FN3K Human

FN3K was first purified and characterized from human erythrocytes. The enzyme was identified as a 35-kDa monomer expressed in various mammalian tissues . It has no significant homology to other known proteins and is encoded by genomic sequences located on human chromosomes 1 and 17 .

The primary function of FN3K is to phosphorylate fructoselysine residues on glycated proteins, converting them to fructoselysine-3-phosphate (FL3P). This phosphorylation destabilizes the FL adduct, leading to its spontaneous decomposition and effectively reversing the non-enzymatic glycation process at an early stage . This process is vital for protecting cells from the deleterious effects of non-enzymatic glycation, which is a significant factor in the pathogenesis of diabetic complications .

The concentrations of fructosamines and advanced glycation end products (AGEs) are elevated in diabetes, contributing to various complications . FN3K’s ability to deglycate these compounds makes it an important enzyme in mitigating the effects of diabetes. Loss of FN3K’s protective enzymatic activity has also been associated with the oncology of colorectal cancer .

Recombinant human FN3K is produced using E. coli expression systems. The recombinant protein is typically supplied as a carrier-free solution, which enhances protein stability and increases shelf-life . It is used in various research applications, including studies on diabetes and protein glycation.

Recombinant human FN3K should be stored at -20 to -70 °C to maintain its stability. It is recommended to use a manual defrost freezer and avoid repeated freeze-thaw cycles .