Beta-Crystallin B2 (CRYBB2) ELISA Kit for Monkey

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-terminal extensions. Beta-crystallins, the most heterogeneous, differ by the presence of the C-terminal 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 basic group member, is part of a gene cluster with beta-A4, beta-B1, and beta-B3. A chain-terminating mutation was found to cause type 2 cerulean cataracts. [provided by RefSeq, Jul 2008]

CRYBB2: a major structural protein of the eye lens. A member of the beta/gamma-crystallin family. Defects are the cause of congenital cerulean type 2 cataract, sutural cataract with punctate and cerulean opacities, and Coppock-like cataract.

Chromosomal Location of Human Ortholog: 22q11.23

Molecular Function: identical protein binding; protein homodimerization activity; structural molecule activity; structural constituent of eye lens

Biological Process: camera-type eye development; visual perception; response to stimulus

Disease: Cataract 3, Multiple Types