Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Level
<0.10 EU per 1 μg of the protein by the LAL method.
Activity
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 # ) that produces 50% of the optimal binding response is 3-15 ng/mL.
Source
Mouse myeloma cell line, NS0-derived
Human EDA2R
(Met1-Glu136)
Accession # Q9HAV5DIEGRMD Human IgG1
(Pro100-Lys330)N-terminus C-terminus Accession #
N-terminal Sequence
AnalysisMet1
Structure / Form
Disulfide-linked homodimer
Predicted Molecular Mass
41.8 kDa (monomer)
SDS-PAGE
61 kDa, reducing conditions
1093-XD |
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Formulation Lyophilized from a 0.2 μm filtered solution in PBS. | ||
Reconstitution Reconstitute at 100 μg/mL in sterile PBS. | ||
Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. | ||
Stability & Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Background: EDA2R/TNFRSF27/XEDAR
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).
References:
Pfeffer, K. (2003) Cytokine Growth Factor Rev. 14:185.
Yan, M. et al. (2000) Science 290:523.
Sinha, S.K. et al. (2002) J. Biol. Chem. 277:44953.
Tanikawa, C. et al. (2010) Mol. Cancer Res. 8:855.
Mikkola, M.L. (2009) Am. J. Med. Genet. 149A:2031.
Prodi, D.A. et al. (2008) J. Invest. Dermatol. 128:2268.
Tanikawa, C. et al. (2009) Oncogene 28:3081.
Newton, K. et al. (2004) Mol. Cell. Biol. 24:1608.
Sinha, S.K. and P.M. Chaudhary (2004) J. Biol. Chem. 279:41873.
Brosh, R. et al. (2010) FEBS Lett. 584:2473.
Punj, V. et al. (2010) Clin. Cancer Res. 16:1140.
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
