Recombinant Human Dystroglycan Protein, CF

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Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

Order Details

Recombinant Human Dystroglycan Protein, CF Summary

Details of Functionality
Measured by the ability of the immobilized protein to enhance the adhesion of H4 human neuroglioma cells.

The ED50 for this effect is 1.5-6.0 μg/mL.

Optimal dilutions should be determined by each laboratory for each application.

Source
Mouse myeloma cell line, NS0-derived human Dystroglycan protein
Met1-Val749, with a C-terminal 6-His tag
Accession #
N-terminal Sequence
Gln28 predicted ( alpha subunit): No results obtained, sequencing might be blocked & Ser654 ( beta subunit)
Structure / Form
Noncovalently-linked heterodimer
Protein/Peptide Type
Recombinant Proteins
Gene
DAG1
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Dilutions
  • Bioactivity
Theoretical MW
67.8 kDa ( alpha subunit) & 11.3 kDa ( beta subunit).
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
SDS-PAGE
65-90 kDa & 20 kDa, reducing conditions

Packaging, Storage & Formulations

Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS.
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 500 μg/mL in PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human Dystroglycan Protein, CF

  • A3a
  • AGRNR
  • DAG1
  • Dag-1
  • DAG156DAG
  • dystroglycan 1 (dystrophin-associated glycoprotein 1)
  • Dystroglycan
  • Dystrophin-associated glycoprotein 1

Background

Dystroglycan, also called DAG‑1 (dystrophin‑associated glycoprotein 1) or DG, is a heterodimeric adhesion molecule that links the extracellular matrix (ECM) to the cell cytoskeleton (1‑4). Human preproDAG‑1 is an 895 amino acid (aa) type I transmembrane protein that contains a 27 aa signal sequence and an 868 aa proform. Autocatalysis of the proform produces two fragments that remain noncovalently‑linked. The first fragment (or alpha ‑chain) is 626 aa in length (aa 28‑653) and contains a mucin‑like region, while the second fragment (or beta ‑chain) is a 42‑44 kDa, 242 aa N‑glycosylated protein with an extracellular (aa 654‑749), transmembrane, and cytoplasmic domain (5). Over aa 28‑749, human DAG‑1 shares 93% aa sequence identity with mouse DAG‑1. It is widely expressed but differentially O‑glycosylated on skeletal muscle and epithelia (which contain a 160 kDa alpha ‑chain) as compared to cardiac muscle, smooth muscle, fibroblasts, keratinocytes, lymphocytes, and hematopoietic stem cells (which contain a 100 ‑ 140 kDa alpha ‑chain) (1‑3, 6‑9). DAG‑1 binding of ECM molecules is influenced by its alpha ‑chain O‑glycosylation (2, 6‑10). In addition to skeletal muscle and neuromuscular junctions in which DAG‑1 binds several ECM molecules, DAG‑1 is important for neuronal migration (through neurexin interactions), keratinocyte attachment to the ECM (through laminin), and adhesion at the immunological synapse and in the hematopoietic stem cell niche (through agrin) (3, 6‑11). In muscle, the beta ‑chain cytoplasmic domain connects with the cytoskeleton via formation of the dystrophin‑glycoprotein complex with isoforms of dystrophin, sarcoglycan, syntrophin, and sarcospan (3). This complex is critical for skeletal muscle viability and regeneration (3, 4, 10, 11). MMP9 cleavage of the 44 kDa beta ‑chain creates a 30 kDa transmembrane form that causes dissociation of the heterodimer and a down‑regulation of ECM interactions (6, 12). Dystroglycanopathies, a group of congenital muscular dystrophies affecting the brain, eye and skeletal muscle, are caused by either abnormalities in glycosyltransferases, or their accessory proteins, or rare DAG‑1 polymorphisms. All result in DAG‑1 hypoglycosylation, especially of O‑mannosyl forms, and affect DAG‑1 binding to ECM proteins (2, 3, 10, 13, 14).

  1. Ibraghimov-Bedkrovnaya, O. et al. (1993) Hum. Mol. Genet. 2:1651.
  2. Godfrey, C. et al. (2011) Curr. Opin. Genet. Dev. 21:278.
  3. Barresi, R. and Campbell, K.P. (2006) J. Cell Sci. 119:199.
  4. Durbeej, M. and K.P. Campbell (1999) J. Biol. Chem. 274:26609.
  5. Akhavan, A. et al. (2008) FASEB J. 22:612.
  6. Herzog, C. et al. (2004) J. Invest. Dermatol. 122:1372.
  7. Leonoudakis, D. et al. (2010) J. Cell Sci. 123:3683.
  8. Zhang, J. et al. (2006) FASEB J. 20:50.
  9. Mazzon, C. et al. (2011) Blood 118:2733.
  10. Michele, D.E. et al. (2002) Nature 418:417.
  11. Cohn, R.D. et al. (2002) Cell 110:639.
  12. Bozzi, M. et al. (2009) IUBMB Life 61:1143.
  13. Yoshida-Moriguchi, T. et al. (2010) Science 327:88.
  14. Hara, Y. et al. (2011) N. Eng. J. Med. 364:939.

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Bioinformatics

Gene Symbol DAG1
Uniprot