Recombinant Human HTR2B protein

The 5-hydroxytryptamine receptor 2B (HTR2B) is a G protein-coupled receptor (GPCR) that binds serotonin (5-HT), a neurotransmitter and hormone involved in regulating mood, cognition, and peripheral physiological processes. HTR2B is primarily expressed in the cardiovascular system, gastrointestinal tract, and central nervous system. It mediates cellular responses through Gq/11 protein signaling, leading to phospholipase C activation, intracellular calcium release, and downstream pathways influencing vascular contraction, cardiac function, and neural activity. Dysregulation of HTR2B has been implicated in conditions such as pulmonary hypertension, heart valve disease, and neuropsychiatric disorders.

Recombinant HTR2B protein is engineered in vitro using expression systems (e.g., mammalian, insect, or bacterial cells) to produce purified, functional receptor variants for research and drug development. Its recombinant form often includes tags (e.g., His-tag) for simplified purification and detection. Structural studies of HTR2B recombinant proteins have advanced understanding of ligand-binding mechanisms, receptor activation, and interactions with antagonists like ergot derivatives or selective serotonin reuptake inhibitors (SSRIs). This protein is critical for high-throughput screening of potential therapeutics targeting serotonin-related pathologies. Additionally, it aids in elucidating HTR2B's role in developmental biology, as studies suggest its involvement in embryonic heart formation. However, challenges persist in maintaining receptor stability and native conformation during recombinant production, necessitating optimized solubilization and membrane mimicry techniques. Current research leverages cryo-EM and X-ray crystallography to resolve HTR2B's 3D structure, facilitating precision drug design while minimizing off-target effects linked to serotonin receptor subtypes.