Cat: IPD-X37566

Recombinant Human UAP1 Protein (Yeast),His

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Analytical Data

  • Gene name

    UAP1

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    Antigen X ;AGX;Sperm-associated antigen 2;AGX-1;AGX-2

  • Species

    Human

  • Source

    Yeast

  • Tag

    N- His

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q16222

  • Expression Region

    1-522aa

  • Molecular Weight

    60.8 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.

Quality inspection process

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Protein Description

UAP1 (Ubiquitin-Activating Enzyme 1) is a critical enzyme involved in the ubiquitin-proteasome system, which plays a pivotal role in regulating protein degradation and turnover within the cell. The research surrounding UAP1 recombinant proteins has gained significant traction due to their potential implications in various biological processes, including cell cycle regulation, DNA repair, and signal transduction. Abnormalities in ubiquitination pathways have been linked to numerous diseases, including cancer, neurodegenerative disorders, and infections, highlighting the importance of understanding UAP1's functional mechanisms. By producing recombinant UAP1 proteins, researchers aim to elucidate the enzyme's structural properties and interaction dynamics with ubiquitin and other substrates. This can provide deeper insights into the regulatory functions of UAP1 and its role in disease pathology. Additionally, the availability of recombinant UAP1 facilitates the exploration of potential therapeutic interventions targeting the ubiquitin-proteasome system. As the field of proteomics continues to expand, the study of UAP1 and its recombinant variants is vital for advancing our comprehension of protein homeostasis and developing novel strategies for treating diseases linked to ubiquitin-related dysregulation.

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