G protein-coupled receptors (GPCRs) are important molecular targets in drug discovery. These receptors play a pivotal role in physiological signaling pathways and are targeted by nearly 50% of currently available drugs. Mounting evidence suggests that GPCRs form dimers and various studies have shown that dimerization is necessary for receptor maturation, signaling and trafficking. However, the physiological implications of dimerization in vivo have not been well explored since detection of GPCR dimers in endogenous systems has been a challenging task. One exciting new approach to this challenge is the generation of antibodies against specific GPCR dimers. Such antibodies could be used as tools for characterization of heteromer-specific function, as reagents for their purification, tissue localization and regulation in vivo and as probes for mapping their functional domains. In addition, such antibodies could serve as alternative ligands for GPCR heteromers. Thus, heteromer-specific antibodies represent novel tools for the exploration and manipulation of GPCR dimer pharmacology.