Recombinant Human SULT1A3 Protein，His & SUMO

SULT1A3, a member of the sulfotransferase enzyme family, plays a critical role in the metabolism of various endogenous and exogenous compounds by catalyzing the sulfonation process. This enzymatic activity is crucial for the detoxification and elimination of drugs, hormones, and environmental toxins, which underscores the importance of SULT1A3 in pharmacology and toxicology. Research has shown that variations in SULT1A3 can influence drug response and susceptibility to certain diseases, including cancer, due to altered metabolic pathways. Additionally, SULT1A3 is involved in the biotransformation of catecholamines and estrogens, pointing to its potential implications in neurodegenerative diseases and hormonal disorders. Given its diverse substrate specificity and biological relevance, the recombinant expression of SULT1A3 is essential for characterizing its enzymatic properties, identifying substrates, and studying drug interactions. By producing a recombinant form of this enzyme, researchers aim to elucidate its structure-function relationship, assess its kinetic parameters, and explore its role in drug metabolism. This knowledge is vital for the development of safer therapeutic agents and personalized medicine approaches, as it can lead to better predictions of drug efficacy and toxicity in different populations. Overall, the study of SULT1A3 recombinant protein is a key area of research that bridges biochemistry, pharmacology, and clinical applications, contributing to our understanding of metabolic processes and their implications for human health.