Cat: IPD-X28557

Recombinant Mouse ATG7 Protein,His

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Analytical Data

  • Gene name

    ATG7

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    APG7L; GSA7; Ubiquitin-like modifier-activating enzyme ATG7; ATG12-activating enzyme E1 ATG7; Ubiquitin-activating enzyme E1-like protein

  • Species

    Mouse

  • Source

    E. coli

  • Tag

    N-His

  • Purity

    Greater than 95% as determined by SDS-PAGE.

  • Uniprot

    Q9D906

  • Expression Region

    Arg477~Val698

  • Molecular Weight

    28kDa

  • 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

ATG7, or autophagy-related protein 7, is a crucial component of the autophagy pathway, a cellular degradation process that maintains homeostasis by removing damaged organelles and misfolded proteins. Dysfunction in autophagy is linked to various diseases, including neurodegenerative disorders, cancer, and infections, making ATG7 a significant target for therapeutic intervention. Research on ATG7 recombinant protein has gained momentum due to its vital role in the conjugation of ATG12 to ATG5, a critical step in autophagosome formation. By understanding the structure and function of ATG7, scientists aim to elucidate its regulatory mechanisms and interactions with other autophagy-related proteins, paving the way for novel strategies to manipulate autophagy in disease contexts. Moreover, the production of ATG7 as a recombinant protein allows for detailed biochemical studies, structural analysis, and potential drug screening applications, further highlighting its importance in both basic and applied research. Overall, the exploration of ATG7 and its role in autophagy could provide insights into cellular health and disease, offering pathways for innovative therapeutic approaches.

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