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| Cat.No | ACP11799 | Target Name | FN3KRP |
|---|---|---|---|
| Form | Lyophilized powder | Expression System | Custom Production. Please inquire and provide the desire expression system. |
| Expression Range | 1-309 | Protein Length | Full length protein |
| Purity | >85% (SDS-PAGE) | Storage Buffer | 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, Liquid form: default storage buffer is Tris/PBS-based buffer, pH 8.0. |
| Target Species | Human | Uniprot ID | Q9HA64 |
|---|
Uniprot Id
Q9HA64
Target Species
Human
Target Name
FN3KRP
Target Full Name
Ketosamine-3-kinase
Target Function
Ketosamine-3-kinase involved in protein deglycation by mediating phosphorylation of ribuloselysine and psicoselysine on glycated proteins, to generate ribuloselysine-3 phosphate and psicoselysine-3 phosphate, respectively. Ribuloselysine-3 phosphate and psicoselysine-3 phosphate adducts are unstable and decompose under physiological conditions. Not able to phosphorylate fructoselysine.
Target Protein Families
Fructosamine kinase family
Target Tissue Specificity
Widely expressed; except in skeletal muscle where it is expressed at very low level. Expressed in erythrocytes.
Target Synonyms
EC 2.7.1.- ; FLJ12171; FN3K related protein; FN3K-related protein; FN3K-RP; FN3KL; Fn3krp; Fn3krp fructosamine-3-kinase-related protein; FN3X; Fructosamine-3-kinase-related protein; Ketosamine-3-kinase; KT3K_HUMAN; MGC40640; RGD1304570; RP23-293H17.3; Testis secretory sperm binding protein Li 211a
Target Background
A high concentration of glucose can result in non-enzymatic oxidation of proteins by reaction of glucose and lysine residues (glycation). Proteins modified in this way are less active or functional. This gene encodes an enzyme which catalyzes the phosphorylation of psicosamines and ribulosamines compared to the neighboring gene which encodes a highly similar enzyme, fructosamine-3-kinase, which has different substrate specificity. The activity of both enzymes may result in deglycation of proteins to restore their function. Alternative splicing results in multiple transcript variants.
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