Search Thermo Fisher Scientific
Search Thermo Fisher Scientific
the dominant structural components of the vertebrate eye lens.
Immunogen sequence: MSSAPAPGP APASLTLWDE EDFQGRRCRL LSDCANVCER GGLPRVRSVK VENGVWVAFE YPDFQGQQFI LEKGDYPRWS AWSGSSSHNS NQLLSFRPVL CANHNDSRVT LFEGDNFQGC KFDLVDDYPS LPSMGWASKD VGSLKVSSGA WVAYQYPGYR GYQYVLERDR HSGEFCTYGE LGTQAHTGQL QSIRRVQH (1-197 aa encoded by BC006285)
Crystallins are separated into two classes: taxon-specific, or enzyme, and ubiquitous. The latter class constitutes the major proteins of the vertebrate eye, which function to maintain 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 defined 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 but absent in the acidic group). Beta-crystallins form aggregates of different sizes and are able to form homodimers through self-association or heterodimers with other beta-crystallins. This gene is a beta acidic group member. Three alternatively spliced transcript variants encoding identical proteins have been reported.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
Protein Aliases: Beta-A2 crystallin; Beta-crystallin A2; betaA2-crystallin; crystallin, beta A2; eye lens structural protein; lens structural protein
Gene Aliases: CRYBA2; CTRCT42; E130107M19Rik
UniProt ID: (Human) P53672, (Mouse) Q9JJV1
Entrez Gene ID: (Human) 1412, (Mouse) 12958, (Rat) 286925
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