Cat: PA2000-4886

Recombinant Human rne Protein,His

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Analytical Data

  • Gene name

    rne

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    rne;ARD1;NIPP1;Nuclear inhibitor of Protein phosphatase 1

  • Species

    Human

  • Source

    E. coli

  • Tag

    His tag N-Terminus

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P21513

  • Expression Region

    35-125aa

  • AA Sequence

    EQKKANIYKGKITRIEPSLEAAFVDYGAERHGFLPLKEIAREYFPANYSAHGRPNIKDVLREGQEVIVQIDKEERGNKGAALTTFISLAGS

  • Molecular Weight

    16.1 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

Recombinant proteins have emerged as vital tools in biomedical research, drug development, and therapeutic applications due to their ability to produce proteins in a controlled manner. The growing demand for proteins, such as enzymes, hormones, and antibodies, has led to the use of recombinant DNA technology, which allows for the insertion of specific genes into host cells, typically bacteria, yeast, or mammalian cell lines. One notable area of interest is the generation of recombinant-nanobody fusion proteins, such as Rne, which can bind specifically to target molecules with high affinity and specificity. Rne protein, often derived from camelid sources, exhibits unique properties, including small size and stability, making it advantageous for various applications in diagnostics and therapeutics. Researchers have focused on optimizing expression systems and purification methods to enhance the yield and functionality of Rne recombinant proteins. Studies have also explored the potential for Rne proteins to serve as targeted delivery systems in drug formulations or to enhance imaging techniques in molecular biology. The ability to manipulate and create Rne proteins that retain their biological activities is paving the way for innovative research and clinical solutions, addressing challenges in disease treatment, diagnostics, and beyond. Overall, the advancements in recombinant protein technology, particularly with respect to Rne, represent significant progress in the life sciences, contributing to our understanding of molecular interactions and therapeutic strategies.

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