FN3KRP Blocking Peptide (N-Term)
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Primary Accession | Q9HA64 |
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Gene ID | 79672 |
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Other Names | Ketosamine-3-kinase, 271-, Fructosamine-3-kinase-related protein, FN3K-RP, FN3K-related protein, FN3KRP |
Target/Specificity | The synthetic peptide sequence is selected from aa 24-38 of HUMAN FN3KRP |
Format | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
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. |
Name | FN3KRP {ECO:0000303|PubMed:15137908, ECO:0000312|HGNC:HGNC:25700} |
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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 (PubMed:14633848, PubMed:15137908). Ribuloselysine-3 phosphate and psicoselysine-3 phosphate adducts are unstable and decompose under physiological conditions (PubMed:14633848, PubMed:15137908). Not able to phosphorylate fructoselysine (PubMed:14633848). |
Tissue Location | Widely expressed; except in skeletal muscle where it is expressed at very low level (PubMed:15331600). Expressed in erythrocytes (PubMed:15137908). |
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Provided below are standard protocols that you may find useful for product applications.
Background
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.
References
Collard F.,et al.Diabetes 52:2888-2895(2003).
Wiemann S.,et al.Genome Res. 11:422-435(2001).
Ota T.,et al.Nat. Genet. 36:40-45(2004).
Collard F.,et al.Biochem. J. 382:137-143(2004).
Oppermann F.S.,et al.Mol. Cell. Proteomics 8:1751-1764(2009).
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