Flavokinase Recombinant Protein
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| Amount : | 20 µg |
| Purification : | Greater than 90.0% as determined by SDS-PAGE. |
| Content : | The Flavokinase solution containing 20mM Tris-HCl buffer (pH8.0) and 10% glycerol. |
| Storage condition : | Flavokinase although stable at 4°C for 1 week, should be stored below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze thaw cycles. |
| AA sequence : | MGSSHHHHHH SSGLVPRGSH MPRADCIMRH LPYFCRGQVV RGFGRGSKQL GIPTANFPEQ VVDNLPADIS TGIYYGWASV GSGDVHKMVV SIGWNPYYKN TKKSMETHIM HTFKEDFYGE ILNVAIVGYL RPEKNFDSLE SLISAIQGDI EEAKKRLELP EHLKIKEDNF FQVSKSKIMNGH. |
| Alternative Name : | Riboflavin kinase, ATP:riboflavin 5'-phosphotransferase, Flavokinase, RFK, RIFK, FLJ11149, RP11-422N19.2. |
Source : Escherichia Coli.
Flavokinase Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 182 amino acids (1-162 a.a.) and having a molecular mass of 20.5kDa. Flavokinase is fused to 20 a.a. His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Flavokinase is a transferases family member, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. Flavokinase is an enzyme that catalyzes the phosphorylation of riboflavin (vitamin B2) to form flavin-mononucleotide (FMN), which is an obligatory step in vitamin B2 utilization and flavin cofactor synthesis. It has been proposed that TNF, through the activation of the RFK gene, enhances the incorporation of FAD in NADPH oxidase enzymes, which is a critical step for the assembly and activation of NADPH oxidase.
For Research Use Only. Not for use in diagnostic/therapeutics procedures.
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