β-Glucuronidase (GUS)

GUS hydrolyzes β-glucuronide bonds in a range of glucuronide conjugates. This recombinant product is expressed in Pichia pastoris and purified for analytical and bioanalytical use.

It cleaves β-glucuronide bonds, releasing free compounds from glucuronide conjugates. This can prepare conjugated analytes for subsequent detection.

GUS occurs in microorganisms, animals and other systems. This product uses recombinant Pichia expression followed by fermentation and purification rather than direct extraction.

Recombinant expression and purification support a standardized process, a defined source and consistent production of high-purity enzyme.

Recombinant GUS is produced through engineered expression; naturally sourced GUS is isolated from tissue or microorganisms. Recombinant production can reduce raw-material variability and aid purity and batch control.

The product material states purity of ≥99% after purification. This helps reduce interference from unrelated proteins and supports assay stability.

The product highlights activity, stability, purity and batch consistency. Pichia expression and purification are intended to support analytical and related biological applications.

It hydrolyzes β-glucuronide bonds in suitable substrates. The resulting reaction can be linked to qualitative or quantitative signals in an assay.

It turns conjugated analytes into free forms by enzymatic hydrolysis, aiding later analysis. Select substrate and detection method for the target compound.

Yes, depending on the assay. GUS acts on glucuronides and arylsulfatase on sulfate esters; a combined system may process both conjugate types if conditions are optimized.

Complex biological samples can contain both glucuronide and sulfate conjugates. The two enzymes address different linkages and can broaden hydrolysis coverage in sample preparation.

High purity limits interference from host proteins and other impurities, helping analytical assays, enzymology studies and prodrug-activation research produce clearer, more stable results.

Standardized Pichia expression and purification can reduce variation from natural source materials. The product positioning emphasizes stability and batch control for standardized assays.

It may be coupled to colorimetric or other signal systems. Standardizing enzyme dose, substrate concentration and reaction conditions can improve consistency when processing many samples.

Use a suitable β-glucuronide substrate and monitor the detectable hydrolysis product. Define activity conditions for the chosen substrate, buffer, temperature and detection method.

Optimum pH, temperature and substrate conditions vary by enzyme source. Follow this product's instructions for recommended conditions and stable results.

Low-temperature storage limits degradation and activity loss. Shelf life is determined by the label and stability validation; avoid prolonged heat and repeated freeze–thaw cycles.

Store at −20°C and avoid repeated freeze–thaw cycles; short-term storage at 4°C may be used as instructed. Follow the actual label and instructions for shelf life.

Pichia expression and purification offer a defined source, high purity, stability and batch consistency as an alternative to naturally extracted enzyme.

Potential areas include forensic toxicology, clinical diagnostics, environmental and microbial testing, and prodrug-activation research, including urine-conjugate hydrolysis, doping analysis and related detection studies.