Cat: IPD-X40306

Recombinant Synechococcus sp. phr Protein ,His & SUMO

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Analytical Data

  • Gene name

    phr

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    DNA photolyase Photoreactivating enzyme

  • Species

    Synechococcus sp.

  • Source

    E. coli

  • Tag

    N- His-SUMO & C- Myc

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P05327

  • Expression Region

    2-484aa

  • Molecular Weight

    74.3 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

Phage display technology has emerged as a powerful tool for the study of protein interactions and the development of novel therapeutics. PHR (phage-derived recombinant) proteins, generated through this technique, enable the identification and characterization of protein-protein and protein-ligand interactions. The unique ability of phage display to present large libraries of peptides or proteins on the surface of bacteriophages allows researchers to screen for specific binding partners with high affinity and selectivity. This method has gained significant attention in various fields such as immunology, oncology, and drug development, facilitating the discovery of unique antibodies and targeting proteins for therapeutic applications. As a result, research on PHR recombinant proteins has become crucial in understanding biological processes, elucidating disease mechanisms, and creating innovative treatment strategies. Furthermore, the ability to engineer and optimize these proteins enhances their potential for use in diagnostics and therapeutics, paving the way for advancements in personalized medicine and targeted therapies. Overall, the research surrounding PHR recombinant proteins highlights the intersection of biotechnology and medicine, showcasing its promising implications for the future of healthcare.

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