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Mouse Anti-FN3K Recombinant Antibody (4F2) (CBMAB-A3059-LY)

The product is antibody recognizes FN3K. The antibody 4F2 immunoassay techniques such as: WB, ELISA.
See all FN3K antibodies

Summary

Host Animal
Mouse
Specificity
Human
Clone
4F2
Antibody Isotype
IgG2a, κ
Application
WB, ELISA

Basic Information

Immunogen
FN3K (NP_071441.1, 61 a.a. ~ 170 a.a) partial recombinant protein with GST tag. MW of the GST tag alone is 26 KDa.
Specificity
Human
Antibody Isotype
IgG2a, κ
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Purity
> 95% Purity determined by SDS-PAGE.
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freezethaw cycles.

Target

Full Name
Fructosamine 3 Kinase
Introduction
FN3K catalyzes phosphorylation of fructosamines formed by glycation, the nonenzymatic reaction of glucose with primary amines followed by Amadori rearrangement. Phosphorylation of fructosamines may initiate metabolism of the modified amine and result in deglycation of glycated proteins (Delpierre et al., 2000 [PubMed 11016445]).[supplied by OMIM
Entrez Gene ID
64122
UniProt ID
Q9H479
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).
Biological Process
Epithelial cell differentiation Source: UniProtKB
Fructosamine metabolic process Source: GO_Central
Fructoselysine metabolic process Source: UniProtKB
Post-translational protein modification Source: Reactome
Protein deglycation Source: UniProtKB
Cellular Location
Cytosol

Minnaert, A. K., van Schie, L., Grootaert, H., Himpe, J., Devos, S., Weyts, W., ... & Remaut, K. (2022). Yeast-produced fructosamine-3-kinase retains mobility after ex vivo intravitreal injection in human and bovine eyes as determined by Fluorescence Correlation Spectroscopy. International Journal of Pharmaceutics, 621, 121772.

Yousefi, T., Pasha, A. R. G., Kamrani, G., Ebrahimzadeh, A., Zahedian, A., Hajian-Tilaki, K., ... & Qujeq, D. (2021). Evaluation of Fructosamine 3-kinase and Glyoxalase 1 activity in normal and breast cancer tissues. BioMedicine, 11(3), 15.

De Bruyne, S., van Schie, L., Himpe, J., De Somer, F., Everaert, I., Derave, W., ... & Delanghe, J. R. (2021). A potential role for fructosamine-3-kinase in cataract treatment. International journal of molecular sciences, 22(8), 3841.

Beeraka, N. M., Bovilla, V. R., Doreswamy, S. H., Puttalingaiah, S., Srinivasan, A., & Madhunapantula, S. V. (2021). The taming of nuclear factor erythroid-2-related factor-2 (Nrf2) deglycation by fructosamine-3-kinase (FN3K)-inhibitors-a novel strategy to combat cancers. Cancers, 13(2), 281.

Szwergold, B. (2021). A Hypothesis: Fructosamine-3-Kinase-Related-Protein (FN3KRP) catalyzes deglycation of maillard intermediates directly downstream from fructosamines. Rejuvenation Research, 24(4), 310-318.

Shrestha, S., Katiyar, S., Sanz-Rodriguez, C. E., Kemppinen, N. R., Kim, H. W., Kadirvelraj, R., ... & Kannan, N. (2020). A redox-active switch in fructosamine-3-kinases expands the regulatory repertoire of the protein kinase superfamily. Science signaling, 13(639), eaax6313.

Sartore, G., Ragazzi, E., Burlina, S., Paleari, R., Chilelli, N. C., Mosca, A., ... & Lapolla, A. (2020). Role of fructosamine-3-kinase in protecting against the onset of microvascular and macrovascular complications in patients with T2DM. BMJ Open Diabetes Research and Care, 8(1), e001256.

De Bruyne, S., Van den Broecke, C., Vrielinck, H., Khelifi, S., De Wever, O., Bracke, K., ... & Delanghe, J. R. (2020). Fructosamine-3-kinase as a potential treatment option for age-related macular degeneration. Journal of clinical medicine, 9(9), 2869.

Sanghvi, V. R., Leibold, J., Mina, M., Mohan, P., Berishaj, M., Li, Z., ... & Wendel, H. G. (2019). The oncogenic action of NRF2 depends on de-glycation by fructosamine-3-kinase. Cell, 178(4), 807-819.

Dunmore, S. J., Al-Derawi, A. S., Nayak, A. U., Narshi, A., Nevill, A. M., Hellwig, A., ... & Singh, B. M. (2018). Evidence that differences in fructosamine-3-kinase activity may be associated with the glycation gap in human diabetes. Diabetes, 67(1), 131-136.

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For research use only. Not intended for any clinical use.

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