Cat: IPD-X40238

Recombinant Arabidopsis thaliana OSM34 Protein ,His & SUMO

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Analytical Data

  • Gene name

    OSM34

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    OSL3_ARATH; OSM34; Osmotin-like protein OSM34

  • Species

    Arabidopsis thaliana

  • Source

    E. coli

  • Tag

    N- His-SUMO & C- Myc

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P50700

  • Expression Region

    23-244aa

  • Molecular Weight

    44.4 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

OSM34 is a recombinant protein derived from the Ostreococcus tauri, a marine green alga known for its simple genome and significant contributions to photosynthesis research. This protein has gained attention due to its potential applications in biotechnology and environmental science. As the global need for sustainable solutions grows, researchers are exploring the algal proteins for their ability to improve carbon fixation and enhance photosynthetic efficiency, which could lead to innovative strategies for carbon capture and renewable energy sources. OSM34, specifically, is being investigated for its unique structural properties and functional capabilities that may facilitate advancements in metabolic engineering and synthetic biology. Understanding the mechanisms behind OSM34's function can provide insights into its role in algal metabolism and interaction with environmental factors. This research not only aims to harness the functional potential of OSM34 for biotechnological applications but also to contribute to a broader understanding of algal biology, which is crucial in the context of climate change and ecological sustainability.

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