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ASPC™

Recombinant Arylsulfatase

Liquid recombinant Arylsulfatase enzyme.
Stable for 12 months at 2-8°C.

This product is available on demand.
The lead time for delivery is 2 months. 

 

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Product Overview

Specifically designed for selective deconjugation of sulfo-conjugates while leaving 𝛃-glucuronide conjugates intact.

AVAILABLE PRESENTATIONS

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  • Information
  • Specifications
  • Information

    ASPC™ is a recombinant arylsulfatase enzyme that efficiently deconjugates a wide range of sulfated moieties. Unlike most commercially available enzymes, which include glucuronidase enzymes, ASPC™ is a pure sulfatase that enables the hydrolysis of sulfates alone, with no other types of conjugations. 

    Conjugation of xenobiotics represents an important biotransformation reaction in humans and animals. Hydrolysis of sulfo-conjugates is particularly relevant in steroid analysis, given that many steroids are converted into a mix of conjugates.

    Because of its purity, ASPC™ avoids both conversions and the generation of interfering peaks typically produced by wild-type enzymes. Unlike wild-type versions, recombinant arylsulfatase can reach pure arylsulfatase activity. It is also significantly more stable, something that is difficult to achieve in wild-type enzymes.

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  • Specifications

    Product Form: Solution, 10% (v/v) glycerol

    Temperature Range: 50 – 55°C

    Optimum Temperature: 52°C

    pH Range: 6.8 - 7.0

    Optimum pH: 6.9 

    Sulfatase activity: ≥ 250,000 Units/ml

    Storage/Stability: Store at 2 – 8°C for up to 12
    months.

    Activity Unit definition: One sulfatase unit
    will hydrolyze 1.0 nmole of p-nitrocatechol
    sulfate at pH 7.0 and 45°C per hour.

    CAS No. 9001-45-0

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Resources

Technical Data Sheets

Technical DataSheet ASPC

Publications & Posters
  • Immobilized Enzymes on Magnetic Beads for Separate Mass Spectrometric Investigation of Human Phase II Metabolite Classes
  • Advanced Metabolomics Analysis Through Chemical Biology Tools for the Selective Investigation of Gut Microbiota-Derived Metabolites 
  • Comparison of two aryl sulfatases for targeted mass spectrometric analysis of microbiota-derived metabolites
  • Comparative dietary sulfated metabolome analysis reveals unknown metabolic interactions of the gut microbiome and the human host
  • Development and characterization of an enzyme formulation for sulfatase and glucuronidase hydrolysis in a single-step
  • Unique Chemical biology tools for advanced metabolomics analysis - exploring gut microbiota metabolism by Daniel Globisch
  • Enzymatic and mass spectrometric methodology for the selective investigation of gut microbiota-derived metabolites by Ioanna Tsiara
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