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Facts about Tumor necrosis factor receptor superfamily member EDAR.
Receptor for EDA isoform A1, but not for EDA isoform A2.
Mediates the activation of NF-kappa-B and JNK.May encourage caspase-independent cell death. .
Human | |
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Gene Name: | EDAR |
Uniprot: | Q9UNE0 |
Entrez: | 10913 |
Belongs to: |
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No superfamily |
Anhidrotic ectodysplasin receptor 1; DLED3; Ectodermal dysplasia receptor; ectodysplasin 1, anhidrotic receptor; ectodysplasin A receptor; Ectodysplasin-A receptor; ED1R; ED5; EDA1R; EDA3EDA-A1 receptor; EDA-A1R; EDAR; FLJ94390; HRM1; mouse, homolog of; tumor necrosis factor receptor superfamily member EDAR
Mass (kDA):
48.582 kDA
Human | |
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Location: | 2q13 |
Sequence: | 2; NC_000002.12 (108894471..108989256, complement) |
Detected in fetal kidney, lung, skin and cultured neonatal epidermal keratinocytes. Not detected in lymphoblast and fibroblast cell lines.
Membrane; Single-pass type I membrane protein.
To understand Boster Bio: Best Uses Of The Edar Marker, you need to know about Steven Boster, a biotechnology innovator and immunochemist. Boster offers high-affinity primary antibodies, which are well-validated on Immunohistochemistry, Western Blotting and ELISA. Learn more information about Steven Boster, including his background and the current projects.
The EDAR candidate gene is a candidate for a rare condition called autosomal-recessive hypohidrotic ectodermal dysfunctiona. Monreal et.al. Monreal et al. discovered it in 2002. The gene was located in the interval 2q11-q13 between the markers D2S293 and D2S121. However, the EDAR gene has not been fully mapped to the candidate gene locus in all families.
The EDAR gene provides instructions for the ectodysplasin A receptor protein, a crucial factor in interactions between two embryonic cell layers. These cell layers (known as ectoderm-mesoderm) are the basis for many of our organs. This receptor is required for the formation of many body structures including skin, hair nails, teeth, and teeth. The 370A allele is associated to a higher sweat gland density, straighter hair, and lower beard thickness.
To understand the role that EDAR markers play in antibody affinity maturation, it is necessary to first understand how clone lines are maintained. In addition to cloning antibodies, this technique is an effective tool in antibody research. Next-generation sequencing is used in this technique to increase the depth and allow for large-scale determinations the paired H or L chains. The single-cell sequencing method has allowed us to use computational tools to reconstruct clonal lineages. Crystal structures of affinity-matured antibodies have also helped us understand how these molecules change over the course of time.
Studying the interactions between antibody molecules haptens allows us to better understand how affinity maturation works. The two antibodies are related because they both exhibit large conformational changes upon engagement of the hapten, while their structures are quite different. The formation additional hydrogen bonds was the first phase. The second phase of affinity matured was marked by an increase of salt bridges.
Next is the identification of antibodies with high affinity for antigens of concern. NGS allows researchers the ability to identify the germ-line progenitors and intermediates on the antibody maturation paths. Single-cell analysis is also available to analyze antibody evolution during virus infection. This makes it possible to detect virus specific antigens. It has been demonstrated that high-affinity antibodies boost the host’s immune defense.
EDAR-based antibody maturation is based on additional interactions with the antigen. The V2 peptide, the basis of the HIV-1 envelope glycoprotein, is a potential target for affinity-matured CH58. Recent studies have revealed that the structure and function of this antibody's germline precursor, both in the bound form and the unliganded version, were determined. The formation two new salt bridges promotes affinity mature.
In this study, anti-hapten antibodies were used that reacted with haptens the same size and orientation of their antigen-binding Epitope. This allowed us to identify antibodies that reacted with distant relatives of the original hapten. This study also revealed the importance epitope structure in antibody-binding. We will now discuss in detail the antigen/antibody interaction in the next sections.
PMID: 10431241 by Monreal A.W., et al. Mutations in the human homologue of mouse dl cause autosomal recessive and dominant hypohidrotic ectodermal dysplasia.
PMID: 11039935 by Yan M., et al. Two-amino acid molecular switch in an epithelial morphogen that regulates binding to two distinct receptors.