The human cytosolic sulfotransfases (hSULTs) comprise a family of 12 phase II enzymes involved in the metabolism of drugs and hormones, the bioactivation of carcinogens, and the detoxification of xenobiotics. Knowledge of the structural and mechanistic basis of substrate specificity and activity is crucial for understanding steroid and hormone metabolism, drug sensitivity, pharmacogenomics, and response to environmental toxins. The family-wide analysis of the screening and structural data provides a comprehensive, high-level view of the determinants of substrate binding, the mechanisms of inhibition by substrates and environmental toxins, and the functions of the orphan family members SULT1C3 and SULT4A1. Evidence is provided for structural "priming" of the enzyme active site by cofactor binding, which influences the spectrum of small molecules that can bind to each enzyme.
Organism species: Homo sapiens (Human)
CATALOG NO. | PRODUCT NAME | APPLICATIONS | |
Proteins | n/a | Recombinant Sulfotransferase Family 1C, Member 3 (SULT1C3) | Recombinant Protein Customized Service Offer |
Antibodies | n/a | Monoclonal Antibody to Sulfotransferase Family 1C, Member 3 (SULT1C3) | Monoclonal Antibody Customized Service Offer |
n/a | Polyclonal Antibody to Sulfotransferase Family 1C, Member 3 (SULT1C3) | Polyclonal Antibody Customized Service Offer | |
Assay Kits | n/a | CLIA Kit for Sulfotransferase Family 1C, Member 3 (SULT1C3) | CLIA Kit Customized Service Offer |
n/a | ELISA Kit for Sulfotransferase Family 1C, Member 3 (SULT1C3) | ELISA Kit Customized Service Offer |
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- "Crystal structure of human sulfotransferase 1C3 (SULT1C3) in complex with PAP."Submitted (FEB-2009) to the PDB data bank