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Recombinant Human EDA2R/TNFRSF27/XEDAR Fc Chimera, CF

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Product Details

Summary
Reactivity HuSpecies Glossary
Applications Binding Activity
Format
Carrier-Free

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Recombinant Human EDA2R/TNFRSF27/XEDAR Fc Chimera, CF Summary

Details of Functionality
Measured by its binding ability in a functional ELISA. When Recombinant Human EDA2R/TNFRSF27/XEDAR Fc Chimera is coated at 0.1 μg/mL (100 μL/well), the concentration of Recombinant Human EDA‑A2/Ectodysplasin A2 (Catalog # 922-ED) that produces 50% of the optimal binding response is 3-15 ng/mL.
Source
Mouse myeloma cell line, NS0-derived human EDA2R/TNFRSF27/XEDAR protein
 Human EDA2R
(Met1-Glu136)
Accession # Q9HAV5
DIEGRMD Human IgG1
(Pro100-Lys330)
N-terminus C-terminus
Accession #
N-terminal Sequence
Met1
Structure / Form
Disulfide-linked homodimer
Protein/Peptide Type
Recombinant Proteins
Gene
EDA2R
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
  • Binding Activity
Theoretical MW
41.8 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
61 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 100 μg/mL in sterile PBS.

Notes

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

Alternate Names for Recombinant Human EDA2R/TNFRSF27/XEDAR Fc Chimera, CF

  • ectodysplasin A2 receptor
  • EDA2R
  • EDA-A2 receptor
  • EDAA2R
  • EDA-A2R
  • EDAA2Rtumor necrosis factor receptor superfamily member XEDAR
  • EDAR2
  • TNFRSF27
  • XEDAR
  • XEDARTNFRSF27tumor necrosis factor receptor superfamily member 27
  • X-linked ectodysplasin-A2 receptor

Background

X-linked Ectodysplasin Receptor (XEDAR), also known as EDA-2R and TNFRSF27, is an approximately 45 kDa transmembrane protein in the TNF receptor superfamily (1). Mature human XEDAR consists of a 136 amino acid (aa) extracellular domain (ECD), a 21 aa transmembrane segment, and a 140 aa cytoplasmic domain (2). Within the ECD, human XEDAR shares 87% aa sequence identity with mouse and rat XEDAR. A 55 kDa long isoform of human XEDAR carries a 21 aa insertion in the juxtamembrane cytoplasmic domain (3). A 20 kDa fragment of the ECD can be shed by metalloprotease mediated cleavage (4). XEDAR binds selectively to the EDA-A2 variant of Ectodysplasin (EDA), while the closely related receptor EDAR binds selectively to the EDA-A1 variant (2). Other than a 2 aa deletion in its TNF-like domain, EDA-A2 is identical to EDA-A1 (2). Mutations in both EDAR and EDA are associated with hypohidrotic ectodermal dysplasia (HED), a disorder of hair, tooth, and eccrine sweat gland morphogenesis (5). XEDAR itself is strongly associated with androgenetic alopecia (male hair loss) (6). XEDAR is widely expressed, notably in embryonic basal epidermal cells and maturing hair follicles (2, 7, 8). Even though it does not contain a cytoplasmic death domain, XEDAR can associate with Fas and induce EDA-A2 dependent apoptosis (7, 9). Its transcription is directly induced by p53, and XEDAR mediated cell death is p53 dependent (7, 10). XEDAR is down‑regulated in breast, colon, and lung cancers, particularly in cases with p53 mutations (7, 11). XEDAR also plays a role in
EDA‑A2 induced skeletal muscle degeneration and osteoblast differentiation (8, 12).
  1. Pfeffer, K. (2003) Cytokine Growth Factor Rev. 14:185.
  2. Yan, M. et al. (2000) Science 290:523.
  3. Sinha, S.K. et al. (2002) J. Biol. Chem. 277:44953.
  4. Tanikawa, C. et al. (2010) Mol. Cancer Res. 8:855.
  5. Mikkola, M.L. (2009) Am. J. Med. Genet. 149A:2031.
  6. Prodi, D.A. et al. (2008) J. Invest. Dermatol. 128:2268.
  7. Tanikawa, C. et al. (2009) Oncogene 28:3081.
  8. Newton, K. et al. (2004) Mol. Cell. Biol. 24:1608.
  9. Sinha, S.K. and P.M. Chaudhary (2004) J. Biol. Chem. 279:41873.
  10. Brosh, R. et al. (2010) FEBS Lett. 584:2473.
  11. Punj, V. et al. (2010) Clin. Cancer Res. 16:1140.
  12. Chang, B. et al. (2007) Cancer Gene Ther. 14:927.

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Bioinformatics

Gene Symbol EDA2R
Uniprot