Phosphorylation is a post translational modification where a hydrogen atom in Serine, Threonine or Tyrosine is replaced by PO3H2.
The incorporation of phosphorylated residues is in most cases straight forward. Nevertheless, when the objective is to obtain high quality material, we know from experience that you need the better reagents, a sound synthesis methodology, and quality control to match it.
State of the art quality control warrants excellent quality, as discussed in our article on the production of high quality peptides.
Examples of references of customers using our custom phosphorylated peptides include;
M.-J.Boucher, L. Selander, L. Carlsson & H. Edlund. 2006.
Phosphorylation Marks IPF1/PDX1 Protein for Degradation by Glycogen Synthase Kinase 3-dependent Mechanisms.
The Journal of Biological Chemistry, 2006:281, 6395-6403.
T. Steinfeldt, S. Könen-Waisman, L. Tong, N. Pawlowski, T. Lamkemeyer, L. D. Sibley, J. P. Hunn & J. C. Howard. 2010.
Phosphorylation of Mouse Immunity-Related GTPase (IRG) Resistance Proteins Is an Evasion Strategy for Virulent Toxoplasma gondii.
PLoS Biol 8(12): e1000576. doi:10.1371/journal.pbio.1000576
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