Crystallin, gamma S (CRYGS) ELISA Kits

Crystallins are separated into two classes taxon-specific, or enzyme, and ubiquitous. Additionally we are shipping CRYGS Antibodies (80) and CRYGS Proteins (14) and many more products for this protein.

list all ELISA KIts Gene Name GeneID UniProt
CRYGS 12970 O35486
CRYGS 689897 P0C5E9
CRYGS 1427 P22914
How to order from antibodies-online
  • +1 877 302 8632
  • +1 888 205 9894 (toll-free)
  • Order online


Showing 5 out of 7 products:

Catalog No. Reactivity Sensitivity Range Images Quantity Delivery Price Details
Mouse 0.057 ng/mL 0.15 ng/mL - 10 ng/mL 96 Tests 13 to 16 Days
  96 Tests 15 to 18 Days
  96 Tests 15 to 18 Days
  96 Tests 15 to 18 Days
  96 Tests 15 to 18 Days

More ELISA Kits for CRYGS Interaction Partners

Mouse (Murine) Crystallin, gamma S (CRYGS) interaction partners

  1. 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

  2. Mutant Crygs gene can lead to changes of BFSP/filensin and other crystallins. Changes to these crystallins, together, may secondarily lead to cataract formation.

  3. mutation causes autosomal recessive cataracts; likely to be involved in epithelial cell proliferation, apoptosis, and migration

  4. gammaS consists of two topologically similar domains, arranged with an approximate twofold symmetry, and each domain shows close structural homology to closely related domains found in other members of the gamma-crystallin family.

  5. disruption of the Hsf4 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

Cow (Bovine) Crystallin, gamma S (CRYGS) interaction partners

  1. biophysical study on the nature and the magnitude of the gammaS-polyethylene glycol interactions

  2. The results are consistent with the hypothesis that short-range, weak, attractive interactions between alpha- and gamma-crystallins are necessary for maximum transparency of the lens.[gamma crystallin]

  3. Mass spectrometry analysis and a database search identified carbamylated proteins originating from alphaA-crystallin, betaB2- and gammaS-(betaS)-crystallins.

Human Crystallin, gamma S (CRYGS) interaction partners

  1. These results highlight the vital role of conserved Tyr corners in stabilizing Greek key motifs in gammaS crystallin and provide useful structural and functional insights into the mechanism of cataract formation in humans.

  2. aberrant modifications in gammaS-crystallin structure might contribute to the lower stability and higher aggregatory potency of the mutated protein, which subsequently resulted in cataracts in the patients

  3. 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.

  4. Cataract-related G18V point mutation affects CRYGS stability and hydration.

  5. novel mutation (G57W) in CRYGS in this Chinese family is associated with autosomal dominant pulverulent cataract.

  6. 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.

  7. The effects of the V41M mutation on the structural changes of gamma S-crystallin were studied.

  8. 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.

  9. 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

  10. age-dependent cleavage of gammaS-crystallin generates a peptide that binds to cell membranes

  11. The degree of deamidation for Gln92 and Gln170 was found to increase from birth to teen-age years and then to remain constant for four decades.

  12. Novel mutations in the crystalline genes have been identified in Chinese families with congenital cataracts.

  13. The presence of significant amounts of small peptides derived from gammaS- and betaB1-crystallins in the water-insoluble fraction of the lens indicates that these interact tightly with cytoskeletal or membrane components.

  14. 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.

  15. Partially folded aggregation intermediates of human gammaD-, gammaC-, and gammaS-crystallin are recognized and bound by human alphaB-crystallin.

  16. Deamidation in cataractous lenses is influenced by surface exposure.

  17. 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.

  18. when glutathione becomes bound to gammaS-crystallin, it causes it to bind in turn to the beta-crystallin polypeptides to form a dimer

  19. analysis of folding and stability of the isolated Greek key domains of the long-lived human lens proteins gammaD-crystallin and gammaS-crystallin

  20. report a novel missense mutation, p.V42M, in CRYGS associated with bilateral congenital cataract in a family of Indian origin

CRYGS Antigen Profile

Antigen Summary

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.

Gene names and symbols associated with Crystallin, gamma S (CRYGS) ELISA Kits

  • crystallin, gamma S (Crygs) antibody
  • crystallin gamma S (CRYGS) antibody
  • crystallin gamma S (Crygs) antibody
  • AI327013 antibody
  • CRYG8 antibody
  • CTRCT20 antibody
  • Opj antibody
  • rncat antibody

Protein level used designations for Crystallin, gamma S (CRYGS) ELISA Kits

beta-crystallin S , opacity due to poor secondary fiber cell junction , recessive nuclear cataract , crystallin, gamma polypeptide 8 , gamma-S-crystallin , gamma-crystallin S , gamma S-crystallin , crystallin, gamma S , gammaS-crystallin , crystallin, gamma 8

12970 Mus musculus
281724 Bos taurus
429134 Gallus gallus
460909 Pan troglodytes
689897 Rattus norvegicus
699720 Macaca mulatta
100101573 Oryctolagus cuniculus
100307056 Cavia porcellus
1427 Homo sapiens
607506 Canis lupus familiaris
100155317 Sus scrofa
Selected quality suppliers for CRYGS (CRYGS) ELISA Kits
Did you look for something else?