Cat: IPD-X28602

Recombinant Mouse Cope1 Protein (Baculovirus),Strep & His

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Analytical Data

  • Gene name

    Cope1

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    Cope; Coatomer subunit epsilon

  • Species

    Mouse

  • Source

    Baculovirus

  • Tag

    Strep;His

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    O89079

  • Expression Region

    M1-A308

  • Protein Length

    Full Length

  • 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

Cope1 is a member of the C3HC4 RING-finger E3 ubiquitin ligase family, playing a crucial role in the ubiquitin-proteasome system, which regulates protein degradation and turnover. Research on Cope1 has gained momentum due to its involvement in various cellular processes, including cell cycle regulation, apoptosis, and stress responses. Dysregulation of Cope1 has been implicated in several pathological conditions, such as cancer, neurodegenerative diseases, and inflammation. Understanding the structure and function of Cope1, particularly through the study of its recombinant protein, has the potential to elucidate its interacting partners and downstream signaling pathways. This knowledge could aid in the development of therapeutic strategies targeting the ubiquitin-proteasome system to treat diseases associated with Cope1 dysfunction. Additionally, the production of Cope1 recombinant protein allows for detailed biochemical assays, structural analyses, and the exploration of its enzymatic activity, thereby contributing to a more comprehensive understanding of its functional roles within the cell. The ongoing studies on Cope1 are expected to reveal valuable insights into its biological significance and therapeutic potential, making it a focus of interest in molecular biology and medical research.

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