Analysis of Tissue-Specific Phosphorylation Sites

Analysis of Tissue-Specific Phosphorylation Sites

Home / Services / In Vivo Functional Characterization / Analysis of Tissue-Specific Phosphorylation / Analysis of Tissue-Specific Phosphorylation Sites

Analysis of Tissue-Specific Phosphorylation Sites


Creative BioMart provides high-quality customized services and advanced techniques to help our customers analyze tissue-specific phosphorylation sites in both plants and animals. Our scientific team offers their skills, knowledge, and experience to help our customers advance their projects successfully.


Phosphorylation mediated by kinases through the addition of a covalently bound phosphate group is the most common and well-studied post-translational modification (PTM). Phosphorylation and dephosphorylation of proteins generate a complex picture of interconnected signaling pathways. Phosphorylation is increasingly being recognized to play a crucial role in almost every cellular activity, such as signaling cascades, metabolism, and development. Notably, some kinases exhibit tissue-specific preferences and this is not caused by tissue-specific kinase expression. Many metabolic pathways are also regulated differently by phosphorylation in different tissues. This suggests that phosphorylation may contribute to functional differences from different tissues.

Dysregulation of cellular signaling is a common hallmark of diseases, and many phosphorylation pathways have been shown to be involved in the pathogenesis of multiple diseases. This makes the discovery of tissue-specific phosphorylation sites and delineation of tissue phosphoproteomes a critical step in uncovering potential mechanisms and designing targeted drugs. Although many phosphorylation sites have been identified in recent years, the comprehensive analysis of tissue-specific phosphorylation sites still remains a challenge.

Tissue distribution and amino-acid sequence features of localized phosphorylation sites.

Figure 1. Tissue distribution and amino-acid sequence features of localized phosphorylation sites. (Lundby A, et al., 2012)

Service Offering

Creative BioMart offers comprehensive analysis of tissue-specific phosphorylation sites to enable the analysis of molecular mechanisms behind phosphorylation. We can handle different tissue sample collection formats. Our scientists are dedicated to providing our customers with end-to-end services to help them save time and effort.

  • Sequence-Based Analysis

    The sequence environments surrounding the phosphorylation sites may vary in different tissues. We have developed a sequence-based method for prediction and analysis of serine, threonine, and tyrosine phosphorylation site in proteins. In silico tools are involved to assist in the identification of enriched sequence motifs that are exclusively tissue-specific.

  • Structure-Based Analysis

    The spatial environment of phosphorylation sites has been found to have tissue-specific trends. We apply advanced techniques to collect 3D structures of phosphorylated proteins. Several databases and computational methods contribute to the prediction of general and kinase-specific phosphorylation sites.

Creative BioMart is an advanced biotech company within the field of kinase/phosphatase biology. We offer our expertise in establishing assays to analyze tissue-specific phosphorylation. The extensive experience of our scientific team translates into the robust wealth of knowledge that we use to provide you with the highest quality of service. If you are interested in any of our services or have additional questions, please do not hesitate to contact us.


  • Lundby A, et al. Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues. Nature communications, 2012, 3(1): 1-10.
  • Bak S, et al. Tissue specific phosphorylation of mitochondrial proteins isolated from rat liver, heart muscle, and skeletal muscle. Journal of proteome research, 2013, 12(10): 4327-4339.
For research use only. Not intended for any clinical use.