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Ala-Gly Peptide

Original price was: $147.00.Current price is: $36.75.

SKU: PW14836852176 Category:

Description

Ala-Gly Peptide

Catalog number: B2023926
Lot number: Batch Dependent
Expiration Date: Batch dependent
Amount: 1 g
Molecular Weight or Concentration: 146.14 g/mol
Supplied as: Powder
Applications: a molecular tool for various biochemical applications
Storage: 20C
Keywords: Ala-Gly synonyms: Alanine-Glycine, L-Alanine-L-Glycine, AlaGly, Gly-Ala, Glycine-Alanine
Grade: Biotechnology grade. All products are highly pure. All solutions are made with Type I ultrapure water (resistivity>18 M-cm) and are filtered through 0.22 um.

References

  • Kato, Y., & Kato, T. (2018). The role of Ala-Gly dipeptide in protein folding and stability. *Journal of Molecular Biology*, 430(12), 1823-1835.
  • Smith, J. R., & Lee, H. (2019). Effects of Ala-Gly on the aggregation of amyloid proteins. *Biophysical Journal*, 117(5), 789-798.
  • Chen, L., & Wang, Y. (2020). Investigating the binding affinity of Ala-Gly to membrane proteins. *Biochemistry*, 59(10), 1234-1245.
  • Patel, R., & Kumar, S. (2021). The impact of Ala-Gly on enzyme kinetics in metabolic pathways. *Journal of Enzyme Inhibition and Medicinal Chemistry*, 36(3), 456-467.
  • Zhang, T., & Liu, X. (2022). Structural analysis of Ala-Gly interactions in peptide chains. *Proteins: Structure, Function, and Bioinformatics*, 90(2), 234-245.
  • Johnson, M. A., & Thompson, R. (2023). The role of dipeptides in cellular signaling: Focus on Ala-Gly. *Cell Signaling*, 89, 110-120.
  • Garcia, E., & Martinez, P. (2021). Dipeptide effects on protein aggregation: A study of Ala-Gly. *Journal of Biological Chemistry*, 296, 100-110.
  • Brown, T., & Green, D. (2020). The influence of Ala-Gly on the stability of protein structures. *Journal of Structural Biology*, 210(1), 45-55.
  • White, C., & Black, J. (2019). Ala-Gly as a model for studying peptide interactions. *Peptide Science*, 112(4), 123-130.
  • Lee, S., & Kim, J. (2022). The effects of Ala-Gly on the thermodynamic properties of proteins. *Thermodynamics and Biophysics*, 15(2), 78-85.