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Crystallins are separated into two classes taxon-specific, or enzyme, and ubiquitous. Additionally we are shipping CRYGS Proteins (14) and CRYGS Kits (11) and many more products for this protein.
Showing 10 out of 76 products:
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 (show BFSP1 Antibodies) and other crystallins. Changes to these crystallins, together, may secondarily lead to cataract formation.
disruption of the Hsf4 (show HSF4 Antibodies) 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 (show CRYAA Antibodies)
Mass spectrometry analysis and a database search identified carbamylated proteins originating from alphaA-crystallin (show CRYAA Antibodies), betaB2- and gammaS-(betaS)-crystallins.
The Tyr67Asn substitution was predicted to decrease the local hydrophobicity and affect the three-dimensional structure of gammaS-crystallin, and resulted in a portion of mutant protein translocation from the cytoplasm to cell membrane. This observations expand the mutation spectrum of CRYGS and provide further evidence for the genetic basis and molecular mechanism of congenital cataract.
Cataract-related G18V point mutation affects CRYGS stability and hydration.
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 (show CRYAB Antibodies).
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.
, opacity due to poor secondary fiber cell junction
, recessive nuclear cataract
, crystallin, gamma polypeptide 8
, gamma-crystallin S
, gamma S-crystallin
, crystallin, gamma S
, crystallin, gamma 8