G protein signalling is a fundamental and highly conserved set of cellular pathways involved in transmitting extracellular signals to intracellular effectors. It is initiated by the activation of G protein-coupled receptors (GPCRs), one of the largest families of cell surface receptors. GPCRs span the cell membrane and upon binding to their specific ligands, such as neurotransmitters, hormones, or chemokines, undergo conformational changes that facilitate the activation of G proteins. G proteins are heterotrimeric protein complexes consisting of three subunits: α, β, and γ. The α subunit, when bound to guanosine triphosphate (GTP), is active and initiates downstream signalling events, whilst the βγ subunits act as a functional unit. The activation of G proteins can occur through two main mechanisms: GPCR-mediated exchange of GDP for GTP on the α subunit or the activation of certain guanine nucleotide exchange factors (GEFs). Upon activation of GPCRs, G proteins frequently activate adenylyl cyclase (AC), leading to the production of cyclic adenosine monophosphate (cAMP). cAMP serves as a second messenger that can regulate various cellular processes. For instance, in the context of hormone signalling, activation of GPCRs by adrenalin stimulates cAMP production, which subsequently activates protein kinase A (PKA) and influences downstream targets involved in glycogen metabolism, lipolysis, and gene expression. Activation of certain GPCRs also leads to the activation of phospholipase C (PLC), which cleaves phosphatidylinositol 4,5-bisphosphate (PIP2) into inositol trisphosphate (IP3) and diacylglycerol (DAG). IP3 induces the release of calcium from intracellular stores, while DAG activates protein kinase C (PKC). Together, IP3 and DAG regulate processes such as calcium signalling, cell growth, and neurotransmitter release. G proteins of the Rho family (small GTPases), including Rho, Rac, and Cdc42, are involved in regulating actin cytoskeleton dynamics and cell migration. GPCRs can activate these small G proteins, which subsequently activate downstream effectors such as Rho-associated protein kinases (ROCKs) and p21-activated kinases (PAKs). These pathways play crucial roles in diverse cellular processes, including cell adhesion, motility, and cell division. Beyond the canonical G protein-dependent signalling, GPCRs can also recruit β-arrestins upon activation. β-arrestins can not only dampen G protein signalling but also act as signalling scaffolds, initiating their own downstream signalling cascades. These β-arrestin-mediated pathways can therefore regulate processes such as receptor desensitization, internalization, and signalling independently of G protein activation. G protein signalling is therefore a ubiquitous and vital mechanism involved in numerous physiological processes. It regulates diverse cellular functions, including neurotransmission, hormone signalling, immune response, sensory perception, and cardiovascular function, with dysregulation of G protein signalling linked to various diseases, including cardiovascular disorders, neurodegenerative diseases, and cancer. We provide a wide product catalogue of research reagents for investigating G protein signaling, including ErbB 3 antibodies, CCR5 antibodies, TIMP1 antibodies, GRO alpha ELISA Kits, and ErbB 3 ELISA Kits. Explore our full G protein signaling product range below and discover more, for less. Alternatively, you can explore our GPCR, Small G Proteins, and Heterotrimeric G Proteins product ranges.