CRYBA2 Break Apart FISH Probe

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. [provided by RefSeq, Jul 2008]


Gene Details
SKU Test Kits Buffer Dye Color Order Now
CRYBA2BA-20-REGO 20 (40 μL) 200 μL color color Request Pricing
CRYBA2BA-20-REGR 20 (40 μL) 200 μL color color Request Pricing
CRYBA2BA-20-ORGR 20 (40 μL) 200 μL color color Request Pricing
CRYBA2BA-20-GOGR 20 (40 μL) 200 μL color color Request Pricing
CRYBA2BA-20-GRRE 20 (40 μL) 200 μL color color Request Pricing
CRYBA2BA-20-GROR 20 (40 μL) 200 μL color color Request Pricing
CRYBA2BA-20-GRGO 20 (40 μL) 200 μL color color Request Pricing
CRYBA2BA-20-AQOR 20 (40 μL) 200 μL color color Request Pricing

Gene Summary

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. [provided by RefSeq, Jul 2008]

Gene Details

Gene Symbol : CRYBA2

Gene Name : Crystallin beta A2

Chromosome : CHR 2: 218,993,404-218,990,189

Locus : 2q35

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