Flavokinase Human

Riboflavin Kinase Human Recombinant
Cat. No.
BT10036
Source
Escherichia Coli.
Synonyms
Riboflavin kinase, ATP:riboflavin 5'-phosphotransferase, Flavokinase, RFK, RIFK, FLJ11149, RP11-422N19.2.
Appearance
Sterile filtered colorless solution.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. They may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

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.

Product Specs

Introduction
Flavokinase, an enzyme belonging to the transferases family, specifically phosphotransferases, catalyzes the phosphorylation of riboflavin (vitamin B2) to flavin-mononucleotide (FMN). This conversion is crucial for vitamin B2 utilization and flavin cofactor synthesis. It's been suggested that TNF, by activating the RFK gene, may boost FAD incorporation into NADPH oxidase enzymes, a key process for their assembly and activation.
Description
Recombinant Human Flavokinase, expressed in E. coli, is a non-glycosylated polypeptide chain comprising 182 amino acids (with a sequence spanning from amino acid 1 to 162) and possesses a molecular weight of 20.5 kDa. A 20 amino acid His-Tag is fused to the N-terminus of the Flavokinase. Purification is achieved using proprietary chromatographic methods.
Physical Appearance
A clear, colorless solution that has been sterilized by filtration.
Formulation
The Flavokinase is supplied in a solution containing 20mM Tris-HCl buffer at a pH of 8.0 and 10% glycerol.
Stability
While Flavokinase remains stable for a week at 4°C, storage below -18°C is recommended. For prolonged storage, adding a carrier protein like 0.1% HSA or BSA is advised. Avoid repeated freeze-thaw cycles.
Purity
Purity exceeding 90.0% as determined by SDS-PAGE analysis.
Synonyms
Riboflavin kinase, ATP:riboflavin 5'-phosphotransferase, Flavokinase, RFK, RIFK, FLJ11149, RP11-422N19.2.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MPRADCIMRH LPYFCRGQVV RGFGRGSKQL GIPTANFPEQ VVDNLPADIS TGIYYGWASV GSGDVHKMVV SIGWNPYYKN TKKSMETHIM HTFKEDFYGE ILNVAIVGYL RPEKNFDSLE SLISAIQGDI EEAKKRLELP EHLKIKEDNF FQVSKSKIMNGH.

Product Science Overview

Function and Mechanism

Riboflavin kinase catalyzes the phosphorylation of riboflavin to form flavin mononucleotide (FMN), which is an essential step in the biosynthesis of flavin cofactors . These cofactors are vital for various biological processes, including cellular respiration, oxidative stress response, and the metabolism of fats, drugs, and steroids .

The reaction mechanism involves the transfer of a phosphate group from ATP to riboflavin, resulting in the production of FMN and ADP. This reaction is crucial for maintaining the cellular levels of flavin cofactors, which are necessary for the proper functioning of flavoproteins .

Expression and Purification

Recombinant human riboflavin kinase is typically expressed in Escherichia coli (E. coli) and purified using conventional chromatography techniques . The recombinant protein often includes a His-tag to facilitate purification and detection. The purified enzyme is used in various research applications to study its structure, function, and role in different biological processes .

Biological Significance

Human riboflavin kinase (HsRFK) is associated with several important physiological and pathological processes. It is involved in protecting cells from oxidative stress and amyloid-β toxicity, which are linked to neurodegenerative diseases such as Alzheimer’s . Additionally, HsRFK expression is related to the progression of certain malignant cancers .

Downregulation of HsRFK can lead to altered expression profiles of clock-controlled metabolic genes and disrupt the protective effects of flavins in stroke treatments . Reduced activity of HsRFK is also associated with protein-energy malnutrition and decreased thyroid hormone levels .

Therapeutic Potential

Given its key functions, HsRFK is considered a potential therapeutic target. Understanding the regulation of HsRFK activity and its interaction with other proteins can provide insights into the molecular basis of diseases associated with aberrant HsRFK availability . Furthermore, the differences between human and bacterial RFK enzymes suggest that bacterial RFK could be targeted for developing new antimicrobial agents .

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