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Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
| Primary Accession | Q16595 |
|---|---|
| Other Accession | NP_000135.2 |
| Gene ID | 2395 |
|---|---|
| Other Names | Frataxin, mitochondrial, Friedreich ataxia protein, Fxn, Frataxin intermediate form, i-FXN, Frataxin(56-210), m56-FXN, Frataxin(78-210), d-FXN, m78-FXN, Frataxin mature form, Frataxin(81-210), m81-FXN, FXN, FRDA, X25 |
| Target/Specificity | The synthetic peptide sequence is selected from aa 51-64 of HUMAN FXN |
| Format | Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI 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. |
| Name | FXN |
|---|---|
| Synonyms | FRDA, X25 |
| Function | Promotes the biosynthesis of heme and assembly and repair of iron-sulfur clusters by delivering Fe(2+) to proteins involved in these pathways. May play a role in the protection against iron-catalyzed oxidative stress through its ability to catalyze the oxidation of Fe(2+) to Fe(3+); the oligomeric form but not the monomeric form has in vitro ferroxidase activity. May be able to store large amounts of iron in the form of a ferrihydrite mineral by oligomerization; however, the physiological relevance is unsure as reports are conflicting and the function has only been shown using heterologous overexpression systems. Modulates the RNA-binding activity of ACO1. |
| Cellular Location | Mitochondrion Cytoplasm, cytosol Note=PubMed:18725397 reports localization exclusively in mitochondria. |
| Tissue Location | Expressed in the heart, peripheral blood lymphocytes and dermal fibroblasts. |
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Provided below are standard protocols that you may find useful for product applications.
Background
This nuclear gene encodes a mitochondrial protein which belongs to FRATAXIN family. The protein functions in regulating mitochondrial iron transport and respiration. The expansion of intronic trinucleotide repeat GAA results in Friedreich ataxia. Alternative splicing results in multiple transcript variants.
References
Tsai, C.L., et al. Biochemistry 49(43):9132-9139(2010)
Thierbach, R., et al. Biochem. J. 432(1):165-172(2010)
Bailey, S.D., et al. Diabetes Care 33(10):2250-2253(2010)
Marino, T.C., et al. Clin. Genet. 77(6):598-600(2010)
Li, K., et al. PLoS ONE 5 (8), E12286 (2010) :
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