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Crystallin, gamma S Proteins (CRYGS)

Crystallins are separated into two classes taxon-specific, or enzyme, and ubiquitous. Additionally we are shipping CRYGS Antibodies (63) and CRYGS Kits (10) and many more products for this protein.

list all proteins Gene Name GeneID UniProt
CRYGS 1427 P22914
CRYGS 12970 O35486
CRYGS 689897 P0C5E9
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Top CRYGS Proteins at antibodies-online.com

Showing 10 out of 13 products:

Catalog No. Origin Source Conjugate Images Quantity Supplier Delivery Price Details
HOST_Escherichia coli (E. coli) Human His tag „Crystallography Grade“ protein due to multi-step, protein-specific purification process 1 mg Log in to see 29 to 34 Days
$4,331.68
Details
HOST_Escherichia coli (E. coli) Mouse His tag „Crystallography Grade“ protein due to multi-step, protein-specific purification process 1 mg Log in to see 29 to 34 Days
$4,331.68
Details
HOST_Escherichia coli (E. coli) Human His tag 100 μg Log in to see 7 to 8 Days
$319.00
Details
HOST_Wheat germ Human GST tag 10 μg Log in to see 9 Days
$405.71
Details
Yeast Cyprinus carpio His tag   1 mg Log in to see 56 to 66 Days
$2,401.67
Details
Yeast Rat His tag   1 mg Log in to see 56 to 66 Days
$2,414.50
Details
Yeast Cow His tag   1 mg Log in to see 56 to 66 Days
$2,414.50
Details
Yeast Dog His tag   1 mg Log in to see 56 to 66 Days
$2,414.50
Details
Yeast Rabbit His tag   1 mg Log in to see 56 to 66 Days
$2,418.17
Details
HOST_Escherichia coli (E. coli) Human Un-conjugated   100 μg Log in to see 3 to 4 Days
$382.86
Details

CRYGS Proteins by Origin and Source

Origin Expressed in Conjugate
Human , ,
,
Mouse (Murine)

Rat (Rattus) ,

Top referenced CRYGS Proteins

  1. Human CRYGS Protein expressed in Escherichia coli (E. coli) - ABIN667553 : Jester: Corneal crystallins and the development of cellular transparency. in Seminars in cell & developmental biology 2008 (PubMed)
    Show all 2 references for ABIN667553

More Proteins for Crystallin, gamma S (CRYGS) Interaction Partners

Human Crystallin, gamma S (CRYGS) interaction partners

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

  2. 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.

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

  4. 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.

  5. 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

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

  7. 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.

  8. Partially folded aggregation intermediates of human gammaD-, gammaC-, and gammaS-crystallin are recognized and bound by human alphaB-crystallin (show CRYAB Proteins).

  9. 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.

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

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 (show BFSP1 Proteins) and other crystallins. Changes to these crystallins, together, may secondarily lead to cataract formation.

  3. disruption of the Hsf4 (show HSF4 Proteins) 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 Proteins)

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

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

CRYGS Protein Profile

Protein 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 Proteins (CRYGS)

  • crystallin, gamma S (CRYGS)
  • crystallin, gamma S (Crygs)
  • beta-crystallin S-like (LOC100155317)
  • AI327013 protein
  • CRYG8 protein
  • CTRCT20 protein
  • Opj protein
  • rncat protein

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

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

GENE ID SPECIES
429134 Gallus gallus
460909 Pan troglodytes
699720 Macaca mulatta
100307056 Cavia porcellus
100155317 Sus scrofa
1427 Homo sapiens
12970 Mus musculus
689897 Rattus norvegicus
281724 Bos taurus
607506 Canis lupus familiaris
100101573 Oryctolagus cuniculus
Selected quality suppliers for CRYGS Proteins (CRYGS)
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