Crystallin, gamma D Protéines (CRYGD)

Crystallins are separated into two classes taxon-specific, or enzyme, and ubiquitous. De plus, nous expédions Crystallin, gamma D Anticorps (45) et Crystallin, gamma D Kits (6) et beaucoup plus de produits pour cette protéine.

afficher tous les protéines Gène GeneID UniProt
CRYGD 1421 P07320
CRYGD 12967 P04342
CRYGD 24278 P10067
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Showing 7 out of 10 products:

Catalogue No. Origin Source Conjugué Images Quantité Fournisseur Livraison Prix Détails
Cellules d'insectes Humain His tag „Crystallography Grade“ protein due to multi-step, protein-specific purification process 1 mg Connectez-vous pour afficher 50 Days
Cellules d'insectes Souris His tag „Crystallography Grade“ protein due to multi-step, protein-specific purification process 1 mg Connectez-vous pour afficher 50 Days
Wheat germ Humain GST tag 10 μg Connectez-vous pour afficher 11 to 12 Days
Escherichia coli (E. coli) Humain His tag 100 μg Connectez-vous pour afficher 13 to 16 Days
HEK-293 Cells Humain Myc-DYKDDDDK Tag Validation with Western Blot 20 μg Connectez-vous pour afficher 11 Days
Levure Rat His tag   1 mg Connectez-vous pour afficher 60 to 71 Days
Levure Boeuf (Vache) His tag   1 mg Connectez-vous pour afficher 60 to 71 Days

CRYGD Protéines protéines par origine et source

Origin Exprimée danse Conjugué
Human , , ,
, ,
Mouse (Murine)

Rat (Rattus)

Plus protéines pour Crystallin, gamma D (CRYGD) partenaires d'interaction

Human Crystallin, gamma D (CRYGD) interaction partners

  1. At physiological pH, CRYGD forms aggregates that look amorphous and disordered by electron microscopy. Surprisingly, solid-state NMR reveals that these amorphous deposits have a high degree of structural homogeneity at the atomic level and that the aggregated protein retains a native-like conformation, with no evidence for large-scale misfolding.

  2. A molecular dynamics approach to explore the structural characterization of cataract causing mutation R58H on human gammaD crystallin.

  3. This research compared the effects of various glycation modifiers on Hgammad-crystallin aggregation, by treating samples of Hgammad-crystallin with ribose, galactose, or methylglyoxal using several biophysical techniques

  4. Study reports the identification of Cys111 as the major residue responsible for disulfide formation in protein dimers as well as for Cu2+-induced aggregation of human gammaD-crystallin.

  5. Using the P23T mutant of gammaD-crystallin, a protein associated with congenital cataract, we have demonstrated that the equilibrium solubility boundary and solution behavior measured using phase diagrams of purified protein solutions is consistent with the assembly of the protein expressed in cell-free expression medium in artificial cells (without fluorescent labelling) and condensates formed in mammalian cells.

  6. we identified two heterozygous rare variants in genes that are involved in early cataract development; the novel c.809C>A; p.(Ser270Tyr) in MAF and the c.168C>G; p.(Tyr56 *) variant in CRYGD, previously reported as pathogenic

  7. Aggregation of Trp > Glu point mutants of human gamma-D crystallin provides a model for hereditary or UV-induced cataract.

  8. the mechanism of aggregation of two gammaD-crystallin mutants, W42R and W42Q: the former a congenital cataract mutation

  9. Mutational analysis of CRYGD identified a recurrent (p.P24T) mutation in two unrelated families with congenital coralliform cataracts and three novel (p.Q101X, p.E104fsX4 and p.E135X) mutations in three families with congenital nuclear cataracts.

  10. The nonsense mutation c.471G>A of the CRYGD gene probably underlies the congenital cataract in the pedigree

  11. Single-molecule Force Spectroscopy Predicts a Misfolded, Domain-swapped Conformation in human gammaD-Crystallin Protein.

  12. We have identified a novel mutation, c.451_452insGACT, in CRYGD, which is associated with nuclear cataract. This is the first insertion mutation of CRYGD found to cause autosomal dominant congenital cataract.

  13. We have used trio-based exome sequencing to uncover a recurrent missense mutation in CRYGD and two novel missense mutations in GJA8 associated with autosomal dominant cataract in three nuclear families.

  14. Created are three double mutants of human gamma D-crystallin for which the phase diagrams for singly mutated proteins can be used to predict the behavior of the double mutants.

  15. oxidation-mimicking W42Q mutant of gammad-crystallin formed non-native polymers starting from a native-like state under physiological conditions

  16. Shared epitopes and smoking were associated with the production of anti-CCP antibodies and rheumatoid factors of IgM and IgA isotypes, which again were associated with erosive disease at presentation only in smokers.

  17. The presence of anti-CCP antibodies was a reliable serologic marker in rheumatoid arthritis diagnosis and was associated with cigarette smoking.

  18. These results indicated that the single lysine residue at the second position (K2) is acetylated at an early age and that the amount of K2-acetylated gamma D-crystallin increased with age.

  19. Results show that thermal denaturation of gammaD-crystallin results in sheet-like aggregates that contain cross-linked oligomers of the protein.

  20. This study identified a novel congenital nuclear and posterior polar cataract phenotype caused by the recurrent mutation p. R140X in CRYGD.

Mouse (Murine) Crystallin, gamma D (CRYGD) interaction partners

  1. Mutant gammaD-V76D reduces protein solubility in the lens and forms substantial intranuclear aggregates that disrupt the denucleation process of inner lens fiber cells

Cow (Bovine) Crystallin, gamma D (CRYGD) interaction partners

  1. 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.

Profil protéine Crystallin, gamma D (CRYGD)

Profil protéine

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. Four gamma-crystallin genes (gamma-A through gamma-D) and three pseudogenes (gamma-E, gamma-F, gamma-G) are tandemly organized in a genomic segment as a gene cluster. 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 D Protéines (CRYGD)

  • crystallin gamma D L homeolog (crygd.L)
  • crystallin gamma D (CRYGD)
  • crystallin, gamma D (CRYGD)
  • crystallin, gamma D (Crygd)
  • Aey4 Protéine
  • CACA Protéine
  • CCA3 Protéine
  • CCP Protéine
  • cry-g-D Protéine
  • Cryg-1 Protéine
  • Cryg4 Protéine
  • CRYGD Protéine
  • CTRCT4 Protéine
  • DGcry-1 Protéine
  • Len Protéine
  • Lop12 Protéine
  • MGC85594 Protéine
  • PCC Protéine

Protein level used designations for Crystallin, gamma D Protéines (CRYGD)

crystallin, gamma D , gamma-D-crystallin , gamma-crystallin D , gamma crystallin 4 , gamma-crystallin 4 , gamma-crystallin 1 , lens opacity 12 , Crystallin, gamma polypeptide 4 , gamma-crystallin 2-2 , gamma-crystallin IIIB

447192 Xenopus laevis
459906 Pan troglodytes
488495 Canis lupus familiaris
1421 Homo sapiens
12967 Mus musculus
24278 Rattus norvegicus
281723 Bos taurus
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