Post-translational modifications, such as tyrosine phosphorylation, play a crucial role in cell signalling by modulating protein activity and mediating signal transduction. Tyrosine kinases phosphorylate tyrosine residues within target proteins and are key players in many cell signalling cascades. Tyrosine kinases specifically phosphorylate tyrosine residues within target proteins and are divided into two categories: receptor tyrosine kinases (RTKs) and non-receptor tyrosine kinases. RTKs are transmembrane proteins that span the cell membrane and have an extracellular ligand-binding domain and an intracellular tyrosine kinase domain. Non-receptor tyrosine kinases, on the other hand, lack transmembrane domains and are typically found in the cytoplasm or indirectly associated with cell membranes. A key features of tyrosine kinases is their specificity for tyrosine residues. They recognize specific amino acid sequences surrounding the tyrosine residue to be phosphorylated, known as kinase recognition motifs. These recognition motifs dictate the substrate specificity of tyrosine kinases, enabling them to selectively phosphorylate specific target proteins or sites within a protein. Tyrosine kinases play crucial roles in cell signalling and are involved in a multitude of cell signalling pathways. Some examples of their key roles in cell signalling include: 1) Receptor Tyrosine Kinases (RTKs), involved in cell growth, differentiation, and survival by transmitting signals from extracellular ligands to the intracellular environment. Ligand binding to the extracellular domain of a RTK induces dimerization or oligomerization, bringing the kinase domains of the receptor in proximity to one another. This leads to trans-autophosphorylation of tyrosine residues within the kinase domain, activating the receptor and initiating downstream signalling cascades. Examples of RTKs include the Epidermal Growth Factor Receptor (EGFR), Insulin Receptor, and Platelet-Derived Growth Factor Receptor (PDGFR); 2) Src Family Kinases (SFKs). SFKs are non-receptor tyrosine kinases involved in regulating cell proliferation, differentiation, and migration. They are associated with various membrane receptors and act downstream of RTKs. SFKs can also be activated by integrins, which are cell adhesion molecules. Src, the prototypical member of the SFKs, phosphorylates tyrosine residues on a wide range of target proteins, influencing signalling pathways involved in cell growth, survival, and cytoskeletal dynamics; 3) Janus Kinases (JAKs), non-receptor tyrosine kinases that play a key role in cytokine signalling. They are associated with cell surface receptors, such as cytokine receptors, and are involved in transmitting signals from cytokines to the nucleus. Upon ligand binding, JAKs are activated and phosphorylate tyrosine residues on both the receptor and associated signal transducers, initiating downstream signalling pathways, including the STAT (Signal Transducers and Activators of Transcription) pathway; 3) BCR-ABL Fusion Protein. The BCR-ABL fusion protein is a constitutively active tyrosine kinase resulting from a chromosomal translocation found in certain leukaemias, such as chronic myeloid leukaemia (CML), with activation of the BCR-ABL kinase initiating signalling cascades that contribute to leukemic transformation. Tyrosine kinases are thus crucial players in cell signalling, phosphorylating specific tyrosine residues within target proteins. They are involved in various signalling pathways, including those mediated by RTKs, SFKs, JAKs, and Abl kinase, regulating cellular processes such as cell growth, differentiation, survival, and migration. We provide a comprehensive product catalogue of research reagents for investigating tyrosine kinases, including EGFR antibodies, ErbB 2 antibodies, FAK antibodies, EGFR ELISA Kits, and ErbB 2 ELISA Kits. Explore our full tyrosine kinases product range below and discover more, for less. Alternatively, you can explore our Receptor Tyrosine Kinases, Src Family, and FAK & PYK product ranges.