GUSB polyclonal antibody

The enzyme β-glucuronidase catalyzes the conversion of β-D-glucuronoside and water to an alcohol and D-glucuronate. Deficiency of β-glucuronidase is the cause of the human lysosomal storage disorder mucopolysaccharidosis type VII (MPS VII). Specifically, two residues appear important for catalytic activity: Glu 451 and Glu 540. Mutations at these sites affect the overall structure of the protein, which normally consists of a homotetramer with each promoter including a jelly roll barrel, an immunoglobulin constant domain and a TIM barrel. Regulation of β-glucuronidase activity may play a role in tumorigenesis and the invasiveness of a number of cancers, and is also an important factor in the development of functional prodrugs that require the cleavage of an active cytostatic by endogenous enzymes for antitumor activity.