Cat: PA1000-2742

Recombinant Human RNF7 Protein,His

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Analytical Data

  • Gene name

    RNF7

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    UBOX5;KIAA0860;RNF37;UBCE7IP5;RING finger Protein 37

  • Species

    Human

  • Source

    E. coli

  • Tag

    His tag N-Terminus

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q9UBF6

  • Expression Region

    1-113aa

  • AA Sequence

    MGSSHHHHHH SSGLVPRGSH MGSMADVEDG EETCALASHS GSSGSKSGGD KMFSLKKWNA VAMWSWDVEC DTCAICRVQV MDACLRCQAE NKQEDCVVVW GECNHSFHNC CMSLWVKQNN RCPLCQQDWV VQRIGK

  • Molecular Weight

    15 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

RNF7 is a member of the RING-finger protein family, which plays important roles in various cellular processes, particularly in the regulation of protein degradation and signaling pathways through the ubiquitin-proteasome system. The study of RNF7 has gained significant attention in recent years due to its involvement in several critical biological functions, including cell proliferation, differentiation, and stress response. RNF7 is known to act as an E3 ubiquitin ligase, facilitating the transfer of ubiquitin to target proteins, which can lead to their degradation or modulation of their functions. Dysregulation of RNF7 has been implicated in various diseases, including cancer and neurodegenerative disorders, making it a potential biomarker and therapeutic target. Understanding the molecular mechanisms underlying RNF7's function, its interactions with substrates, and its regulation is crucial for elucidating its role in these pathological conditions. Recent advances in recombinant protein technology have enabled the production of purified RNF7, allowing for in-depth biochemical and structural studies. These investigations aim to provide insights into RNF7's cellular functions, its interaction networks, and how it exerts its effects at the molecular level. The recombinant RNF7 protein has become a valuable tool in research for developing novel strategies to manipulate its activity, which could have significant implications for therapeutic interventions in diseases associated with its dysfunction. Thus, RNF7 represents an intriguing target for ongoing research focused on elucidating its biological roles and potential applications in medicine.

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