Phosphorylation is a post translational modification where a hydrogen atom in Serine, Threonine or Tyrosine is replaced by PO3H2.
Phosphorylation is the enzymatic process through which a phosphate group is added via an ester bond, generally by a kinase, to either a small molecule or a protein. Protein phosphorylation is important in regulating signal transduction systems, as it affects the activity of its target, for instance in turning an enzyme ‘on’ or ‘off’. 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.
For a large subset of proteins, phosphorylation is tightly associated with protein activity and is a key point of protein function regulation. Phosphorylation regulates protein function and cell signaling by causing conformational changes in the phosphorylated protein. These changes can affect the protein in two ways. First, conformational changes regulate the catalytic activity of the protein. Thus, a protein can be either activated or inactivated by phosphorylation. Second, phosphorylated proteins recruit neighboring proteins that have structurally conserved domains that recognize and bind to phosphomotifs. These domains show specificity for distinct amino acids. For example, Src homology 2 (SH2) and phosphotyrosine binding (PTB) domains show specificity for phosphotyrosine (pY), although distinctions in these two structures give each domain specificity for distinct phosphotyrosine motifs. Phosphoserine (pS) recognition domains include MH2 and the WW domain, while phosphothreonine (pT) is recognized by forkhead-associated (FHA) domains. The ability of phosphoproteins to recruit other proteins is critical for signal transduction, in which downstream effector proteins are recruited to phosphorylated signaling proteins. Protein phosphorylation is a reversible PTM that is mediated by kinases and phosphatases, which phosphorylate and dephosphorylate substrates, respectively. These two families of enzymes facilitate the dynamic nature of phosphorylated proteins in a cell. Indeed, the size of the phosphoproteome in a given cell is dependent upon the temporal and spatial balance of kinase and phosphatase concentrations in the cell and the catalytic efficiency of a particular phosphorylation site.
We provide peptides with high quality peptides modified with two, three, four, and five phosphorylation sites. With mature synthetic purification technology and an enterprising elite team, National Peptide has become a trusted peptide supply brand.
Success case : Four phosphorylation
MS analysis:
Each peptide is shipped with a Document of HPLC and MS data for free. Other test datas can also be provided according to customer demand . Peptides are packed with ice bag and desiccants during shipment and storage. After opening, we recommend peptides are stored dry in a freezer (details given in our technical guide to handling peptides; a copy is shipped with each peptide).

a.What is the minimum quantity for a peptide?

The minimun for one peptide should be 1mg, and there is no maximum quantity for a peptide at Bankpeptide.

b.Which kind of solvent should I use?

According to your needs, the peptides can often dissolved in water, DMF,DMSO, and PBS Buffer.

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Ham BM (2012) Proteomics of biological systems: Protein phosphorylation using mass spectrometry techniques. Hoboken (NJ): John Wiley & Sons.

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