Cat: IPD-X32558

Recombinant Mouse Sialidase-2 Protein (P. pastoris),His

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Analytical Data

  • Gene name

    Sialidase-2

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    Neu2; Sialidase-2; EC 3.2.1.18; Cytosolic sialidase; Mouse skeletal muscle sialidase; MSS; Murine thymic sialidase; MTS; N-acetyl-alpha-neuraminidase 2

  • Species

    Mouse

  • Source

    P. pastoris

  • Tag

    N-10*His

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q9JMH3

  • Expression Region

    M1-Q379

  • Protein Length

    Full Length

  • 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

Sialidase-2, also known as neuraminidase 2, is an enzyme that plays a crucial role in sialic acid metabolism, which is essential for various biological processes, including cell signaling, immune response, and pathogen-host interactions. The significance of sialidase-2 has gained attention due to its involvement in several pathological conditions, including cancer progression, inflammation, and viral infections. Recent studies have indicated that aberrant regulation of sialidase-2 can lead to altered glycosylation patterns on cell surfaces, affecting cellular communication and immune evasion mechanisms. Researchers are increasingly focused on understanding the enzyme's structure, functionality, and regulatory mechanisms to elucidate its biological roles. Furthermore, the development of recombinant sialidase-2 presents promising avenues for therapeutic interventions. It could be leveraged in drug discovery, vaccine development, and as a potential biomarker for various diseases. This research is not only pivotal for expanding our knowledge of glycoprotein dynamics but also holds potential for clinical applications in targeting diseases linked to sialic acid dysregulation. Consequently, the exploration of recombinant sialidase-2 is at the forefront of molecular biology and biochemistry research, offering insights that could lead to innovative strategies for disease management and treatment.

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