|Other Names||Ketosamine-3-kinase, 271-, Fructosamine-3-kinase-related protein, FN3K-RP, FN3K-related protein, FN3KRP|
|Target/Specificity||The synthetic peptide sequence used to generate the antibody AP7067b was selected from the C-term region of human FN3X. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.|
|Format||The synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml deionized water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Function||Phosphorylates psicosamines and ribulosamines, but not fructosamines, on the third carbon of the sugar moiety. Protein- bound psicosamine 3-phosphates and ribulosamine 3-phosphates are unstable and decompose under physiological conditions. Thus phosphorylation leads to deglycation.|
|Tissue Location||Expressed in erythrocytes.|
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Provided below are standard protocols that you may find useful for product applications.
Mammalian fructosamine-3-kinase (FN3K) catalyzes phosphorylation of fructosamines formed by glycation, the nonenzymatic reaction of glucose with primary amines. FN3K for example catalyzes transformation of fructoselysine (FL) residues on glycated proteins, to FL-3-phosphate (FL3P). This phosphorylation destablilizes FL and propels spontaneous decomposition, thereby reversing at an early stage the nonenzymatic glycation process. Phosphorylation of fructosamines may initiate metabolism of the modified amine and result in deglycation of glycated proteins. In mammals, FN3K has a closely related homologue, FN3KRP (FN3K-related protein), which in the human genome is located just 8 kb upstream of FN3K on chromosome 17q25.3 FN3KRP, which is 68% sequence identity with FN3K, is a deglycating enzyme which phosphorylates the third carbon of the sugar moiety of ketosamines, and may play a role in freeing proteins from ribulosamines or psicosamines. A deglycation system may be an important factor in protecting cells from the deleterious effects of nonenzymatic glycation, which appears to be an important factor in the pathogenesis of diabetic complications.
Conner, J.R., et al., Biochem. Biophys. Res. Commun. 323(3):932-936 (2004).Collard, F., et al., Diabetes 52(12):2888-2895 (2003).Collard, F., et al., Biochem. J. 382 (PT 1), 137-143 (2004) (): ().
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