Cat: IPD-X25286

Recombinant Mouse TRAP1 Protein,His & Myc

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Analytical Data

  • Gene name

    TRAP1

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Species

    Mouse

  • Source

    E. coli

  • Tag

    N- His & C- Myc

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P19473

  • Expression Region

    1-134aa

  • Molecular Weight

    23.1 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

TRAP1 (TNF receptor-associated protein 1) is a mitochondrial protein that has garnered significant attention in recent years due to its multifaceted role in cellular processes, particularly in cancer biology and stress response. Originally identified as a protein that associates with tumor necrosis factor receptors, TRAP1 has been found to have chaperone-like functions, protecting cells from stress-induced damage and regulating mitochondrial function. Its implication in oncogenesis has made it a focal point of research, as it is overexpressed in various cancers, contributing to tumor progression and resistance to therapy. Studies indicate that TRAP1 influences key pathways, such as apoptosis and the unfolded protein response, making it a potential target for therapeutic intervention. The recombinant expression of TRAP1 facilitates the detailed study of its structure and function, allowing researchers to explore its role in tumor biology and its potential as a biomarker or therapeutic target. Additionally, understanding the mechanistic pathways through which TRAP1 operates could provide insights into novel cancer treatment strategies, particularly in the context of enhancing the efficacy of existing therapies and overcoming drug resistance. Overall, the study of TRAP1 reaffirms the importance of mitochondrial proteins in cancer and highlights the need for further investigations to elucidate its full functional repertoire and therapeutic potential.

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