Cat: IPD-X30509

Recombinant Mouse IDS/Iduronate 2-sulfatase Protein,His

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Analytical Data

  • Gene name

    IDS/Iduronate 2-sulfatase

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    MPS2; SIDS; Hunter Syndrome; Idursulfase; Alpha-L-iduronate sulfate sulfatase

  • Species

    Mouse

  • Source

    E. coli

  • Tag

    N-His

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q08890

  • Expression Region

    Leu180~Asp448

  • Molecular Weight

    34kDa

  • Endotoxin

    < 1.0 EU per μg protein as determined by the LAL method.

  • Form

    Freeze-dried powder

  • Buffer formulation

    PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.

  • Reconstitution

    Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.

  • Customization

    Site-directed mutagenesis Custom tag design Custom buffer formulation Custom full-length protein production

  • Stability Test

    The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.

  • Storage & Shelf Life

    Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

  • Shipping

    In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.

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Protein Description

Iduronate 2-sulfatase (IDS) is a critical enzyme involved in the degradation of glycosaminoglycans (GAGs), specifically heparan sulfate and dermatan sulfate. Deficiencies or mutations in the IDS gene lead to mucopolysaccharidosis type II (MPS II), a rare X-linked genetic disorder characterized by the accumulation of GAGs in various tissues, resulting in progressive physical and neurological symptoms. Research on recombinant IDS protein has gained significant attention due to its potential therapeutic application in enzyme replacement therapy (ERT) for MPS II patients. By producing active recombinant IDS, scientists aim to provide a consistent and effective treatment option to replace the deficient enzyme. Advances in recombinant protein technology have enabled the optimization of IDS expression and purification processes, enhancing enzyme stability and activity. Furthermore, studies have focused on the enzyme's structure-function relationship, elucidating the effects of specific mutations on its activity. Continued research into IDS not only enhances our understanding of MPS II pathogenesis but also improves the development of innovative therapies for lysosomal storage disorders.

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