UGT2B17 Protein, Human (Cell-Free, His)

The UGT2B17 protein is a key UDP-glucuronosyltransferase (UGT) that directs phase II biotransformation by conjugating lipophilic substrates with glucuronic acid. This process enhances water solubility and promotes excretion of metabolites into urine or bile. UGT2B17 Protein, Human (Cell-Free, His) is the recombinant human-derived UGT2B17 protein, expressed by E. coli Cell-free , with N-10*His labeled tag. The total length of UGT2B17 Protein, Human (Cell-Free, His) is 507 a.a., with molecular weight of 64.5 kDa.

UGT2B17, a key player in phase II biotransformation, orchestrates the conjugation of lipophilic substrates with glucuronic acid, a crucial process that enhances water solubility and facilitates the excretion of metabolites into urine or bile. This versatile UDP-glucuronosyltransferase (UGT) exhibits a specific affinity for endogenous steroid hormones, including androgens such as epitestosterone and androsterone, as well as estrogens like estradiol and epiestradiol. Through its catalytic prowess, UGT2B17 actively contributes to the glucuronidation of these steroid hormones, shaping their bioavailability and aiding in the detoxification and elimination of these compounds from the body. The enzymatic activity of UGT2B17 underscores its essential role in maintaining the delicate balance of steroid homeostasis and metabolic processes.

Human

E. coli Cell-free

N-10*His

O75795 (G24-D530)

7367

GKVLVWPTEYSHWINMKTILEELVQRGHEVIVLTSSASILVNASKSSAIKLEVYPTSLTKNDLEDFFMKMFDRWTYSISKNTFWSYFSQLQELCWEYSDYNIKLCEDAVLNKKLMRKLQESKFDVLLADAVNPCGELLAELLNIPFLYSLRFSVGYTVEKNGGGFLFPPSYVPVVMSELSDQMIFMERIKNMIYMLYFDFWFQAYDLKKWDQFYSEVLGRPTTLFETMGKAEMWLIRTYWDFEFPRPFLPNVDFVGGLHCKPAKPLPKEMEEFVQSSGENGIVVFSLGSMISNMSEESANMIASALAQIPQKVLWRFDGKKPNTLGSNTRLYKWLPQNDLLGHPKTKAFITHGGTNGIYEAIYHGIPMVGIPLFADQHDNIAHMKAKGAALSVDIRTMSSRDLLNALKSVINDPIYKENIMKLSRIHHDQPVKPLDRAVFWIEFVMRHKGAKHLRVAAHNLTWIQYHSLDVIAFLLACVATMIFMITKCCLFCFRKLAKTGKKKKRD

64.5 kDa

Greater than 90% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.