Cell signalling is a highly regulated process that involves the transmission of information within and between cells, coordinating various physiological responses. Post-translational modifications, such as phosphorylation, play a critical role in cell signalling by modulating protein activity and mediating signal transduction. Tyrosine phosphatases are key enzymes responsible for removing phosphate groups from phosphorylated tyrosine residues, thereby regulating protein function, and terminating or modulating cell signalling events. They catalyse the dephosphorylation of tyrosine residues within target proteins and act as key regulators in cellular signalling pathways, balancing the actions of tyrosine kinases. A key feature of tyrosine phosphatases is their specificity for phosphotyrosine residues. Like kinases, phosphatases recognize specific amino acid sequences surrounding the phosphorylated residues, known as phosphatase recognition motifs. These motifs dictate the substrate specificity of phosphatases, allowing them to selectively dephosphorylate target proteins or sites within a protein. The recognition motifs for tyrosine phosphatases are characterized by conserved amino acid sequences surrounding the phosphorylated tyrosine residue, with the two best-known motifs being the "pTyr" motif (pTyr-X-X-hydrophobic, where "X" represents any amino acid residue, and the hydrophobic residue is often a phenylalanine (F) or leucine (L)), and the "pYxxP" motif, characterized by a phosphorylated tyrosine followed by two amino acids, usually small and uncharged, and then a proline residue. Tyrosine phosphatases play critical roles in numerous cell signalling pathways, ensuring the fine-tuned regulation of cellular responses. Some examples of their key roles in cell signalling include: 1) Protein Tyrosine Phosphatases (PTPs). PTPs comprise a large family of enzymes that specifically dephosphorylate tyrosine residues. The human genome contains 107 PTPs that regulate various cellular processes, including cell growth, differentiation, and survival. For example, the SH2 domain containing PTPs, such as SHP1 and SHP2, are involved in immune cell signalling and are crucial for the regulation of immune responses. SHP2 acts downstream of numerous receptors, dephosphorylating specific tyrosine residues to modulate signalling cascades; 2) Receptor Protein Tyrosine Phosphatases (RPTPs). RPTPs are transmembrane proteins that function as both cell adhesion molecules and tyrosine phosphatases. They play important roles in development, axon guidance, and neural plasticity. For instance, RPTPs like PTPδ and PTPσ are involved in neuronal development and synapse formation. Their phosphatase activity regulates receptor signalling events and influences cellular interactions; 3) Dual-Specificity Phosphatases (DSPs): DSPs are a group of phosphatases that can dephosphorylate both tyrosine and serine/threonine residues. They play critical roles in the regulation of mitogen-activated protein kinase (MAPK) pathways. DSPs, such as MKP1 and MKP3, specifically dephosphorylate and inactivate MAPKs, allowing for the termination of signalling and control of cellular responses; 4) Src Homology 2 (SH2) Domain-Containing Tyrosine Phosphatase 2 (SHP2). SHP2 is a non-receptor tyrosine phosphatase that acts as a positive regulator in various signalling pathways. It functions downstream of RTKs and cytokine receptors and is involved in cellular responses to growth factors, cytokines, and hormones. SHP2 dephosphorylates specific tyrosine residues on target proteins, influencing downstream signalling events. We offer a comprehensive product catalogue of research tools for studying tyrosine phosphatases, including CD45 antibodies, CD45RB antibodies, SHP2 antibodies, IGFBP3 antibodies, and IGFBP3 ELISA Kits. Explore our full tyrosine phosphatases product range below and discover more, for less.