Beta-crystallin A3 antibody

Background of Beta-crystallin A3 antibody

Crystallins are the domint structural components of the vertebrate eye lens. Defects in CRYBA1 are the cause of congenital zonular cataract with sutural opacities (CCZS).Crystallins are separated into two classes: taxon-specific, or enzyme, and ubiquitous. The latter class constitutes the major proteins of vertebrate eye lens and maintains the transparency and refractive index of the lens. Since lens central fiber cells lose their nuclei during development, these crystallins are made and then retained throughout life, making them extremely stable proteins. Mammalian lens crystallins are divided into alpha, beta, and gamma families; beta and gamma crystallins are also considered as a superfamily. Alpha and beta families are further divided into acidic and basic groups. Seven protein regions exist in crystallins: four homologous motifs, a connecting peptide, and N- and C-termil extensions. Beta-crystallins, the most heterogeneous, differ by the presence of the C-termil extension (present in the basic group, none in the acidic group). Beta-crystallins form aggregates of different sizes and are able to self-associate to form dimers or to form heterodimers with other beta-crystallins. This gene, a beta acidic group member, encodes two proteins (crystallin, beta A3 and crystallin, beta A1) from a single mR, the latter protein is 17 aa shorter than crystallin, beta A3 and is generated by use of an alterte translation initiation site. Deletion of exons 3 and 4 causes the autosomal domint disease 'zonular cataract with sutural opacities'. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Entrez Gene record to access additiol publications.