Cat: IPD-X38472

Recombinant Human PSPN Protein,His & GST

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Analytical Data

  • Gene name

    PSPN

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    PSP

  • Species

    Human

  • Source

    E. coli

  • Tag

    N- His & GST

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    O60542

  • Expression Region

    Val29~Gly156

  • Molecular Weight

    44kDa

  • 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

PSPN (Proteolipid Protein 1), a critical component of myelin in the central nervous system, has garnered significant interest in research due to its key role in the formation and maintenance of myelin sheaths. Myelin sheaths are essential for the proper functioning of neuronal communication, as they facilitate the rapid transmission of electrical impulses along axons. Disruptions in myelin integrity are implicated in various neurological disorders, including multiple sclerosis and leukodystrophies. Recent studies have focused on the biochemical and structural characterization of PSPN to better understand its functions and interactions within myelin. Advancements in techniques such as cryo-electron microscopy and X-ray crystallography have allowed researchers to elucidate the molecular organization of PSPN and its impact on myelin stability. Additionally, studies investigating the mutations in the PSPN gene have provided insights into how alterations in its expression and function may lead to demyelination and neurological deficits. Understanding the role of PSPN not only aids in comprehending myelination processes but also paves the way for potential therapeutic strategies aimed at repairing myelin damage and treating related diseases. As the field progresses, the ongoing exploration of PSPN could unveil novel pathways for intervention and enhance our understanding of myelin-associated disorders.

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