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Crystallins are separated into two classes taxon-specific, or enzyme, and ubiquitous. Zusätzlich bieten wir Ihnen CRYGS Proteine (14) und CRYGS Kits (7) und viele weitere Produktgruppen zu diesem Protein an.
Showing 10 out of 77 products:
Human Polyclonal CRYGS Primary Antibody für EIA, WB - ABIN950652
Acosta-Sampson, King: Partially folded aggregation intermediates of human gammaD-, gammaC-, and gammaS-crystallin are recognized and bound by human alphaB-crystallin chaperone. in Journal of molecular biology 2010
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Human Polyclonal CRYGS Primary Antibody für EIA, IHC (fro) - ABIN492834
Quax-Jeuken, Driessen, Leunissen, Quax, de Jong, Bloemendal: beta s-Crystallin: structure and evolution of a distinct member of the beta gamma-superfamily. in The EMBO journal 1985
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Human Polyclonal CRYGS Primary Antibody für EIA, IP - ABIN492833
Robinson, Lampi, Speir, Kruppa, Easterling, Robinson: Quantitative measurement of young human eye lens crystallins by direct injection Fourier transform ion cyclotron resonance mass spectrometry. in Molecular vision 2006
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Human Polyclonal CRYGS Primary Antibody für WB - ABIN654694
Chen, Callis, King: Mechanism of the very efficient quenching of tryptophan fluorescence in human gamma D- and gamma S-crystallins: the gamma-crystallin fold may have evolved to protect tryptophan residues from ultraviolet photodamage. in Biochemistry 2009
novel mutation (G57W) in CRYGS in this Chinese family is associated with autosomal dominant pulverulent cataract.
The data suggest that enhanced attractive protein-protein interactions, arising from the deamidation of HGS, promote protein aggregation, thereby leading to increased light scattering and opacity over time.
The effects of the V41M mutation on the structural changes of gamma S-crystallin were studied.
The cataract-associated mutant D26G of human gammaS-crystallin is remarkably close to the wild type molecule in structural features, with only a microenvironmental change in the packing around the mutation site.
replacement of valine in position 42 by the longer and bulkier methionine in human gammaS-crystallin perturbs the compact beta-sheet core packing topology in the N-terminal domain of the molecule
age-dependent cleavage of gammaS-crystallin generates a peptide that binds to cell membranes
Molecular dynamics (MD) simulations, circular dichroism (CD), and dynamic light scattering (DLS) measurements were used to investigate the aggregation propensity of the eye-lens protein gammaS-crystallin.
Partially folded aggregation intermediates of human gammaD-, gammaC-, and gammaS-crystallin are recognized and bound by human alphaB-crystallin (zeige CRYAB Antikörper).
A lens gamma S-crystallin has been identified with an in vivo modification, S-methylation of cysteine residues, that may block intermolecular disulfide bondng and serve as a form of protection against cataract.
when glutathione becomes bound to gammaS-crystallin, it causes it to bind in turn to the beta-crystallin polypeptides to form a dimer
gammaS may have a functional role related to actin, perhaps in 'shepherding' filaments to maintain the optical properties of the lens cytoplasm and normal fiber cell maturation
Mutant Crygs gene can lead to changes of BFSP/filensin (zeige BFSP1 Antikörper) and other crystallins. Changes to these crystallins, together, may secondarily lead to cataract formation.
disruption of the Hsf4 (zeige HSF4 Antikörper) gene leads to cataracts via at least three pathways: down-regulation of gamma-crystallin, particularly gamma S-crystallin; decreased lens beaded filament expression; and loss of post-translational modification of alpha A-crystallin (zeige CRYAA Antikörper)
Mass spectrometry analysis and a database search identified carbamylated proteins originating from alphaA-crystallin (zeige CRYAA Antikörper), betaB2- and gammaS-(betaS)-crystallins.
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. This gene encodes a protein initially considered to be a beta-crystallin but the encoded protein is monomeric and has greater sequence similarity to other gamma-crystallins. This gene encodes the most significant gamma-crystallin in adult eye lens tissue. Whether due to aging or mutations in specific genes, gamma-crystallins have been involved in cataract formation.
, gamma S-crystallin
, crystallin, gamma S
, crystallin, gamma 8
, gamma-crystallin S
, opacity due to poor secondary fiber cell junction
, recessive nuclear cataract
, crystallin, gamma polypeptide 8