Recombinant Human Gamma-crystallin D(CRYGD)

Code CSB-EP006020HU
Size US$1726
  • (Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.

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Product Details

Purity Greater than 90% as determined by SDS-PAGE.
Target Names CRYGD
Uniprot No. P07320
Research Area Neuroscience
Alternative Names CACA; CCA3; CCP; CRGD_HUMAN; CRYG4; Crygd; Crystallin; gamma D; Crystallin; gamma-4; CTRCT4; Gamma crystallin D; Gamma D crystallin; Gamma-crystallin 4; Gamma-crystallin D; Gamma-D-crystallin; PCC
Species Homo sapiens (Human)
Source E.coli
Expression Region 1-174aa
Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request.
Mol. Weight 47.6kDa
Protein Length Full Length
Tag Info N-terminal GST-tagged
Form Liquid or Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol.
Note: If you have any special requirement for the glycerol content, please remark when you place the order.
If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. Our default final concentration of glycerol is 50%. Customers could use it as reference.
and FAQs
Protein FAQs
Storage Condition Store at -20°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet & COA Please contact us to get it.

Target Data

Function Crystallins are the dominant structural components of the vertebrate eye lens.
Gene References into Functions
  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. PMID: 28474685
  2. A molecular dynamics approach to explore the structural characterization of cataract causing mutation R58H on human gammaD crystallin. PMID: 29532225
  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 PMID: 29949747
  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. PMID: 30251679
  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. PMID: 28401204
  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 PMID: 28849415
  7. Aggregation of Trp > Glu point mutants of human gamma-D crystallin provides a model for hereditary or UV-induced cataract. PMID: 26991007
  8. the mechanism of aggregation of two gammaD-crystallin mutants, W42R and W42Q: the former a congenital cataract mutation PMID: 27417136
  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. PMID: 26732753
  10. The nonsense mutation c.471G>A of the CRYGD gene probably underlies the congenital cataract in the pedigree PMID: 27455011
  11. Single-molecule Force Spectroscopy Predicts a Misfolded, Domain-swapped Conformation in human gammaD-Crystallin Protein. PMID: 26703476
  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. PMID: 26147294
  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. PMID: 25403472
  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. PMID: 25613833
  15. oxidation-mimicking W42Q mutant of gammad-crystallin formed non-native polymers starting from a native-like state under physiological conditions PMID: 25787081
  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. PMID: 25205362
  17. The presence of anti-CCP antibodies was a reliable serologic marker in rheumatoid arthritis diagnosis and was associated with cigarette smoking. PMID: 24366391
  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. PMID: 25393041
  19. Results show that thermal denaturation of gammaD-crystallin results in sheet-like aggregates that contain cross-linked oligomers of the protein. PMID: 24415662
  20. This study identified a novel congenital nuclear and posterior polar cataract phenotype caused by the recurrent mutation p. R140X in CRYGD. PMID: 24465161
  21. Presentation and discussion of the first crystal structure of the P23T mutant at 2.5 A resolution. PMID: 23670788
  22. Outcome from protein formulation characterization supports the hypothesis that the gammaD-crystallin it is able to recover and improve the mechanical properties of chemical damaged hair. PMID: 23651449
  23. study establishes that UV-B irradiation of gammaD-Crystallin leads to structurally specific modifications and precipitation via two mechanisms: amorphous aggregates and amyloid fibers PMID: 23957864
  24. The missense P24T mutation in CRYGD was responsible for the coralliform cataract afflicting a four-generation Chinese family. PMID: 24103489
  25. Mass spectrometry identifies residues 80-163 as the amyloid core, which spans most of the C-terminal domain, the linker, and a small portion of the N-terminal domain. PMID: 23082813
  26. human W42R gammaD-crystallin mutant structure provides a link between congenital and age-related cataracts PMID: 23124202
  27. A missense mutation in CRYGD linked with autosomal dominant congenital cataract of aculeiform type. PMID: 22669729
  28. study of effects of G61C mutation on gammaD-crystallin structure, stability and aggregation; results suggest the decrease in protein stability followed by aggregation-prone property may be the major cause in hereditary cataract induced by the G61C mutation PMID: 21655238
  29. The mutations in CRYGD were shown to cause changes in protein surface polarity, hydrophobicity, and spatial structure, contributing to protein deposition and cataract formation. PMID: 18041179
  30. neither structural nor stability changes in the protein are responsible for the R76S gammaD-crystallin variant's association with cataract PMID: 22394327
  31. Upon acid-induced amyloid fibril formation, the C-terminal domain forms amyloid beta-sheets, the N-terminal domain becomes extremely disordered but lies near to the beta-sheets. Fibril nucleation & extension occur only in the C-terminal domain. PMID: 22328156
  32. The heterozygous 109C to A CRYGD missense mutation is associated with a distinct crystalline cataract in two US Caucasian pedigrees. PMID: 22219628
  33. mutants and possibly age-damaged gammaD-crystallin can escape quality control by lens chaperones rationalizing the observation that they nucleate protein aggregation and lead to cataract PMID: 22289178
  34. A novel substitution has been found in CRYGD in a Brazilian family with congenital cataract in which there is no segregation with the disease, indicating that it is probably not a disease-causing mutation. PMID: 21866214
  35. CRYGD gene mutation co-segregated with all autosomal dominant congenital nuclear cataract affected individuals and was not observed in either unaffected family members or in 200 normal unrelated individuals. PMID: 21031598
  36. Identification of the residues in the P23T mutant that give rise to novel hydrophobic surfaces, and regions of the protein backbone where fluctuations in different timescales are restricted, which explains how lens opacity could result from this mutation. PMID: 21827768
  37. A novel mutation in gammaD-crystallin associated with autosomal dominant congenital cataract in a Chinese family. PMID: 21527994
  38. P24T mutation of gammaD-crystallin (CRYGD) was responsible for two Chinese pedigrees with congenital coralliform cataracts. CRYGD and coralliform cataracts are highly related, and P24T may be a hot-point mutation for this disorder. PMID: 21552497
  39. Data show that only substitutions of the second Greek key pair of each crystallin domain slowed refolding, and suggest that the second Greek keys may provide nucleation sites during the folding of the double-Greek-key crystallin domains. PMID: 21432932
  40. S130P point mutations of gammaD crystallin was the most resistant to aggregation, indicating a decrease of its intrinsic aggregation propensity. PMID: 21184609
  41. The conformational features and aggregation properties of the mutant protein E107A human gammaD-crystallin (HGDC), associated with congenital nuclear cataract, were analyzed. PMID: 21197114
  42. Family having anterior polar coronary cataract that co-segregates with novel allele R77S of CRYGD in all affected members. PMID: 20508808
  43. This work thus provides direct evidence of the dominant role played by net hydrophobic and anisotropic protein-protein interactions in the aggregation of the P23T cataract-associated gammaD-crystallin. PMID: 20553008
  44. Findings indicate that Glu135 and Arg142 of gammaD-crystallin are crucial for stabilizing its hydrophobic domain interface in native conformation, and disruption of charges on the gammaD-crystallin surface may lead to unfolding and subsequent aggregat'n. PMID: 19937657
  45. Data show that during thermal denaturation, the mutant proteins exhibited lowered thermal stability compared with WT. PMID: 19758984
  46. This the first report of a mutation in the Gamma-D crystallin gene (CRYGD) resulting in autosomal dominant congenital cerulean cataracts. PMID: 12676897
  47. This study has identified an eighth type of cataract morphology associated with CRYGD and suggests that a CRYGD mutation may underlie the historically important "coralliform" cataract first reported in 1895. PMID: 15041957
  48. It appearS to be caused by a missense mutation in the CRYGD gene, further supporting the notion that alterations to CRYG play an important factor in human cataract formation. PMID: 15064679
  49. These results suggest that insolubility, rather than loss of stability, is the primary basis for human gammaD-crystallin P23T mutation-derived congenital cataracts. PMID: 15451671
  50. The cataract-causing mutation proline23 to threonine does not exhibit any significant structural change relative to the native protein. However, in marked contrast to the native protein, the mutant shows a dramatically lowered solubility. PMID: 15709761
  51. domain interface residues of the refolded C-td act as a nucleating center for refolding of the N-td PMID: 15722442
  52. To our knowledge, this is the first example of phenotypic heterogeneity associated with the Arg 58 His CRYGD mutation. PMID: 16030500
  53. Hydrophobic cluster residues of gammaD crystallin contribute to protein folding and protein stability. PMID: 16046626
  54. The R36S mutation in CRYGD identified in this Chinese family caused a nuclear golden crystal cataract phenotype not described before. PMID: 16288201
  55. interface deamidation decreases the thermodynamic stability of HgammaD-Crys and lowers the kinetic barrier to unfolding due to introduction of a negative charge into the domain interface PMID: 16891314
  56. The backbone conformation of tryptophans in human gammaD-Crys may have evolved to enable the lens to become a very effective UV filter, while the efficient quenching provides an in situ mechanism to protect the tryptophans from photochemical degradation. PMID: 16981715
  57. R36S mutation in CRYGD gene results in an autosomal dominant congenital cataract phenotype that is different from previous reports. This is the first report of congenital cataract caused by R36S mutation in CRYGD gene. PMID: 17217786
  58. We identified a mutation in the CRYGD gene (P23S) of the gamma-crystallin gene cluster that is associated with a polymorphic congenital cataract that occurs with frequency of approximately 0.3% in a human population. PMID: 17564961
  59. analysis of folding and stability of the isolated Greek key domains of the long-lived human lens proteins gammaD-crystallin and gammaS-crystallin PMID: 17905830
  60. The liquid-liquid coexistence curve and the diffusivity of the P23V mutant human gammaD-crystallin is investigated. PMID: 17923670
  61. Novel mutation, c.494delG, in CRYGD associated with nuclear cataract. Hypothesized to impair nuclear transfiguration and degradation in lens fiber cell differentiation, leading to opacity formation during lens development. PMID: 18079686
  62. Human gammaD-crystallin formed amyloid fibrils upon incubation at acid pH. PMID: 18253099
  63. This is the first reported case of a congenital coralliform cataract phenotype associated with the mutation of Gly61Cys (P.G61C) in the CRYGD gene; it demonstrates a possible mechanism of action for the mutant gene. PMID: 18334953
  64. Data show that a combination of energy transfer with electron transfer together with the high rigidity of the protein matrix around Trps, could protect HgammaD-Crys from excited-state reactions causing permanent covalent damage. PMID: 18795792
  65. The structure of the cataract-causing P23T mutant of human gammaD-crystallin exhibits distinctive local conformational and dynamic changes PMID: 19216553
  66. high-resolution NMR studies of human gammaD-crystallin and P23T was presented. PMID: 19275895
  67. Fast charge transfer quenching is an evolved property of the gamma D-crystallin fold, probably protecting it from ultraviolet-induced photodamage. PMID: 19358562
  68. Raman spectroscopy analysis shows that gamma D-crystallin mutant Arg14Cys protein forms aggregates even at pH 4.5; the lower pH enables monitoring of the evolution of disulfide cross-links with conformations around the CC-disulfide-CC dihedral angles. PMID: 19382745
  69. This first report of p.P23T CRYGD mutation underlying cerulean cataract in the Saudi population strongly supports the mutation's relation with the phenotype. PMID: 19633732
  70. A novel R15S mutation in CRYGD caused congenital coralliform cataract in a Chinese family. PMID: 19668596

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Involvement in disease Cataract 4, multiple types (CTRCT4)
Protein Families Beta/gamma-crystallin family
Database Links

HGNC: 2411

OMIM: 115700

KEGG: hsa:1421

STRING: 9606.ENSP00000264376

UniGene: Hs.546247

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