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Crystallins are the dominant structural components of the vertebrate eye lens.. Additionally we are shipping CRYbB2 Antibodies (31) and CRYbB2 Proteins (15) and many more products for this protein.
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Results show that both betaB2- and betaA3-crystallin (show CRYBA1 ELISA Kits) bind calcium with moderate affinity.
combined with previously reported observations of alpha-crystallin quaternary structure have led us to propose a structural model of how activated alpha-crystallin chaperones unfolded betaB2-crystallin
Mass spectrometry analysis and a database search identified carbamylated proteins originating from alphaA-crystallin (show CRYAA ELISA Kits), betaB2- and gammaS-(betaS)-crystallins.
conserved Trp residues might play a more crucial role in the correct folding and structural integrity of beta-crystallin domains than in gamma-crystallins
The first pregnancy was terminated in week 22. Copy number variation analysis revealed, in both the aborted fetus and the mother, a 495 kb duplication at 22q11.23 encompassing CRYBB3 and CRYBB2
Study demonstrates that, in solution, human betaB2-crystallin is not domain swapped and exhibits a face-en-face dimer structure similar to the crystal structure of truncated betaB1-crystallin (show CRYBB1 ELISA Kits).
This is the first study to analyze the association between genetic variations in the CRYBB2 gene with PCa. rs9608380, associated with Prostate cancer, is a potentially functional variant
Congenital cataracts were caused by the de novo gene conversion event in CRYBB2 in a consanguineous Jewish Ashkenazi family.
missense mutation in CRYBB2 gene leads to progressive congenital membranous cataract by impacting the solubility and function of betaB2-crystallin
The distinct behaviors of the mutants suggested that the residue at position 188 might play a regulatory role in betaB2-crystallin aggregation/fibrillization but not reside in the core of the aggregates/fibrils.
The last strand at the C-terminus of CRYBB2 is important for the protein stability and assembly.
Identification of the first CRYBB2 mutation in an Italian family causing a clinical picture of autosomal dominant congenital cataract.
The congenital cataract-linked A2V mutation impairs tetramer formation and promotes aggregation of betaB2-crystallin.
In conclusion, CRYBB2 regulates expression of different lncRNAs to influence ovary development
ovaries from female Crybb2(-/-) mice exhibited significantly reduced numbers of primordial, secondary and pre-ovulatory follicles when compared with WT mice, while the rate of atretic follicles was also increased
BetaB2-crystallin has a role in hippocampal function and behavioral phenotypes.
The reduced fertility of Crybb2 knockout male mice may result from the disordered proliferation and apoptosis of germ cells in the testis, possibly due to reduced CaMKIV (show CAMK4 ELISA Kits) from the loss of Crybb2.
Removal of both amino- and carboxyl-terminal extensions of recombinant crystallin beta B2 increases the entropy and enthalpy of dimer binding but to a lesser degree than occurs in truncated recombinant beta A3 crystallin (show CRYBA1 ELISA Kits).
Thus, some of the fiber differentiation processes are likely mediated by RTK-dependent but Ras-independent pathways.
betaB2-crystallin is expressed in developing and mature sperm and mice of both sexes harboring the Philly mutation in the betaB2-crystallin gene are subfertile when analyzed on a Swiss Webster genetic background.
presence of measurable interactions between MIP26 and all crystallins, with the extent of interactions decreasing from alphaA- and alphaB-crystallin to betaB2- and gammaC-crystallin.
These results confirm the third allele of Crybb2 in the mouse that also affected exon 6 and the fourth Greek key motif. Moreover, expression analysis of Crybb2 identified for the first time distinct regions of expression in the brain.
BetaB2-crystallin is not essential for the normal development of a transparent lens in the mouse. It plays an increasingly important role in maintaining the transparency of the lens after birth.
Crystallins are the dominant structural components of the vertebrate eye lens.
crystallin, beta B2
, beta-crystallin B2
, beta B2-crystallin
, beta-B2 crystallin
, beta-crystallin Bp
, eye lens structural protein
, Philly cataract
, R.norvegicus CRYBB2 gene (crystallin, beta B2)
, Beta-B2 crystallin
, Beta-crystallin Bp