Recombinant Human Dystroglycan Fc Chimera Protein, CF


Immobilized Recombinant Human Dystroglycan Fc Chimera (Catalog # 10223-DG) enhances the adhesion of H4 human neuroglioma cells. The ED50 for this effect is 1.5‑9 μg/mL.

Product Details

Reactivity HuSpecies Glossary
Applications Bioactivity

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Recombinant Human Dystroglycan Fc Chimera 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 1.5-9 μg/mL.
Human embryonic kidney cell, HEK293-derived human Dystroglycan protein
Human Dystroglycan
Accession # Q14118
N-terminus C-terminus
Accession #
N-terminal Sequence

Gln28 inferred from AA sequence (alpha subunit) & Ser654 (beta subunit)

Structure / Form
Disulfide-linked homodimer
Protein/Peptide Type
Recombinant Proteins
>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.


  • Bioactivity
Theoretical MW
68 kDa (alpha subunit) & 37 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.
70-100 kDa and 120-135 kDa (alpha subunit) & 45-55 kDa (beta subunit)

Packaging, Storage & Formulations

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


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

Alternate Names for Recombinant Human Dystroglycan Fc Chimera Protein, CF

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


Dystroglycan, also called DAG1 (dystrophin‑associated glycoprotein 1) or DG, is a heterodimeric adhesion molecule that links the extracellular matrix (ECM) to the cell cytoskeleton (1‑4). Human DAG1 is a type I transmembrane protein that is initially expressed as a large prepro protein. Autocatalysis of the proform produces two fragments (an alpha and beta chain) that remain noncovalently‑linked. The alpha chain (aa 28-653) contains a mucin‑like region, while the beta chain (aa) consists of an extracellular domain, a transmembrane region, and a cytoplasmic domain (5). Over aa 28-749, human DAG1 shares 93% aa sequence identity with mouse DAG1. DAG1 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). DAG1 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 DAG1 binds several ECM molecules, DAG1 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 DAG1 polymorphisms. All result in DAG1 hypoglycosylation, especially of O‑mannosyl forms, and affect DAG1 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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