Cat: PA2000-4102

Recombinant Human RNF5 Protein,His

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Analytical Data

  • Gene name

    RNF5

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    RNF5;G16;NG2;RMA1;E3 ubiquitin-Protein ligase RNF5

  • Species

    Human

  • Source

    E. coli

  • Tag

    His tag N-Terminus

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q99942

  • Expression Region

    2-180aa

  • AA Sequence

    AAAEEEDGGPEGPNRERGGAGATFECNICLETAREAVVSVCGHLYCWPCLHQWLETRPERQECPVCKAGISREKVVPLYGRGSQKPQDPRLKTPPRPQGQRPAPESRGGFQPFGDTGGFHFSFGVGAFPFGFFTTVFNAHEPFRRGTGVDLGQGHPASSWQDSLFLFLAIFFFFWLLSI

  • Molecular Weight

    25.8 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

RNF5, an E3 ubiquitin ligase, plays a crucial role in regulating various cellular processes by mediating proteasomal degradation of target proteins, thereby influencing cell signaling, immune responses, and stress responses. Research on RNF5 has gained momentum due to its implications in several diseases, including cancer, autoimmune disorders, and neurodegenerative diseases. The ability of RNF5 to modulate the stability and activity of key regulatory proteins makes it a valuable target for therapeutic intervention. Moreover, RNF5's involvement in the endoplasmic reticulum (ER) stress response highlights its importance in maintaining cellular homeostasis. Recent studies have demonstrated that RNF5 participates in the regulation of protein quality control mechanisms, further underlining its significance in disease contexts. Recombinant RNF5 proteins are essential for in-depth studies aimed at elucidating its biological functions, understanding its role in various signaling pathways, and exploring its potential as a biomarker or therapeutic target. By generating recombinant RNF5, researchers can investigate its interactions with substrate proteins and other cellular factors, providing insights into the molecular mechanisms by which it exerts its effects. Overall, the exploration of RNF5 and its functions through recombinant protein studies represents a promising avenue for advancing our knowledge of cellular regulation and developing novel therapeutic strategies for related diseases.

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