Cat: IPD-X39538

Recombinant Human RAD23B Protein,His

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Analytical Data

  • Gene name

    RAD23B

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    HHR23B; P58; HR23B; XP-C Repair Complementing Protein; XP-C Repair Complementing Complex 58 kDa; UV excision repair protein RAD23 homolog B

  • Species

    Human

  • Source

    E. coli

  • Tag

    N-His

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P54727

  • Expression Region

    Met1~Asp409

  • Molecular Weight

    57kDa

  • 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

RAD23B is a member of the RAD23 family of proteins that plays a crucial role in maintaining genomic stability and regulating DNA repair processes. It functions primarily as a key player in the nucleotide excision repair pathway, which is essential for repairing bulky DNA lesions caused by environmental factors such as UV radiation and chemical exposure. RAD23B contains a ubiquitin-like domain that allows it to interact with ubiquitinated proteins, facilitating the recognition and repair of damaged DNA by recruiting repair factors to sites of lesions. Recent studies have highlighted the significance of RAD23B in various cellular processes, including the modulation of transcription, signaling pathways related to cell cycle and apoptosis, and its potential involvement in tumorigenesis. Given its essential role in DNA repair and cellular homeostasis, RAD23B has garnered attention as a potential biomarker for cancer and a target for therapeutic interventions. Understanding the molecular mechanisms governing RAD23B function and regulation may provide insights into developing strategies to enhance DNA repair capacity in cancer cells, thereby improving the efficacy of existing therapies. Current research endeavors aim to elucidate the structural and functional characteristics of RAD23B, explore its interactions with other proteins involved in DNA repair, and investigate its implications in cancer biology, thereby paving the way for novel therapeutic approaches targeting genomic stability.

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