Reactivity | HuSpecies Glossary |
Applications | Binding Activity |
Format | Carrier-Free |
Details of Functionality | Measured by the ability of the immobilized rhEDAR/Fc Chimera to bind biotinylated rhEDA-A1/His in a functional ELISA. Optimal dilutions should be determined by each laboratory for each application. |
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Source | Mouse myeloma cell line, NS0-derived human EDAR protein
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Accession # | |||||||
N-terminal Sequence | Glu27 |
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Structure / Form | Disulfide-linked homodimer |
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Protein/Peptide Type | Recombinant Proteins |
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Gene | EDAR |
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Purity | >90%, by SDS-PAGE under reducing conditions and visualized by silver stain |
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Endotoxin Note | <0.10 EU per 1 μg of the protein by the LAL method. |
Dilutions |
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Theoretical MW | 44.3 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 | 55-60 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 PBS. |
Purity | >90%, by SDS-PAGE under reducing conditions and visualized by silver stain |
Reconstitution Instructions | Reconstitute at 100 μg/mL in sterile PBS. |
EDAR is a type I transmembrane protein which is a member of the TNF Receptor Superfamily (TNFRSF). The extracellular domain contains 14 cysteine residues, six of which approximate the TNFRSF cysteine-rich region; the cytoplasmic domain contains a region with homology to the death domains found in other TNFRSF members. Human EDAR is a 488 amino acid (aa) protein with a predicted 26 aa signal, a 163 aa extracellular domain, a 22 aa transmembrane domain, and a 277 aa cytoplasmic domain. The human and mouse EDAR homologs share 91% identity. Within the TNFRSF, EDAR shares the highest homologies with XEDAR and TNFRSF19/TROY. EDA-A1 is the EDAR ligand. EDA and EDAR have been associated with hypohidrotic ectodermal dysplasia (HED). HED is characterized by abnormalities in hair, teeth and eccrine sweat gland morphogenesis. HED was initially found to associate with two gene loci, tabby and downless. Tabby was later identified as the gene for EDA and downless as the autosomal EDAR gene. EDA has two splice variants, EDA-A1 and EDA-A2, which differ by only two amino acids. Despite this minor difference, the EDA isoforms display strong receptor specificity. EDA-A1 only binds EDAR, whereas EDA-A2 binds to XEDAR, an X-linked TNFRSF member with high homology to EDAR. Mutations in EDA, EDAR and XEDAR have been associated with HED.
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