|Other Names||Beta-crystallin A4, Beta-A4 crystallin, CRYBA4|
|Format||Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Function||Crystallins are the dominant structural components of the vertebrate eye lens.|
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Crystallins are separated into two classes:taxon-specific, or enzyme, and ubiquitous. The latter classconstitutes the major proteins of vertebrate eye lens and maintainsthe transparency and refractive index of the lens. Since lenscentral fiber cells lose their nuclei during development, thesecrystallins are made and then retained throughout life, making themextremely stable proteins. Mammalian lens crystallins are dividedinto alpha, beta, and gamma families; beta and gamma crystallinsare also considered as a superfamily. Alpha and beta families arefurther divided into acidic and basic groups. Seven protein regionsexist in crystallins: four homologous motifs, a connecting peptide,and N- and C-terminal extensions. Beta-crystallins, the mostheterogeneous, 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 toself-associate to form dimers or to form heterodimers with otherbeta-crystallins. This gene, a beta acidic group member, is part ofa gene cluster with beta-B1, beta-B2, and beta-B3. [provided byRefSeq].
Zhou, G., et al. Mol. Vis. 16, 1019-1024 (2010) :Zhang, X., et al. Mol. Vis. 15, 2911-2918 (2009) :Billingsley, G., et al. Am. J. Hum. Genet. 79(4):702-709(2006)Collins, J.E., et al. Genome Biol. 5 (10), R84 (2004) :Mackay, D.S., et al. Am. J. Hum. Genet. 71(5):1216-1221(2002)
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