Use your antibodies-online credentials, if available.
Keine Produkte auf Ihrer Vergleichsliste.
Ihr Warenkorb ist leer.
Crystallins are separated into two classes taxon-specific, or enzyme, and ubiquitous. Zusätzlich bieten wir Ihnen CRYbA2 Antikörper (13) und CRYbA2 Proteine (10) und viele weitere Produktgruppen zu diesem Protein an.
Whole exome sequencing in dominant cataract (zeige MIP ELISA Kits) identifies a new causative factor, CRYBA2, and a variety of novel alleles in known genes.
The cell-stress molecules alphaB-crystallin (zeige CRYAB ELISA Kits) and iNOS (zeige NOS2 ELISA Kits) are overexpressed in GNE (zeige GNE ELISA Kits) myopathy muscle and may identify early disease mechanisms.
These findings demonstrate the first mutation in the Cryba2 gene
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.
crystallin, beta A2
, beta-crystallin A2
, eye lens structural protein
, beta-A2 crystallin
, lens structural protein