Cat: IPD-X40429

Recombinant Human UNC119 Protein ,His & SUMO

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Analytical Data

  • Gene name

    UNC119

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    Retinal protein 4 Short name: hRG4

  • Species

    Human

  • Source

    E. coli

  • Tag

    N- His-SUMO

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q13432

  • Expression Region

    1-240aa

  • Molecular Weight

    43 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

UNC119 is a pivotal protein known for its role in the regulation of G protein signaling and cellular processes. Originally identified in *Caenorhabditis elegans*, UNC119 is recognized for its involvement in the trafficking and localization of myristoylated proteins, highlighting its significance in cellular signaling pathways. The protein functions as a chaperone that binds to myristoylated G proteins, preventing their aggregation and ensuring proper cellular localization. This has profound implications in various physiological processes, including sensory perception, cell migration, and signal transduction. Recent studies focus on the structural and functional aspects of UNC119, emphasizing its potential as a therapeutic target for diseases associated with dysregulated G protein signaling, such as cancer and neurological disorders. Researchers are increasingly interested in generating recombinant UNC119 protein for crystallography and biophysical analyses, providing insights into its interaction mechanisms. Understanding UNC119's structure-function relationship could pave the way for innovative drug designs that modulate its activity, thereby influencing G protein signaling pathways in targeted therapies. As the demand for detailed mechanistic studies grows, the exploration of UNC119 through recombinant protein technology is a promising frontier in cell biology and pharmacology.

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