Sino Biological offers a wide selection of tools for research on sulfatases and sulfotransferases, including recombinant proteins, antibodies (rabbit mAbs, mouse mAbs, and rabbit pAbs), ELISA kits, and ORF cDNA clones.
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Sulfatases are enzymes that catalyze the hydrolysis of sulfate ester bonds from a wide variety of substrates, including steroids, carbohydrates and proteins. Comparison of the crystal structures of one bacterial and three human sulfatases showed that they have a highly similar three-dimensional structure in addition to a superimposable core region, which constitutes the catalytic site of the enzymes. Critical residues involved in generating and resolving the sulfatase-sulfate ester intermediate are conserved in most sulfatases, therefore supporting their common role to form similar active sites regardless of the different substrates that are hydrolyzed. Sulfatases play important roles in the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodelling sulfated glycosaminoglycans in the extracellular space. Several human inherited diseases are caused by the deficiency of individual sulfatases.
Sulfotransferases are transferase enzymes that catalyze the transfer of a sulfate group from a donor molecule to an acceptor group of numerous substrates. The most common sulfate donor is 3'-phosphoadenosine-5'-phosphosulfate (PAPS). This reaction, often referred to as sulfuryl transfer, sulfation, or sulfonation, is widely observed from bacteria to humans and plays a key role in various biological processes such as cell communication, growth and development, and defense. In humans three sulfotransferase families, SULT1, SULT2, and SULT4, have been identified that contain at least thirteen distinct members. Sulfatases and sulfotransferases form the major catalytic machinery for the synthesis and breakage of sulfate esters.