CRYBA2 Products

Description

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. CRYBA2( AAH06285, 1 a.a. - 198 a.a.) recombinant protein with GST. PLEASE NOTE - This product originates in Taiwan. If in stock in Taiwan, delivery is 10-14 days. If not in stock, lead times can be extended. We will inform you of any extended delays within 48 hours.

Bioinformatics

Product By Gene ID	1412
Alternate Names	Beta-A2 crystallin beta-crystallin A2 crystallin, beta A2 eye lens structural protein

Research Areas for CRYBA2

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Vision