Cat: IPD-X38433

Recombinant Rat PUMA Protein,His

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Analytical Data

  • Gene name

    PUMA

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    JFY1; BBC3; BCL2 Binding Component 3

  • Species

    Rat

  • Source

    E. coli

  • Tag

    N-His

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q80ZG6

  • Expression Region

    Arg76~Val170

  • Molecular Weight

    15kDa

  • 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

PUMA (p53 upregulated modulator of apoptosis) is a pivotal pro-apoptotic protein that plays a significant role in the intrinsic pathway of apoptosis, which is crucial for maintaining cellular homeostasis and preventing tumorigenesis. Initially discovered as a target gene of the tumor suppressor p53, PUMA is known for its ability to promote apoptosis in response to various cellular stressors, including DNA damage and oncogenic signals. Its mechanism of action involves the disruption of mitochondrial membrane integrity by binding to anti-apoptotic Bcl-2 family members, thereby facilitating the activation of caspases and leading to programmed cell death. Research on PUMA has gained traction due to its potential implications in cancer therapy, as targeting the regulatory pathways of PUMA could enhance the effectiveness of existing treatments. Furthermore, studies have shown that PUMA expression is often downregulated in various malignancies, suggesting its role as a crucial player in tumor suppression. Understanding the structural and functional characteristics of PUMA, including its interactions with other apoptotic regulators, is essential for developing novel therapeutic strategies aimed at reactivating its apoptotic potential in cancer cells. This has led to an increased interest in PUMA as a biomarker for cancer prognosis and a target for innovative drugs that can restore its function. As research continues, the insights gained from PUMA studies hold promise not only for advancing cancer treatment but also for uncovering broader mechanisms of apoptosis regulation within cellular contexts.

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