Search Thermo Fisher Scientific
Search Thermo Fisher Scientific
The antibody was affinity-purified from mouse ascites by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE).
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.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
Protein Aliases: Beta crystallin B2; Beta crystallin Bp; Beta-B2 crystallin; Beta-crystallin B2; Beta-crystallin Bp; CCA 2; CRYB B2; CRYBB 2; crystallin, beta B2; CTA-221G9.7; eye lens structural protein; OTTHUMP00000198622; R.norvegicus CRYBB2 gene (crystallin, beta B2)
Gene Aliases: CCA2; Cryb-2; CRYB2; CRYB2A; CRYBB2; CTRCT3; D22S665
UniProt ID: (Human) P43320, (Mouse) P62696, (Rat) P62697
Entrez Gene ID: (Human) 1415, (Mouse) 12961, (Rat) 25422
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