Crystallin, gamma D (CRYGD) ELISA Kits

Crystallins are separated into two classes taxon-specific, or enzyme, and ubiquitous. Additionally we are shipping Crystallin, gamma D Antibodies (49) and Crystallin, gamma D Proteins (10) and many more products for this protein.

list all ELISA KIts Gene Name GeneID UniProt
CRYGD 1421 P07320
CRYGD 12967 P04342
CRYGD 24278 P10067
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Top Crystallin, gamma D ELISA Kits at antibodies-online.com

Showing 4 out of 5 products:

Catalog No. Reactivity Sensitivity Range Images Quantity Delivery Price Details
Human
  96 Tests 2 to 3 Days
$713.90
Details
Mouse
  96 Tests 16 to 26 Days
$618.29
Details
Rat < 6.4 pg/mL 15.6 pg/mL - 1000 pg/mL   96 Tests 11 to 18 Days
$824.38
Details
Cow < 0.123 ng/mL 0.312 ng/mL - 20 ng/mL   96 Tests 11 to 18 Days
$895.45
Details

More ELISA Kits for Crystallin, gamma D Interaction Partners

Human Crystallin, gamma D (CRYGD) interaction partners

  1. a previously unknown oxidoreductase activity in gammaD-crystallin (HgammaD) is found. This activity was assigned to a redox-active internal disulfide bond that is dynamically exchanged among HgammaD molecules. The W42Q variant acts as a disulfide sink, reducing oxidized WT and forming a distinct internal disulfide that kinetically traps the aggregation-prone intermediate.

  2. 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.

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

  4. 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

  5. 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.

  6. 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.

  7. 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

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

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

  10. 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.

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

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

  13. 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.

  14. 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.

  15. 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.

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

  17. 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.

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

  19. 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.

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

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.

Crystallin, gamma D (CRYGD) 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. 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 (CRYGD) ELISA Kits

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

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

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

GENE ID SPECIES
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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