Recombinant Human EDA-A1/Ectodysplasin A1 Protein

• Reactivity: Hu
• Applications: Binding Activity

Recombinant Human EDA-A1/Ectodysplasin A1 Protein Summary

• Details of Functionality: Measured by its ability to compete with biotinylated human EDA-A1 for binding to immobilized rhEDA R/Fc Chimera.
• Source: Mouse myeloma cell line, NS0-derived human EDA-A1/Ectodysplasin A1 protein
  Ser160-Ser391 & Lys178-Ser391
• Accession #: Q92838
• N-terminal Sequence: Ser160 & Lys178
• Structure / Form: Homotrimer
• Protein/Peptide Type: Recombinant Proteins
• Gene: EDA
• Purity: >90%, by SDS-PAGE under reducing conditions and visualized by silver stain
• Endotoxin Note: <0.01 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

• Theoretical MW: 24.1 kDa & 22.2 kDa (monomers).
  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: 30-40 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 with BSA as a carrier protein.
• Purity: >90%, by SDS-PAGE under reducing conditions and visualized by silver stain
• Reconstitution Instructions: Reconstitute at 10 μg/mL in sterile PBS containing at least 0.1% human or bovine serum albumin.

Notes

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

Alternate Names for Recombinant Human EDA-A1/Ectodysplasin A1 Protein

• EDAA1
• EDA-A1

Background

Ectodysplasin is a 45 kDa type II transmembrane TNF superfamily protein that is associated with X-linked hypohidrotic ectodermal dysplasia (HED), a disorder of hair, tooth, and sweat gland development (1 - 4). The human EDA-A1 cDNA encodes a 41 amino acid (aa) cytoplasmic region, a 21 aa transmembrane segment, and a 329 aa extracellular region that contains a terminal TNF homology domain, a collagenous domain, and a stalk region (3, 5, 6). Within the collagenous and TNF homology domains, human EDA-A1 shares greater than 97% aa sequence identity with bovine, canine, mouse, and rat EDA-A1. Multiple alternately spliced EDA variants have been described (4, 7). The dominant variant, EDA-A2, has a deletion of two amino acids that changes the receptor binding selectivity from EDAR to XEDAR (4, 7, 8). The collagenous domain of EDA-A1 mediates non-covalent homotrimer formation (5, 6). Shedding of the collagenous and TNF homology domains of EDA-A1 is accomplished by a furin-like protease. The released fragment maintains its trimeric state and ability to bind EDAR (9, 10). Some EDA-A1 polymorphisms found in HED patients alter the protease recognition site and prevent shedding (9). EDA-A1 is expressed in developing hair follicles, epidermis, teeth, sweat glands, salivary glands, and forebrain (6, 8, 11 - 13). It regulates ectodermal appendage formation and is critical to the patterning and morphogenesis of hair follicles, partially through the induction of Lymphotoxin beta (5, 12, 14). Receptor and ligand expression are regulated by factors involved in many aspects of tissue morphogenesis. EDA-A1 expression is induced by Wnt6 (12, 13), while the expression of EDAR is induced by Activin beta A and inhibited by BMP-2, -4, and -7 (13, 15).

1. Mikkola, M.L. and I. Thesleff (2003) Cytokine Growth Factor Rev. 14:211. 
2. Botchkarev, V.A. and M.Y. Fessing (2005) J. Invest. Dermatol. 10:247.  
3. Kere, J. et al. (1996) Nat. Genet. 13:409. 
4. Bayes, M. et al. (1998) Hum. Mol. Genet. 7:1661. 
5. Ezer, S. et al. (1999) Hum. Mol. Genet. 8:2079.  
6. Mikkola, M.L. et al. (1999) Mech. Dev. 88:133. 
7. Hashimoto, T. et al. (2006) Gene 371:42. 
8. Yan, M. et al. (2000) Science 290:523.
9. Chen, Y. et al. (2001) Proc. Natl. Acad. Sci. 98:7218.
10. Elomaa, O. et al. (2001) Hum. Mol. Genet. 10:953.
11. Pispa, J. et al. (2003) Gene Exp. Patterns 3:675.
12. Laurikkala, J. et al. (2002) Development 129:2541.
13. Laurikkala, J. et al. (2001) Dev. Biol. 229:443.
14. Cui, C.Y. et al. (2006) Proc. Natl. Acad. Sci. 103:9142.
15. Mou, C. et al. (2006) Proc. Natl. Acad. Sci. 103:9075.

Publications for EDA-A1/Ectodysplasin A1 (3944-ED)(1)

Publication using 3944-ED

• S Li, J Zhou, J Bu, K Ning, L Zhang, J Li, Y Guo, X He, H He, X Cai, Y Chen, PS Reinach, Z Liu, W Li Ectodysplasin A protein promotes corneal epithelial cell proliferation J. Biol. Chem., 2017;292(32):13391-13401. 2017 [PMID: 28655773] (In Vivo, Mouse)

Bioinformatics

• Gene Symbol: EDA
• Uniprot:
  • Q92838()