Reactivity | HuSpecies Glossary |
Applications | Bioactivity |
Format | Carrier-Free |
Details of Functionality | Bioassay data are not available. |
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Source | Mouse myeloma cell line, NS0-derived human Desmoglein-1 protein
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Accession # | |||||||
N-terminal Sequence | Glu50 |
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Structure / Form | Disulfide-linked homodimer |
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Protein/Peptide Type | Recombinant Proteins |
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Gene | DSG1 |
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Purity | >95%, by SDS-PAGE under reducing conditions and visualized by silver stain |
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Endotoxin Note | <1.0 EU per 1 μg of the protein by the LAL method. |
Dilutions |
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Theoretical MW | 82 kDa (monomer). 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 | 110 kDa, reducing conditions |
Storage | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Buffer | Lyophilized from a 0.2 μm filtered solution in Tris, NaCl and Citrate. |
Purity | >95%, by SDS-PAGE under reducing conditions and visualized by silver stain |
Reconstitution Instructions | Reconstitute at 100 μg/mL in sterile PBS. |
Desmoglein-1 is one of three members of the desmoglein subfamily of calcium-dependent cadherin cell adhesion molecules. Together with desmocollins, another subfamily within the cadherin superfamily, the desmoglein isoforms form the adhesive components of desmosomes, the cell-cell adhesive structures that are found in epithelial cells. Human Desmoglein-1 is a type I transmembrane glycoprotein of 1049 amino acid (aa) residues with a 23 aa signal peptide and a 26 aa propeptide. It differs from other classic cadherins by having four instead of five cadherin repeat domains in its extracellular region, and a much larger cytoplasmic region containing five desmoglein repeat domains which share homology with the cadherin repeats. Instead of having the HAV adhesion motif found in type I cadherins, Desmoglein-1 has R/YAL as the adhesion motif on its amino-terminal cadherin repeat. The cytoplasmic tail of Desmoglein-1 interacts with desmoplakins, plakoglobin and plakophilins. In turn, these proteins link the Desmoglein-1 with the intermediate filaments. Desmoglein-1 has been shown to be important in establishing cell-cell adhesion and function in the epidermis. In the autoimmune skin disease pemphigus foliaceus, autoantibodies to Desmoglein-1 can cause the loss of keratinocyte adhesion resulting in blisters.
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