Cat: IPD-X25925

Recombinant Human NAPG Protein,His

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Analytical Data

  • Gene name

    NAPG

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    SNAPG; Gamma SNAP; N-ethylmaleimide-sensitive factor attachment protein gamma

  • Species

    Human

  • Source

    E. coli

  • Tag

    N-His

  • Purity

    Greater than 95% as determined by SDS-PAGE.

  • Uniprot

    Q99747

  • Expression Region

    Met1~Cys312

  • Molecular Weight

    41 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

The NAPG protein, known for its role in various cellular processes, has garnered significant attention in recent years due to its potential implications in both basic biology and therapeutic applications. Initially identified in the context of neuronal function, NAPG has been implicated in the regulation of synaptic vesicle trafficking and neurotransmitter release. This association highlights its importance in neurological disorders, particularly those related to synaptic dysfunction, such as Alzheimer’s disease and schizophrenia. As research progresses, the focus has shifted towards understanding the structural and functional properties of NAPG, enabling the development of recombinant forms of the protein. These recombinant proteins are being explored for their utility in elucidating the molecular mechanisms underlying NAPG's functions, as well as for their potential as innovative therapeutic agents. The ability to synthesize NAPG in vitro allows for detailed studies of its interactions with other cellular components and provides a platform for high-throughput screening of small molecules aimed at modulating its activity. Furthermore, advancements in protein engineering techniques are paving the way for the design of NAPG variants with enhanced stability and specificity, which could lead to novel interventions in disease models. As the landscape of NAPG research evolves, it promises to unveil critical insights into its biological significance and therapeutic potential, positioning it as a promising candidate for future drug development endeavors.

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