Cat: IPD-X39598

Recombinant Human NPQ Protein,His

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Analytical Data

  • Gene name

    NPQ

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    SPX; C12orf39; Spexin

  • Species

    Human

  • Source

    E. coli

  • Tag

    N-His

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q9BT56

  • Expression Region

    Ala27~Trp116

  • Molecular Weight

    33kDa

  • 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

Non-Photochemical Quenching (NPQ) is a vital photoprotective mechanism in photosynthetic organisms, allowing them to dissipate excess light energy as heat and prevent damage to the photosynthetic apparatus. This process is particularly crucial under conditions of high light intensity, where reactive oxygen species (ROS) can cause photoinhibition and reduce photosynthetic efficiency. The study of NPQ has gained momentum due to the increasing interest in optimizing photosynthesis for crop improvement and bioenergy production. Recent advances in molecular biology and biochemistry have facilitated the recombinant expression of NPQ-related proteins, such as the PsbS protein in higher plants and its homologs in algae. Research into the structure-function relationships of these proteins, alongside their interactions within the thylakoid membranes, has provided insights into the regulatory mechanisms underlying NPQ. By manipulating the expression and activity of NPQ proteins, scientists aim to enhance the photoprotective capacity of plants, potentially leading to improved biomass yields and stress tolerance. Furthermore, understanding NPQ at a molecular level could contribute to the development of novel biotechnological applications aimed at optimizing photosynthetic efficiency in agricultural systems, thus addressing challenges related to food security and climate change. As such, the characterization of recombinant NPQ proteins is critical for unveiling the underlying mechanisms and potential pathways for agricultural enhancements.

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