Cat: IPD-X34051

Recombinant Human RECQ4 Protein (Baculovirus),Strep & His

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Analytical Data

  • Gene name

    RECQ4

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    RecQ4

  • Species

    Human

  • Source

    Baculovirus

  • Tag

    N-StrepⅡ;His

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    O94761

  • Expression Region

    A427-P1116

  • Protein Length

    Partial

  • 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

RECQ4 is a member of the RecQ helicase family, which plays a crucial role in maintaining genomic stability by unwinding DNA during replication and repair processes. Its dysfunction is associated with various disorders, including cancer predispositions and progeroid syndromes, highlighting its importance in cellular maintenance mechanisms. Researchers have increasingly focused on studying RECQ4 due to its potential implications in tumorigenesis and aging. Its helicase activity is vital for resolving replication stress, a condition that arises from impediments during DNA synthesis, often leading to double-strand breaks and genomic instability. Understanding RECQ4's structure-function relationship can provide insights into its biological role and therapeutic opportunities. Recent advances in protein expression and purification techniques have enabled the exploration of RECQ4's biochemical properties and interaction partners, further emphasizing its potential as a target for cancer therapies. Given the rising interest in targeted treatments, ongoing research aims to delineate the pathways mediated by RECQ4, which could reveal novel strategies for mitigating cancer risk and improving longevity by preserving genomic integrity.

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