Protein phosphorylation is a crucial regulatory post-translational modification that plays critical roles in various cellular processes, including signal transduction, cell cycle regulation, gene expression, and metabolism. It involves the addition of a phosphate group to specific amino acid residues, typically serine, threonine, or tyrosine, within a protein. Phosphorylation is tightly regulated by kinases and phosphatases, which add or remove phosphate groups, respectively. In the context of cancer, protein phosphorylation events can have significant implications. Dysregulation of phosphorylation signalling pathways is frequently observed in cancer cells, leading to aberrant cell growth, survival, migration, and invasion. Some well-known examples include: 1) Phosphorylation of oncogenes and tumour suppressors. Phosphorylation plays a role in activating oncogenes (genes promoting cancer development) or inactivating tumour suppressor genes. For example, phosphorylation of Ras can lead to its constitutive activation whilst phosphorylation of the tumour suppressor protein p53 at specific serine residues, such as Ser15, Ser20, and Ser46, can modulate its stability, transcriptional activity, and interaction with other proteins, impairing its function in cell cycle regulation and DNA repair; 2) Phosphorylation in signal transduction pathways. Phosphorylation is central to many signalling cascades involved in cancer development. For instance, the activation of receptor tyrosine kinases (RTKs), such as epidermal growth factor receptor (EGFR), triggers downstream signalling pathways through phosphorylation events. Dysregulation of these pathways, including the Ras/MAPK and PI3K/AKT pathways, is frequently observed in cancer; 3) Phosphorylation of cell cycle regulators. Protein phosphorylation events regulate the cell cycle, ensuring proper progression and coordination of cell division. Cyclin-dependent kinases (CDKs) phosphorylate target proteins, driving the transition between different cell cycle phases. Dysregulation of CDK activity and the associated phosphorylation events can lead to uncontrolled cell division; 4) Phosphorylation of epigenetic regulators. Phosphorylation can modulate the activity of proteins involved in epigenetic regulation, such as histone modifications and DNA methylation. Aberrant phosphorylation of histones or chromatin remodeling proteins can alter gene expression patterns, contributing to cancer development and progression; 5) Phosphorylation of transcription factors. STAT3 is a transcription factor involved in regulating cell survival, proliferation, and immune responses. In many cancers, STAT3 is constitutively phosphorylated at Tyr705 by various kinases, including Janus kinases (JAKs) and Src family kinases. Phosphorylated STAT3 translocates to the nucleus, where it promotes the transcription of genes involved in cell cycle progression and anti-apoptotic pathways. Protein kinases and their phosphorylation events have become attractive targets for cancer therapies. Inhibitors of specific kinases, such as tyrosine kinase inhibitors (TKIs), have shown success in targeting aberrant signalling pathways in various cancers. Targeting specific phosphorylation events or pathways can help restore normal cellular processes and inhibit cancer growth. We offer a comprehensive product range of research reagents for investigating protein phosphorylation, including EGFR antibodies, FAK antibodies, c-Kit antibodies, EGFR ELISA Kits, and FAK ELISA Kits. Explore our full protein phosphorylation product range below and discover more, for less. Alternatively, you can explore our Tyrosine Kinases and Serine & Threonine Kinases product ranges.