Analytical Data
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Gene name
RFK
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简介
RFK protein plays a key role in cellular metabolism by catalyzing the phosphorylation of riboflavin (vitamin B2) to generate flavin mononucleotide (FMN), making it the rate-limiting enzyme in FAD synthesis. This enzyme activity is critical for tumor necrosis factor (TNF)-induced reactive oxygen species (ROS) generation. RFK Protein, Human (His) is the recombinant human-derived RFK protein, expressed by E. coli , with N-His labeled tag.
- Application
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Alternative Names
Riboflavin kinase; Flavokinase; RFK; ATP:riboflavin 5'-phosphotransferase
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
Q969G6
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Expression Region
M1-H155
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Protein Length
Full Length
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Molecular Weight
18 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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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.
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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.
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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.
Quality inspection process
Related Products
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.
