Recombinant Mouse P2yr13 protein

P2Y13 receptor, a member of the P2Y purinergic receptor family, is a G protein-coupled receptor (GPCR) activated by extracellular nucleotides such as adenosine diphosphate (ADP). It plays critical roles in regulating cellular processes like platelet aggregation, neurotransmission, immune responses, and metabolic homeostasis. The P2Y13 receptor is encoded by the *P2RY13* gene in humans and is predominantly expressed in the brain, spleen, and hematopoietic tissues. Structurally, it features seven transmembrane domains, characteristic of GPCRs, with extracellular loops involved in ligand binding and intracellular regions mediating G protein coupling (typically Gαi/o, inhibiting cAMP production).

Recombinant P2Y13 protein refers to the engineered form of this receptor, produced using heterologous expression systems (e.g., mammalian cells, insect cells, or yeast) for functional and pharmacological studies. Its recombinant expression enables large-scale production, purification, and structural analysis, which are essential for drug discovery. Researchers often tag the protein (e.g., with His or FLAG tags) to facilitate purification via affinity chromatography. Challenges in producing functional P2Y13 include maintaining proper post-translational modifications (e.g., glycosylation) and conformational stability during purification.

Current studies focus on P2Y13's role in diseases such as atherosclerosis, neuroinflammation, and type 2 diabetes, making it a potential therapeutic target. Structural insights from recombinant P2Y13 have aided in designing selective agonists/antagonists. However, its signaling complexity, including interactions with arrestins and other secondary messengers, requires further exploration. Advances in cryo-EM and computational modeling are accelerating mechanistic studies, positioning recombinant P2Y13 as a key tool for unraveling nucleotide signaling pathways and developing precision therapies.