Cat: IPD-X26317

Recombinant Human Bax Protein (E. coli Cell-free),His

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Analytical Data

  • Gene name

    Bax

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    rHuBCL2L4, His; Apoptosis Regulator BAX; Bcl-2-Like Protein 4; BCL2L4; BAX

  • Species

    Human

  • Source

    E. coli Cell-free

  • Tag

    N-10*His

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q07812-1

  • Expression Region

    M1-G192

  • Protein Length

    Full Length of Isoform-1

  • Molecular Weight

    23.3 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

Bax is a pro-apoptotic protein belonging to the Bcl-2 family, playing a crucial role in the intrinsic pathway of apoptosis. Its primary function is to promote cell death in response to various stress signals, including DNA damage and oxidative stress, by permeabilizing the mitochondrial outer membrane, leading to the release of cytochrome c and activation of caspases. Research into Bax has gained significant momentum due to its implications in cancer, neurodegenerative diseases, and other pathologies where apoptosis regulation is disrupted. Understanding Bax's structure and function is essential for developing targeted therapies that either mimic or inhibit its activity, potentially providing strategies to selectively induce death in cancer cells or protect against unwanted cell loss in neurodegeneration. Recent studies have focused on elucidating the molecular mechanisms underlying Bax activation and its interactions with other apoptotic and anti-apoptotic proteins. Advanced techniques such as cryo-electron microscopy and X-ray crystallography have allowed researchers to visualize Bax conformational changes upon activation, offering insights into its oligomerization process and membrane insertion behavior. Additionally, the exploration of Bax’s role in non-apoptotic processes, like autophagy and cell cycle regulation, has further expanded its significance in cellular biology. Overall, the ongoing investigation of Bax recombinant proteins not only enhances our understanding of apoptotic pathways but also opens avenues for innovative therapeutic approaches in various diseases characterized by dysregulated apoptosis.

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