Transmembrane adaptor proteins (TRAPs) play vital roles in cellular signalling by acting as membrane intermediaries that connect cell surface receptors to various intracellular signalling molecules. These multifaceted proteins are trafficked to and embedded within the cell membrane and there serve as key regulators of signal transduction, cellular activation, immune responses, and other crucial cellular processes. TRAPs facilitate the physical coupling of cell surface receptors, such as immune receptors, cytokine receptors, and growth factor receptors, to downstream signalling molecules by associating with both receptors and intracellular signalling molecules. TRAPs thereby enable a more efficient transmission of extracellular signals across the cell membrane. For example, the transmembrane adaptor protein linker for activation of T cells (LAT) plays a pivotal role in T-cell receptor signalling by linking the receptor complex to downstream signalling pathways, leading to T-cell activation and immune responses. TRAPs also contribute to the organization and assembly of specialized membrane microdomains, such as lipid rafts and immunological synapses. These microdomains are thought to facilitate the concentration and segregation of signalling molecules, increasing the efficiency of signal transduction. The TRAPs LAT and phosphoprotein associated with glycosphingolipid-enriched microdomains (PAG) are involved in the formation and maintenance of these microdomains, thereby influencing cellular activation and immune cell responses. TRAPs also act to amplify or modulate signalling pathways by acting as scaffolds in recruitment of multiple signalling molecules. By bringing together various components of signalling cascades, TRAPs enhance the efficiency and specificity of signal propagation. For example, the transmembrane adaptor protein DNAX-activating protein of 12 kDa (DAP12) amplifies activating signals in immune cells by recruiting and activating downstream signalling molecules such as Syk (Spleen tyrosine kinase), a non-receptor protein tyrosine kinase, PLCγ (Phospholipase C gamma) and Vav family proteins, guanine nucleotide exchange factors (GEFs) that activate Rho family GTPases, ultimately regulating cellular activation and immune responses. Certain TRAPs also participate in the regulation of receptor internalization and recycling processes. They control the endocytic fate of receptors, influencing the duration and strength of signalling. Transmembrane adaptor protein CD3ζ, for instance, plays a role in controlling the internalization and recycling of the T-cell receptor complex, thus regulating T-cell activation, and signalling dynamics. Finally, transmembrane adaptor proteins also play significant roles in cell adhesion and migration processes. They are involved in the assembly of focal adhesions and regulate cytoskeletal dynamics, influencing cell motility and tissue morphogenesis. TRAPs like integrin-associated protein (CD47) and PAG contribute to the regulation of cell adhesion, migration, and tissue organization by interacting with integrins and cytoskeletal proteins. Similarly, ADAP (Adhesion and degranulation-promoting adaptor protein) plays a critical role in T cell adhesion and integrin activation. ADAP interacts with the cytoplasmic tail of integrin β chains and regulates their clustering and activation, facilitating T cell adhesion and immune synapse formation. We offer a large product range of research reagents for studying transmembrane adapters, including ICAM3 antibodies, LAT antibodies, NCR1 antibodies, TLR2 antibodies, and TLR2 ELISA Kits. Explore our full transmembrane adapters product range below and discover more, for less.