• Purity

  >95%, by SDS-PAGE under reducing conditions and visualized by silver stain

• Endotoxin Level

  <0.01 EU per 1 μg of the protein by the LAL method.  

• Activity

  Measured by its binding ability in a functional ELISA. When Recombinant Mouse 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 # ) that produces 50% of the optimal binding response is 3‑15 ng/mL.

• Source

  Mouse myeloma cell line, NS0-derived

  Mouse XEDAR/EDA2R (Met1-Thr138) Accession # Q8BX35	IEGRMDP	Mouse IgG2A (Glu98-Lys330)
  N-terminus		C-terminus

• Accession #

• N-terminal Sequence    
  Analysis

  Met1

• Structure / Form

  Disulfide-linked homodimer

• Predicted Molecular Mass

  42.6 kDa (monomer)

• SDS-PAGE

  57-60 kDa, reducing conditions

Background: EDA2R/TNFRSF27/XEDAR

X‑linked Ectodysplasin Receptor (XEDAR), also known as EDA2R and TNFRSF27, is an approximately 45 kDa transmembrane protein in the TNF receptor superfamily (1). Mature mouse XEDAR consists of a 138 amino acid (aa) extracellular domain (ECD) with three tandem TNFR cysteine‑rich domains, a 21 aa transmembrane segment, and a 138 aa cytoplasmic domain. Within the ECD, mouse XEDAR shares 87% and 96% aa sequence identity with human and rat XEDAR, respectively. A 20 kDa fragment of the ECD can be shed by metalloprotease mediated cleavage (2). XEDAR binds selectively to the EDA‑A2 variant of Ectodysplasin (EDA), while the closely related receptor EDAR binds selectively to the EDA‑A1 variant (3). Other than a 2 aa deletion in its TNF‑like domain, EDA‑A2 is identical to EDA‑A1 (3). Mutations in both EDAR and EDA are associated with hypohidrotic ectodermal dysplasia (HED), a disorder of hair, tooth, and eccrine sweat gland morphogenesis (4). XEDAR itself is strongly associated with androgenetic alopecia (male hair loss) (5). XEDAR is widely expressed, notably in embryonic basal epidermal cells and maturing hair follicles (3, 6, 7). Even though it does not contain a cytoplasmic death domain, XEDAR can associate with Fas and induce EDA‑A2 dependent apoptosis (6, 8). Its transcription is directly induced by p53, and XEDAR mediated cell death is p53 dependent (6, 9). XEDAR is down‑regulated in breast, colon, and lung cancers, particularly in cases with p53 mutations (6, 10). XEDAR also plays a role in EDA‑A2 induced skeletal muscle degeneration and osteoblast differentiation (7, 11).

• References:

1. Pfeffer, K. (2003) Cytokine Growth Factor Rev. 14:185.

2. Tanikawa, C. et al. (2010) Mol. Cancer Res. 8:855.

3. Yan, M. et al. (2000) Science 290:523.

4. Mikkola, M.L. (2009) Am. J. Med. Genet. 149A:2031.

5. Prodi, D.A. et al. (2008) J. Invest. Dermatol. 128:2268.

6. Tanikawa, C. et al. (2009) Oncogene 28:3081.

7. Newton, K. et al. (2004) Mol. Cell. Biol. 24:1608.

8. Sinha, S.K. and P.M. Chaudhary (2004) J. Biol. Chem. 279:41873.

9. Brosh, R. et al. (2010) FEBS Lett. 584:2473.

10. Punj, V. et al. (2010) Clin. Cancer Res. 16:1140.

11. Chang, B. et al. (2007) Cancer Gene Ther. 14:927.

• Long Name:

  Ectodysplasin A2 Receptor

• Entrez Gene IDs:

  60401 (Human); 245527 (Mouse)

• Alternate Names:

  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