Cat: IPD-X36959

Recombinant Human RFK Protein,His & GST

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Analytical Data

  • Gene name

    RFK

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    RIFK; Flavokinase; ATP:riboflavin 5'-phosphotransferase

  • Species

    Human

  • Source

    E. coli

  • Tag

    N- His & GST

  • Purity

    Greater than 95% as determined by SDS-PAGE.

  • Uniprot

    Q969G6

  • Expression Region

    Met1~His155

  • Molecular Weight

    48kDa

  • 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

RFK (Riboflavin Kinase) is an enzyme involved in the biosynthesis of riboflavin (vitamin B2), essential for various biological processes, including energy production and antioxidant defense. Research on RFK has gained prominence due to its potential role in metabolic disorders and its implications in the development of novel therapeutic strategies. Specifically, understanding RFK's structure and function could lead to insights into how riboflavin metabolism affects cellular health and physiological well-being. Additionally, exploring RFK’s interactions with other macromolecules may unveil new regulatory mechanisms within metabolic pathways. The significance of RFK is further underscored by its application in biotechnology, where recombinant forms of the protein can be utilized in studies focused on enzyme engineering and the production of riboflavin in microbial systems. The investigation of RFK, therefore, not only enhances our understanding of riboflavin metabolism but also provides valuable tools for the advancement of synthetic biology and metabolic engineering. Moreover, as the demand for riboflavin in food and pharmaceutical industries rises, RFK's recombinant proteins represent a promising avenue for developing efficient production systems, highlighting its relevance in both fundamental research and applied biosciences.

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