Cat: PA2000-3623

Recombinant E.coli rpsG Protein,His

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Analytical Data

  • Gene name

    rpsG

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    rpsG;spoIIIG;RNA polymerase sigma-G factor

  • Species

    E.coli

  • Source

    E. coli

  • Tag

    His tag N-Terminus

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P02359

  • Expression Region

    2-179aa

  • AA Sequence

    PRRRVIGQRKILPDPKFGSELLAKFVNILMVDGKKSTAESIVYSALETLAQRSGKSELEAFEVALENVRPTVEVKSRRVGGSTYQVPVEVRPVRRNALAMRWIVEAARKRGDKSMALRLANELSDAAENKGTAVKKREDVHRMAEANKAFAHYRWLSLRSFSHQAGASSKQPALGYLN

  • Molecular Weight

    23.9 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

The rpsG gene, which encodes the ribosomal protein S7, plays a crucial role in the assembly and function of the ribosome, the cellular machinery responsible for protein synthesis. Researching rpsG is vital because ribosomal proteins are essential for maintaining the integrity and efficiency of the translational process, and any alterations in these proteins can lead to various developmental and metabolic disorders. Moreover, studies on rpsG and its encoded protein have implications for understanding antibiotic resistance, as some antibiotics target ribosomal proteins to inhibit bacterial growth. Recombinant protein technology offers a powerful approach to investigate the structure and function of the RpsG protein in detail. By producing rpsG in a heterologous system, researchers can analyze its interactions with other ribosomal components and characterize its biochemical properties. This understanding can shed light on the evolutionary adaptations of ribosomes across different organisms and may contribute to the development of novel antimicrobial agents. Additionally, studying rpsG can provide insights into the mechanisms of ribosome biogenesis and the regulation of gene expression at the translational level. Overall, the exploration of rpsG through recombinant protein studies is essential for elucidating fundamental biological processes and addressing critical challenges in microbiology and medicine.

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