Phosphorylation plays crucial roles in cell signalling by modulating protein activity and mediating signal propagation. Serine and threonine kinases are key enzymes that phosphorylate serine and threonine residues, respectively, and are involved in numerous cell signalling pathways. These kinases typically consist of a conserved catalytic domain responsible for transferring the phosphate group from ATP to the target residue of the substrate. One of the key features of serine and threonine kinases is their specificity for the target residues. They recognize specific amino acid sequences surrounding the serine or threonine residues to be phosphorylated, known as kinase recognition motifs. These motifs dictate the substrate specificity of kinases, enabling them to selectively phosphorylate specific target proteins or sites within a protein. Serine and threonine kinases are involved in a wide array of cellular processes, playing key roles in cell signalling. The human genome encodes over 500 serine/threonine kinases and they participate in signalling cascades initiated by a large variety of extracellular stimuli, including growth factors, hormones, and stress signals. Some key examples of pathways involving serine and threonine kinases include: 1) the MAPK (Mitogen-Activated Protein Kinase) pathway, which is a crucial signalling pathway involved in cell growth, proliferation, and differentiation. It consists of a series of phosphorylation events, primarily mediated by serine and threonine kinases. For example, the activation of extracellular signal-regulated kinases (ERKs) within the MAPK pathway requires the phosphorylation of both serine and threonine residues, leading to the regulation of gene expression and cellular responses; 2) the PI3K/Akt pathway, involved in regulating cell survival, growth, and metabolism. Serine/threonine kinases, such as phosphoinositide-dependent kinase 1 (PDK1) and mammalian target of rapamycin complex 2 (mTORC2), phosphorylate serine and threonine residues on Akt (also known as protein kinase B), a key effector protein in this pathway. Phosphorylation of Akt by these kinases leads to its activation and subsequent regulation of downstream targets involved in cell survival and metabolism; 3) cell cycle regulation, where serine and threonine kinases play crucial roles. Cyclin-dependent kinases (CDKs) are a group of serine/threonine kinases that work in conjunction with their regulatory subunits, cyclins, to control the progression of the cell cycle. Phosphorylation of specific target proteins by CDKs allows for the orderly transition between different phases of the cell cycle; 4) transforming growth factor-beta (TGF-β) signalling pathways, which are involved in diverse cellular processes, including cell growth, differentiation, and immune response regulation. Serine/threonine kinases, such as TGF-β receptor kinases, phosphorylate downstream signalling molecules, such as Smad proteins. Phosphorylation of Smads allows them to translocate to the nucleus and regulate gene expression, mediating the cellular response to TGF-β; 5) the Wnt/β-catenin pathway, essential for embryonic development, tissue homeostasis, and stem cell maintenance. Serine/threonine kinases, such as glycogen synthase kinase-3β (GSK-3β), phosphorylate β-catenin, a key effector protein in this pathway. Phosphorylation of β-catenin marks it for degradation, preventing its accumulation and subsequent activation of target genes. We provide a wide product catalogue of research reagents for studying serine and threonine kinases, including AKT1 antibodies, p38 antibodies, S6K1 antibodies, S6K1 ELISA Kits, and pan-AKT ELISA Kits. Explore our full serine and threonine kinases product range below and discover more, for less. Alternatively, you can explore our Other Kinases, MAPK Pathway, and PKC product ranges.