FN3K Antibody (N-term)(Ascites)
Mouse Monoclonal Antibody (Mab)
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Application
| WB, E |
|---|---|
| Primary Accession | Q9H479 |
| Reactivity | Human |
| Host | Mouse |
| Clonality | Monoclonal |
| Isotype | IgG1 |
| Clone Names | 788CT24.5.1 |
| Calculated MW | 35171 Da |
| Gene ID | 64122 |
|---|---|
| Other Names | Fructosamine-3-kinase, 271-, FN3K |
| Target/Specificity | Purified His-tagged FN3K protein was used to produced this monoclonal antibody. |
| Dilution | WB~~1:1000~8000 E~~Use at an assay dependent concentration. |
| Format | Mouse monoclonal antibody supplied in crude ascites with 0.09% (W/V) sodium azide. |
| Storage | Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
| Precautions | FN3K Antibody (N-term)(Ascites) is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | FN3K {ECO:0000303|PubMed:14633848, ECO:0000312|HGNC:HGNC:24822} |
|---|---|
| Function | Fructosamine-3-kinase involved in protein deglycation by mediating phosphorylation of fructoselysine residues on glycated proteins, to generate fructoselysine-3 phosphate (PubMed:11016445, PubMed:11522682, PubMed:11975663). Fructoselysine-3 phosphate adducts are unstable and decompose under physiological conditions (PubMed:11522682, PubMed:11975663). Involved in intracellular deglycation in erythrocytes (PubMed:11975663). Involved in the response to oxidative stress by mediating deglycation of NFE2L2/NRF2, glycation impairing NFE2L2/NRF2 function (By similarity). Also able to phosphorylate psicosamines and ribulosamines (PubMed:14633848). |
| Tissue Location | Widely expressed (PubMed:11522682). Expressed in erythrocytes (PubMed:11016445). |
For Research Use Only. Not For Use In Diagnostic Procedures.
Provided below are standard protocols that you may find useful for product applications.
BACKGROUND
May initiate a process leading to the deglycation of fructoselysine and of glycated proteins. May play a role in the phosphorylation of 1-deoxy-1-morpholinofructose (DMF), fructoselysine, fructoseglycine, fructose and glycated lysozyme.
REFERENCES
Delpierre G., et al. Diabetes 49:1627-1634(2000).
Yu L.-R., et al. J. Proteome Res. 6:4150-4162(2007).
Burkard T.R., et al. BMC Syst. Biol. 5:17-17(2011).
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