Cat: IPD-X39064

Recombinant Human VAMP8 Protein,His & GST

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Analytical Data

  • Gene name

    VAMP8

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    EDB; VAMP5; endobrevin

  • Species

    Human

  • Source

    E. coli

  • Tag

    N- His & GST

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q9BV40

  • Expression Region

    Met1~Ser100

  • Molecular Weight

    43kDa

  • 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, or vesicle-associated membrane protein 8, is a member of the soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) family, which plays a crucial role in the process of membrane fusion, particularly in intracellular trafficking. Research on VAMP8 has gained attention due to its involvement in processes such as exocytosis and endocytosis, which are essential for neurotransmitter release, hormone secretion, and membrane recycling in various cell types. Abnormalities in VAMP8 function have been linked to several diseases, including cancer and neurodegenerative disorders, highlighting its potential as a therapeutic target. The recombinant expression of VAMP8 protein facilitates in-depth studies of its biochemical properties and interactions with other proteins, allowing researchers to elucidate its specific mechanisms in cellular processes. Furthermore, the understanding of VAMP8's role in the secretory pathway can provide insights into the development of novel strategies for manipulating cellular communication and improving therapeutic outcomes in diseases associated with dysregulated membrane trafficking. Thus, the study of VAMP8 recombinant protein is not only important for fundamental cell biology but also for potential translational implications in medicine.

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