protein

RFK Protein, Human (His)

HY-P73677

5 μg;10 μg;50 μg;100 μg

40;70;190;320 USD

RFK Protein, Human (His)

proteins

E. coli

5 μg;10 μg;50 μg;100 μg

40;70;190;320 USD

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. The total length of RFK Protein, Human (His) is 155 a.a., with molecular weight of ~18 kDa.

Human

The RFK protein serves as the rate-limiting enzyme in the synthesis of flavin adenine dinucleotide (FAD) by catalyzing the phosphorylation of riboflavin (vitamin B2) to form flavin-mononucleotide (FMN). This enzymatic activity is essential for the production of FAD, a crucial cofactor involved in various redox reactions within cells. Beyond its role in riboflavin metabolism, RFK has been implicated in the regulation of reactive oxygen species (ROS) production induced by tumor necrosis factor (TNF). Through its interaction with TNFRSF1A and CYBA, RFK physically and functionally couples TNFRSF1A to NADPH oxidase, a key enzyme complex in ROS generation. TNF activation of RFK may enhance the incorporation of FAD in NADPH oxidase, highlighting the importance of RFK in orchestrating critical steps for the assembly and activation of this oxidative stress-inducing enzyme complex.

Riboflavin kinase; Flavokinase; RFK; ATP:riboflavin 5'-phosphotransferase

Greater than 95% as determined by reducing SDS-PAGE.

Supplied as a 0.2 μm filtered solution of 50 mM Tris-HCL, 300 mM NaCl, pH 8.0, 10% Glycerol.

Shipping with dry ice