Peptide Modifications: Phosphorylation

Phosphorylation of Ser, Thr and Tyr is a reversible protein modification involved in regulating a myriad of cellular events including receptor signaling, protein association and compartmentalization, activation and inhibition of protein function, and cell survival.

Many hormones can adapt the activity of specific enzymes by increasing their phosphorylation state of Ser or Thr residues. Growth factors (like insulin) can trigger phosphorylation of Tyr. The phosphate groups on these amino acids can be quickly removed, thus Ser, Thr and Tyr function as molecular switches during regulation of cellular processes (e.g. cancer proliferation).

Synthetic peptides have played a useful role in studies of protein kinase substrates and interaction domains. Several factors have hindered or limited the applicability of various techniques for phosphorylated peptide synthesis, such as the inability of achieving full automation using solid phases, or the lack of convenient interfacing with standard analytical platforms. LifeTein's process for synthesis of peptides and phosphopeptides on PeptideSyn^TM platform overcomes previous limitations and demonstrates its scalability by increasing the synthesis efficiency. The PeptideSyn^TM platform is well suited to the study of protein kinase substrates, antigens, binding molecules, and inhibitors.

• We offer phosphorylation on pSer, pTyr, pThr or D-pSer, D-pTyr, D-pThr.
• Phosphorylation is available at two sites, three sites, four sites and five sites, for example, NDEpSpTDYEpSERQpTD.

Case Study: Solid-phase synthesis of a peptide with 4 phosphorylation sites.

A 14 amino acid peptide (molecular weight: 1981.53) with 4 phosphorylation sites at 95% purity was delivered in 3 weeks: xxxpSpTxxxpSxxxpTx

HPLC Results:

MS Results:

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