Arylsulfatase

PaAst is an arylsulfatase that hydrolyzes aryl sulfate ester bonds. It can be used in assays and bioconversions involving sulfate-ester substrates. This recombinant product is expressed in Pichia pastoris and purified as a high-purity enzyme.

It hydrolyzes aryl sulfate esters, cleaving the sulfate-ester bond and releasing the corresponding products. This supports enzymatic analysis, detection and bioconversion.

They occur in microorganisms, plants and animals. Traditional products may be extracted from natural material, whereas PaAst is produced by recombinant Pichia fermentation and purification.

Fermentation followed by protein purification supports a stable recombinant production system and reduces dependence on naturally sourced material.

Recombinant PaAst is produced through genetic engineering and purified after expression; natural enzymes are extracted from tissues or microorganisms. Recombinant production makes the source clearer and can improve standardization and batch control.

The product material states purity of ≥99% after protein purification. High purity helps reduce interference from unrelated proteins in assays and downstream applications.

The listed advantages are stability, purity, batch consistency, a recombinant alternative to natural sources and broad compatibility. Standardized expression and purification support assay and industrial uses.

It does not require direct extraction from natural tissue. A controlled expression and purification process can provide an enzyme of defined source and high purity as a recombinant alternative.

Depending on the substrate and method, it may be developed for aryl-sulfate assays in clinical testing, forensic toxicology, agricultural assessment and environmental testing.

After recombinant expression, standardized protein purification removes host proteins and other impurities. Protein analysis shown on the product page indicates high purity.

It reduces effects of host proteins and impurities on enzyme activity, substrate reactions and analysis, particularly where low assay background and batch consistency matter.

Recombinant expression and standardized purification can reduce variation associated with natural raw materials. Consult the actual batch test report for batch-specific figures.

The product recommends storage at −20°C and avoiding repeated freeze–thaw cycles. For short-term use, follow the instructions for low-temperature storage.

Low temperature reduces protein degradation and activity loss. Follow specified long-term storage conditions and minimize freeze–thaw cycles.

Freezing and thawing may cause changes in local concentration, aggregation or protein conformation, affecting activity and stability. Aliquot according to expected use.

Yes, if the application requires it. Design a multi-enzyme system around substrate specificity, preferred conditions and stability; optimize blending ratios for the target workflow.

Its high purity and clearly defined recombinant source make it a potential tool enzyme for substrate hydrolysis, signal generation and assay-method development involving aryl sulfates.

Pichia expression and purification provide a defined source, high purity, potential batch consistency and a more standardized process compared with extraction from natural material.

Possible development areas include clinical diagnostics, forensic toxicology, agricultural assessment and environmental work: for example related disease screening, hydrolysis of urine conjugates, doping analysis, soil sulfur-cycle studies, agar desulfation and pollutant degradation.