Cat: PA2000-2934

Recombinant Human ruvC Protein,His

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Analytical Data

  • Gene name

    ruvC

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    ruvC;Crossover junction endodeoxyribonuclease RuvC

  • Species

    Human

  • Source

    E. coli

  • Tag

    His tag N-Terminus

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P0A814

  • Expression Region

    2-173aa

  • AA Sequence

    AIILGIDPGSRVTGYGVIRQVGRQLSYLGSGCIRTKVDDLPSRLKLIYAGVTEIITQFQPDYFAIEQVFMAKNADSALKLGQARGVAIVAAVNQELPVFEYAARQVKQTVVGIGSAEKSQVQHMVRTLLKLPANPQADAADALAIAITHCHVSQNAMQMSESRLNLARGRLR

  • Molecular Weight

    34.6 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

RuvC is a crucial protein involved in the DNA repair and maintenance processes, particularly in the resolution of Holliday junctions during homologous recombination. This process is vital for genetic diversity, DNA repair, and ensuring genomic stability in organisms. The RuvC protein, an endonuclease, specifically recognizes and cleaves these crossover structures formed during DNA recombination, facilitating the proper segregation of chromosomes during cell division. Research into RuvC has gained momentum due to its important roles in microbiology, molecular genetics, and biotechnology. It has been found in various bacteria and plays a significant role in their survival and adaptability in changing environments. Moreover, understanding the mechanisms of RuvC can provide insights into broader biological processes, including mutation rates and the evolution of antibiotic resistance. Additionally, RuvC has implications in synthetic biology and genetic engineering, where it can be manipulated for targeted gene editing applications. As researchers continue to explore the structural and functional characteristics of RuvC, its potential applications in developing novel therapeutic strategies against antibiotic-resistant bacteria and improving genome editing technologies are being investigated, highlighting its importance in both fundamental and applied biological research.

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