Cat: IPD-X25647

Recombinant Human Niemann Pick C1/NPC1 Protein (Yeast),His & Myc

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Analytical Data

  • Gene name

    Niemann Pick C1/NPC1

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    Niemann-Pick C1 protein

  • Species

    Human

  • Source

    Yeast

  • Tag

    C- His-Myc

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    O15118

  • Expression Region

    23-261aa

  • Molecular Weight

    30.2 kDa

  • 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

Niemann-Pick disease type C1 (NPC1) is a inherited lysosomal lipid storage disorder characterized by the impaired intracellular transport of cholesterol and other lipids, leading to their accumulation in various tissues, particularly the brain and liver. Mutations in the NPC1 gene are responsible for the majority of NPC cases, and the NPC1 protein plays a crucial role in the mobilization of cholesterol from late endosomes and lysosomes to other cellular compartments. Research into NPC1 protein has garnered significant attention due to its implications in neurodegenerative diseases and the aging process. Understanding the structure and function of the NPC1 protein is vital for developing therapeutic strategies for NPC and related disorders. Recent studies utilizing recombinant NPC1 proteins have provided insights into the protein's conformational dynamics, lipid binding properties, and its interactions within the cellular environment. By characterizing recombinant NPC1, researchers aim to elucidate the molecular mechanisms underlying cholesterol trafficking and explore potential avenues for pharmacological intervention, thereby addressing the unmet medical need for effective treatments for NPC and helping mitigate the disease's impact on affected individuals and their families.

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