Approximately 30% of drugs target GPCRs, yet only a handful of studies have reported chemical probes to photoaffinity label these proteins in living cells. This is likely due to the very low expression levels of GPCRs. We present probe-TAMRA as a tool for investigating the fundamental biology of FPR1 and its viability as a drug target in inflammatory diseases. In the future we aim to apply probe-TAMRA to confirm the presence of FPR1 in endogenous settings, to visualise protein trafficking, and to understand the oligomerisation state of this receptor on the cell surface, as there is evidence that interconverting populations of large and small oligomers play a role in signal transduction. The photocrosslinking group incorporated into the probe also provides a means of determining the target selectivity of formylpeptides and probes; the off-target band that we observe on gel may be a feature of formyl-peptide based tools and warrants further exploration.