Cat: IPD-X39800

Recombinant Saccharomyces cerevisiae HYP2 Protein ,His & SUMO

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Analytical Data

  • Gene name

    HYP2

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    Hypusine-containing protein HP2 eIF-4D

  • Species

    Saccharomyces cerevisiae

  • Source

    E. coli

  • Tag

    N- His-SUMO

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P23301

  • Expression Region

    2-157aa

  • Molecular Weight

    33 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.

Quality inspection process

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Protein Description

HYP2, or Hypoxia-Inducible Factor 2 Alpha (HIF-2α), plays a crucial role in cellular responses to hypoxic conditions, regulating genes involved in angiogenesis, erythropoiesis, and metabolism. Researchers have become increasingly interested in HYP2 due to its implications in various pathological conditions, including cancer, where its overexpression may contribute to tumor progression and metastasis, as well as in ischemic diseases, where it aids in tissue adaptation by promoting blood vessel formation. The ability of HYP2 to modulate cellular responses to oxygen availability highlights its importance in maintaining homeostasis under stress conditions. Moreover, understanding the regulatory mechanisms of HYP2 not only paves the way for developing therapeutic strategies targeting its activity but also provides insights into the fundamental processes of cellular signaling and adaptation. Recombination technology has enabled the production of HYP2 recombinant proteins, facilitating detailed studies of its functional roles, interactions with other signaling pathways, and potential as a therapeutic target. Thus, research on HYP2 encompasses a multidisciplinary approach involving molecular biology, biochemistry, and clinical applications, underscoring its significance in both health and disease contexts.

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