Recombinant Human Beta-crystallin S(CRYGS

Code CSB-EP006025HU
Size US$1726
Image
  • (Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.

Have Questions? Leave a Message or Start an on-line Chat

Product Details

Purity Greater than 90% as determined by SDS-PAGE.
Target Names CRYGS
Uniprot No. P22914
Alternative Names AI327013; Beta-crystallin S; CRBS_HUMAN; CRYG8; crygs; Crystallin; gamma 8; Crystallin; gamma polypeptide 8; Crystallin; gamma S; CTRCT20; Gamma crystallin S; Gamma S crystallin; Gamma-crystallin S; Gamma-S-crystallin; Opacity due to poor secondary fiber cell junction; recessive nuclear cataract; Opj; rncat
Species Homo sapiens (Human)
Source E.coli
Expression Region 2-178aa
Target Protein Sequence SKTGTKITFYEDKNFQGRRYDCDCDCADFHTYLSRCNSIKVEGGTWAVYERPNFAGYMYILPQGEYPEYQRWMGLNDRLSSCRAVHLPSGGQYKIQIFEKGDFSGQMYETTEDCPSIMEQFHMREIHSCKVLEGVWIFYELPNYRGRQYLLDKKEYRKPIDWGAASPAVQSFRRIVE
Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request.
Mol. Weight 47.9kDa
Protein Length Full Length of Mature Protein
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.
Troubleshooting
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. 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 PMID: 29857103
  2. 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. PMID: 29964096
  3. Cataract-related G18V point mutation affects CRYGS stability and hydration. PMID: 27052457
  4. novel mutation (G57W) in CRYGS in this Chinese family is associated with autosomal dominant pulverulent cataract. PMID: 24328668
  5. 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. PMID: 26158710
  6. The effects of the V41M mutation on the structural changes of gamma S-crystallin were studied. PMID: 24287181
  7. 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. PMID: 23761725
  8. 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 PMID: 23284690
  9. age-dependent cleavage of gammaS-crystallin generates a peptide that binds to cell membranes PMID: 22995907
  10. 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. PMID: 22593035
  11. 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. PMID: 21244846
  12. Partially folded aggregation intermediates of human gammaD-, gammaC-, and gammaS-crystallin are recognized and bound by human alphaB-crystallin. PMID: 20621668
  13. Deamidation in cataractous lenses is influenced by surface exposure. PMID: 12093281
  14. 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. PMID: 12475213
  15. when glutathione becomes bound to gammaS-crystallin, it causes it to bind in turn to the beta-crystallin polypeptides to form a dimer PMID: 14763903
  16. report a novel missense mutation, p.V42M, in CRYGS associated with bilateral congenital cataract in a family of Indian origin PMID: 19262743
  17. Fast charge transfer quenching is an evolved property of the gamma S-crystallin fold, probably protecting it from ultraviolet-induced photodamage. PMID: 19358562
  18. Results confirm the high stability of wild-type HgammaS-crystallin and demonstrates that the G18V mutation destabilizes the protein toward heat and GuHCl-induced unfolding. PMID: 19558189

Show More

Hide All

Involvement in disease Cataract 20, multiple types (CTRCT20)
Protein Families Beta/gamma-crystallin family
Database Links

HGNC: 2417

OMIM: 116100

KEGG: hsa:1427

STRING: 9606.ENSP00000312099

UniGene: Hs.376209

Most popular with customers

Newsletters

Get all the latest information on Events, Sales and Offers. Sign up for newsletter today.

© 2007-2020 CUSABIO TECHNOLOGY LLC All rights reserved. 鄂ICP备15011166号-1