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Phosphorylation of proteins is one of the key post-translational modifications (PTMs) that affect the biological functions of proteins, cells, organs, living organisms, etc. Creative BioMart's extensive experience in post-translational modification of proteins based on computational and experimental methods enables us to provide protein phosphorylation service to accelerate your projects.
Protein phosphorylation is the most common and well-studied modification method in organisms, in which amino acid residues are phosphorylated by protein kinases by adding covalently bound phosphate groups. Phosphorylation occurs on serine, threonine, and tyrosine residues and functions to modulate protein function, enzymatic activity, protein-protein interactions, and protein localization. It is now known that more than 80% of the different proteins (over 17,000) encoded by genes are protein phosphorylated, the vast majority of which are phosphorylated at multiple sites per protein. Because of its reversibility, phosphorylation provides a fast, flexible, and sometimes transient signal that cells use to rapidly transmit information and respond to stimuli. Studies have shown that the phosphorylation of tyrosine kinase receptors plays a key role in the induction and growth of cancer cells, and various small-molecule inhibitors and monoclonal antibodies targeting different tyrosine kinase receptors have also been developed as first-line drugs for the treatment of cancer.
Fig 1. Reversible Protein Phosphorylation Is a Molecular Switch Mechanism. (Humphrey S J, et al., 2015)
Phosphorylation of proteins is a dynamic, reversible event that depends on the activities of kinases and phosphatases. However, kinase biology is extremely complex. In addition, many proteins are phosphorylated at multiple sites, and kinase recognition sites may overlap, resulting in diverse and complex patterns of protein phosphorylation. To address these challenges, Creative BioMart has successfully employed a variety of techniques to reliably study protein phosphorylation to fully understand the phosphorylation status of proteins. In addition, we utilized a consensus site-based computer program to predict potential phosphorylation sites in other proteins. Our phosphorylation modification of proteins service supports the following studies:
(1) Phosphorylation at the interface regulates protein-protein binding
(2) Orthosteric and allosteric effects of phosphorylation on protein structure and protein-protein binding
(3) Disorder and order-disorder coupling transition after phosphorylation
(4) Cooperativity and crosstalk between multiple phosphorylation sites or other PTMs.
We employ the following in vivo and in vitro methods for assessing protein phosphorylation status, assessing phosphorylation of specific amino acids, and determining whether specific kinases (or phosphatases) modify proteins of interest.
Our mission is to provide global customers with the most comprehensive and professional customized protein phosphorylation service. If you have any special requirements about our services, please feel free to contact us. We are looking forward to working together with your attractive projects.
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