The Crybb3 Polyclonal Antibody (PACO08617) is a valuable tool for researchers studying Crybb3, a protein involved in eye development and function. This antibody, generated in rabbits, is highly specific for detecting Crybb3 in various samples and is validated for use in immunohistochemistry and immunofluorescence applications.Crybb3, a beta-crystallin protein, is primarily expressed in the lens of the eye and plays a key role in maintaining lens transparency and refractive index. Mutations in the Crybb3 gene have been linked to cataract formation and other eye disorders, making it an important target for investigation in ophthalmology research.
The Crybb3 Polyclonal Antibody enables researchers to visualize and study the expression and localization of Crybb3 in different cell types and tissues, providing valuable insights into its function and potential implications for eye health. This antibody is a valuable tool for studies aimed at understanding the molecular mechanisms underlying eye development and disease.
CRYBB3: a major structural protein of the eye lens. A member of the beta/gamma-crystallin family. Protein type: CytoskeletalChromosomal Location of Human Ortholog: 22q11.23Molecular Function: protein bindingDisease: Cataract 22, Multiple Types
UniProt Protein Details:
NCBI Summary:
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-B2. Mutations in this gene result in cataract congenital nuclear autosomal recessive type 2. [provided by RefSeq, Feb 2013]
