Cat: PA1000-3440

Recombinant Human VAMP8 Protein,His

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Analytical Data

  • Gene name

    VAMP8

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    VAMP8;Vesicle-associated membrane Protein 8

  • Species

    Human

  • Source

    E. coli

  • Tag

    His tag N-Terminus

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q9BV40

  • Expression Region

    1-100aa

  • AA Sequence

    MEEASEGGGNDRVRNLQSEVEGVKNIMTQNVERILARGENLEHLRNKTEDLEATSEHFKTTSQKVARKFWWKNVKMIVLICVIVFIIILFIVLFATGAFS

  • 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

VAMP8 (Vesicle-associated membrane protein 8) is a member of the SNARE (Soluble N-ethylmaleimide-sensitive factor attachment protein receptor) protein family, which plays a crucial role in intracellular membrane trafficking and exocytosis. Research on VAMP8 has gained significant attention due to its involvement in physiological processes such as insulin secretion and neurotransmitter release, as well as its potential implications in various pathologies, including diabetes and neurological disorders. VAMP8 facilitates the fusion of transport vesicles with target membranes, a key step in the delivery of cargo proteins and hormones. Studies have shown that VAMP8 interacts with other SNARE proteins, such as Syntaxin and SNAP-25, forming a complex that mediates membrane fusion events. Additionally, the regulation of VAMP8 activity is influenced by various post-translational modifications and interactions with regulatory proteins. Understanding the structure and function of VAMP8 is essential for elucidating its role in cellular communication and homeostasis. Researchers have focused on producing recombinant VAMP8 proteins to investigate their functional properties and interactions in vitro. These recombinant proteins are valuable for studying the molecular mechanisms of SNARE-mediated exocytosis and may provide insights into therapeutic strategies targeting dysregulated membrane trafficking observed in diseases. Overall, the study of VAMP8 and its recombinant forms is vital for advancing our knowledge in cell biology and can contribute to developing novel interventions for related disorders.

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