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Crystallins are separated into two classes taxon-specific, or enzyme, and ubiquitous.
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Glycation of human gammaB-crystallin
Complex heterogeneous mutations in the gammaB crystallin gene have been described resulting in autosomal dominant congenital cataracts with three distinct phenotypes (lamellar, anterior polar, and complete cataracts) in the same family.
-47C allele of rs2289917 in CRYGB showed the strongest association with cataract.
The alphaB-crystallin (show CRYAB Proteins) oligomers formed long-lived stable complexes with their gammaD-crystallin substrates.
In gammaD-crystallin, methylation is exclusively at Cys (show DNAJC5 Proteins) 110, whereas in gammaC- and gammaB-crystallins, the principal methylation site is Cys (show DNAJC5 Proteins) 22 with minor methylation at Cys (show DNAJC5 Proteins) 79
Possible sites for posttranslational modifications in gamma B crystallin.
This study establishes baseline frequency data for four SNPs in CRYGA (show CRYGA Proteins) and CRYGB genes for future case control studies on the role of these SNPs in the genetic basis of cataract.
The cataract-causing mutation Crygb-nop has a 4 bp replacement in exon 3 at Ser138 truncating the wild-type sequence at 144. The mutated protein does not fold properly, resulting in amyloid-like intranuclear inclusions.
This dominant cataract was caused by the gammaB-S11R mutation.
Gamma-B crystallin synonymous codons provide a secondary code for protein folding in the cell.
results suggest that two regions of gamma-B crystallin (residues 61-74, 145-159) play key roles in aggregative interactions. The regions, each containing a single-turn helix in the native structure, are located in structurally analogous positions
Crystallins are separated into two classes taxon-specific, or enzyme, and ubiquitous. The latter class constitutes the major proteins of vertebrate eye lens and maintains 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 considered 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. Gamma-crystallins are a homogeneous group of highly symmetrical, monomeric proteins typically lacking connecting peptides and terminal extensions. They are differentially regulated after early development. Four gamma-crystallin genes (gamma-A through gamma-D) and three pseudogenes (gamma-E, gamma-F, gamma-G) are tandemly organized in a genomic segment as a gene cluster. Whether due to aging or mutations in specific genes, gamma-crystallins have been involved in cataract formation.
crystallin, gamma B
, gamma 2-cry
, gamma-crystallin B
, crystallin, gamma 1-2
, gamma-crystallin 3
, nuclear opacity
, crystallin, gamma polypeptide 2
, gamma-crystallin 1-2
, gamma-crystallin II