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Your Position: ホーム > Protein > beta-Glucuronidase/GUSB > BEB-H52H3

Human beta-Glucuronidase/GUSB Protein, His Tag (active enzyme)

  • Synonym
    BG, MPS7
  • Source
    Human beta-Glucuronidase Protein, His Tag(BEB-H52H3) is expressed from human 293 cells (HEK293). It contains AA Leu 23 - Thr 651 (Accession # P08236).
    Predicted N-terminus: Leu 23
  • Molecular Characterization
    beta-Glucuronidase/GUSB Structure

    This protein carries a polyhistidine tag at the C-terminus

    The protein has a calculated MW of 74.5 kDa. The protein migrates as 75-85 kDa under reducing (R) condition (SDS-PAGE) due to glycosylation.

  • Endotoxin
    Less than 1.0 EU per μg by the LAL method.
  • Purity

    >95% as determined by SDS-PAGE.

  • Formulation

    Lyophilized from 0.22 μm filtered solution in 50 mM Tris,150 mM NaCI,pH7.5 with trehalose as protectant.

    Contact us for customized product form or formulation.

  • Reconstitution

    Please see Certificate of Analysis for specific instructions.

    For best performance, we strongly recommend you to follow the reconstitution protocol provided in the CoA.

  • Storage

    For long term storage, the product should be stored at lyophilized state at -20°C or lower.

    Please avoid repeated freeze-thaw cycles.

    This product is stable after storage at:

    1. -20°C to -70°C for 12 months in lyophilized state;
    2. -70°C for 3 months under sterile conditions after reconstitution.
SDS-PAGE
beta-Glucuronidase/GUSB SDS-PAGE

Human beta-Glucuronidase Protein, His Tag on SDS-PAGE under reducing (R) condition. The gel was stained with Coomassie Blue. The purity of the protein is greater than 95%.

Bioactivity

Measured by its ability to hydrolyze 4-methylumbelliferyl-beta -D-glucuronide. The specific activity is >3500 pmol/min/μg(QC tested).

  • Background
    Human beta -Glucuronidase (EC 3.2.1.31) 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. 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.
  • Clinical and Translational Updates

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