The enzyme ∫-glucuronidase catalyzes the conversion of ∫-D-glucuronoside and water to an alcohol and D-glucuronate. Deficiency of ∫-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 ∫-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.
Key Feature
Clonality
Polyclonal
Isotype
IgG
Host Species
Rabbit
Tested Applications
WBIPIFELISA
recommended for detection of &beta-glucuronidase of mouse, rat and human origin by WB, IP, IF and ELISA
Species Reactivity
HumanMouseRat
Concentration
1mg/ml
Purification
Affinity purified
Target Information
Alternative Names
epitope corresponding to amino acids 352-651 mapping at the C-terminus of &beta -glucuronidase of human origin
Tissue Specificity
epitope corresponding to amino acids 352-651 mapping at the C-terminus of β-glucuronidase of human origin