylation within the cysteine-rich region of dystrophin enhances its association with beta-dystroglycan and 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 Reduction of 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 of a homozygous novel DAG1 missense mutation c.2006G>T in the beta-subunit of dystroglycan in two Libyan siblings with with a novel muscle-eye-brain disease-like phenotype with multicystic leucodystrophy. PMID: 24052401 The study 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 These data suggest that proteolysis, tyrosine phosphorylation and translocation of dystroglycan to the nucleus resulting in altered gene transcription could be important mechanisms in the progression of prostate cancer. PMID: 24077328 T192M point-mutation in dystroglycan leads to a weaker interactions with laminin-1, which leads to hypoglycosylation and which finally leads to the limb girdle disease. PMID: 24361964 GTDC2 generates CTD110.6 antibody-reactive N-acetylglucosamine epitopes on the O-mannosylated alpha-dystroglycan. PMID: 24041696 the Dystroglycan-mediated cortical microtubule anchoring, the disruption of which initiates gastrulation EMT. PMID: 23940118 Loss of alpha-dystroglycan and increased CD133 expression are frequent events in human colon cancer and evaluation of CD133 expression could help to identify 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 ability for tumor growth. PMID: 22996647 novel role for HNK-1ST as a tumor suppressor controlling the functional glycans on alpha-DG and the importance of sulfate transfer in the glycosylation of alpha-DG. PMID: 22801424 Dynamics of expression patterns of dystroglycan in human glioblastoma PMID: 22307776 The virus-induced perturbation of alpha6beta1 integrin signalling 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 expression and distribution of DAG1 and dystroglycan subunits in placental tissues undergoing placentation. PMID: 22138543 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 is common in pancreatic cancer, potentially contributing to the aggressive behavior of this disease. PMID: 20338590 the ligand-binding activity of alpha-dystroglycan is conferred primarily 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 has a role in inducing alpha-dystroglycan hyperglycosylation in skeletal and cardiac muscle PMID: 21203384 Ameloblastoma cells proliferate and are differentiated by capturing perlecan differentially with alpha-dystroglycan and integrin beta1, respectively PMID: 21255062 Data show that loss of nuclear p27(kip1) is a frequent event in human RCCs and is a powerful predictor of poor outcome which, in combination with low DG expression, could help to 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, which provide insight to the complex in vivo O-glycosylation of alpha-dystroglycan. PMID: 20507882 Biological role of dystroglycan in Schwann cell function, especially myelination, and its implications in diseases is reviewed. 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 analysis of the main cleavage site involved in enzymatic processing of beta-dystroglycan recombinant ectodomain by MMP-9 PMID: 19946898 study identified phosphorylated O-mannosyl glycan on mucin-like domain of alpha-DG, which was required for laminin binding; patients with muscular dystrophy have defects in a postphosphoryl modification of this phosphorylated O-linked mannose PMID: 20044576 Post-translational disruption of dystroglycan-ligand interactions in congenital muscular dystrophies. PMID: 12140558 Glomeruli possess large 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 oestrogen receptor-positive breast tumours and interact with metastasis gene C4.4a and dystroglycan. PMID: 12592373 Expression is frequently reduced in human breast and colon cancers and is associated with tumor progression. PMID: 12598319 in human coxsackievirus B myocarditis a focal disruption of the DAG can principally occur and may contribute to the pathogenesis of human enterovirus-induced dilated cardiomyopathy PMID: 12920582 mutation of certain residues prevents both ezrin binding and the induction of actin-rich surface protrusions PMID: 15175275 Cells that are defective in components of the O-mannosylation pathway showed strikingly reduced lymphocytic choriomeningitis virus infectbility. PMID: 16254364 alpha-DG glycosylation may differ between neurons and glial cells in congenital musculaar dystrophy brains. PMID: 16466646 DG may be involved in the progression of primary brain tumors PMID: 16575202 Fukutin seems to bind to both the hypoglycosylated and fully glycosylated form of alpha-dystroglycan, and seems bind to the core area rather than the sugar chain of alpha-dystroglycan PMID: 17005282

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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