|Detection of Human beta ‑Glucuronidase/GUSB by Western Blot. Western blot shows lysates of HT‑29 human colon adenocarcinoma cell line. PVDF Membrane was probed with 1 µg/mL of Human beta ‑Glucuronidase/GUSB Antigen Affinity-purified Polyclonal Antibody (Catalog # AF6144) followed by HRP-conjugated Anti-Sheep IgG Secondary Antibody (Catalog # HAF016). A specific band was detected for beta ‑Glucuronidase/GUSB at approximately 82 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 8.|
Detection of Human beta ‑Glucuronidase/GUSB by Simple WesternTM. Simple Western lane view shows lysates of HT‑29 human colon adenocarcinoma cell line, loaded at 0.2 mg/mL. A specific band was detected for beta ‑Glucuronidase/GUSB at approximately 92 kDa (as indicated) using 10 µg/mL of Sheep Anti-Human beta ‑Glucuronidase/GUSB Antigen Affinity-purified Polyclonal Antibody (Catalog # AF6144) followed by 1:50 dilution of HRP-conjugated Anti-Sheep IgG Secondary Antibody (Catalog # HAF016). This experiment was conducted under reducing conditions and using the|
12-230 kDa separation system.
Human beta -Glucuronidase (EC 188.8.131.52) encoded by the GUSB gene is a lysosomal hydrolase involved in the stepwise degradation of glucuronic acid-containing glycosaminoglycans that include heparan sulfate, chondroitin sulfate and hyaluronan (1). The enzyme is only active on the glucuronic acid of the non-reducing end. The native protein has been reported as a tetrameric glycoprotein composed of identical subunits (1, 2). Mutations in the GUSB gene are linked to mucopolysaccharidosis type VII (3). Accumulation of partially degraded glycosaminoglycans, with glucuronic acid residues at the non-reducing termini, are usually found in the lysosomes of patients with the disease (3). It has also been reported that this enzyme may contribute to the depletion of chondroitin from cartilage and thereby facilitate the damage of joints in rheumatoid arthritis (4).
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