Cell signalling is a highly regulated process that involves the transmission of information within cells, coordinating various physiological responses. Post-translational modifications, such as phosphorylation, play a critical role in cell signalling, allowing for the dynamic regulation of protein activity. Serine and threonine phosphatases are key enzymes responsible for removing these phosphate groups from phosphorylated serine and threonine residues, respectively. They play many crucial roles in reversing and thereby modulating the phosphorylation events mediated by serine/threonine kinases, ensuring signal dampening or termination, and thereby maintaining signalling homeostasis. These phosphatases typically possess a conserved catalytic domain responsible for dephosphorylating the target residues. One of the key features of serine and threonine phosphatases is their substrate specificity. Like protein 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. Serine and threonine phosphatases play critical roles in numerous cell signalling pathways, ensuring regulation of cellular responses. Some important examples of their roles in cell signalling include: 1) the MAPK (Mitogen-Activated Protein Kinase) pathway where serine/threonine phosphatases, such as protein phosphatase 1 (PP1) and protein phosphatase 2A (PP2A), act as negative regulators of the MAPK pathway by dephosphorylating key components of the pathway. For instance, PP2A dephosphorylates and inactivates MAPKs (ERKs, JNKs, and p38), thus terminating downstream signalling; 2) Protein Phosphatase 2B (PP2B)/Calcineurin, a serine/threonine phosphatase that plays a critical role in calcium signalling. It is involved in regulating various cellular processes, including T-cell activation, neuronal function, and cardiac muscle contraction. Calcineurin dephosphorylates downstream targets, such as the transcription factor NFAT (Nuclear Factor of Activated T-cells), allowing its translocation to the nucleus and subsequent regulation of gene expression; 3) Protein Phosphatase 2C (PP2C), a family of serine/threonine phosphatases that play important roles in stress signalling and cell cycle regulation. In the stress-activated p38 MAPK pathway, PP2C dephosphorylates and inactivates p38 MAPK, terminating the stress response. PP2C also acts as a negative regulator of the cell cycle by dephosphorylating and inactivating CDKs (Cyclin-Dependent Kinases) and their associated cyclins, thereby preventing inappropriate cell cycle progression; 4) myosin phosphatase, a serine/threonine phosphatase involved in the regulation of smooth muscle contraction. It dephosphorylates the regulatory light chain of myosin, leading to relaxation of smooth muscle cells. We offer a large product catalogue of research tools for investigating serine and threonine phosphatases, including DUSP1 antibodies, NIPP1 antibodies, PPP2R5A antibodies, PPP2R1B antibodies, and DUSP3 antibodies. Explore our full serine and threonine phosphatases product range below and discover more, for less.