Recombinant Human UGT2B7 protein

UGT2B7 is a member of the uridine diphosphate (UDP)-glucuronosyltransferase (UGT) enzyme family, which plays a critical role in phase II drug metabolism and the elimination of endogenous and exogenous compounds. Located primarily in the liver, kidneys, and gastrointestinal tract, UGT2B7 catalyzes the glucuronidation reaction, conjugating glucuronic acid from UDP-glucuronic acid to lipophilic substrates. This process enhances the water solubility of target molecules, facilitating their excretion via bile or urine. UGT2B7 exhibits broad substrate specificity, metabolizing drugs (e.g., morphine, epirubicin, zidovudine), steroids (e.g., estradiol, androsterone), and bile acids. Notably, it is responsible for the bioactivation of morphine-6-glucuronide, a potent analgesic metabolite.

Recombinant UGT2B7 protein is engineered using heterologous expression systems (e.g., insect cells, mammalian cells, or bacteria) to study its enzymatic activity, substrate preferences, and interactions with inhibitors or inducers. This tool enables researchers to dissect UGT2B7’s role in drug metabolism without interference from other enzymes or cellular components. Genetic polymorphisms in UGT2B7. such as the common His268Tyr variant, influence enzymatic efficiency and contribute to interindividual variability in drug responses, toxicity risks, and disease susceptibility (e.g., cancer, endocrine disorders). Recombinant UGT2B7 is also used in high-throughput screening for drug development, toxicology assessments, and personalized medicine strategies to predict patient-specific metabolic profiles. Its study provides insights into detoxification pathways, drug-drug interactions, and the mechanistic basis of diseases linked to impaired glucuronidation.