CyaY; FA; FARR; FRDA; X25; FXN; Friedreich ataxia protein.

For Research Use Only. Not for use in diagnostic procedures.

E Coli

> 95% by SDS-PAGE

Liquid. In 20mM Tris-HCl Buffer (pH 8.5) containing 20% glycerol, 0.1M NaCl 1mM DTT.

1 mg/ml (determined by Bradford assay) (lot specific)

Can be stored at 4 degree C short term (1-2 weeks).
For long term storage, aliquot and store at -20 degree C or -70 degree C.
Avoid repeated freezing and thawing cycles.

Small volumes of FXN recombinant protein vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.

Frataxin, also known as FXN, is an iron binding protein which belongs to FRATAXIN family. It is an anti-apoptotic protein which prevents mitochondrial damage, reactive oxygen species production and act as either an iron chaperone or an iron storage protein. Frataxin is localized to the mitochondrion and regulating mitochondrial iron transport and respiration. Defects in this protein cause Friedreich ataxia. Recombinant Frataxin protein was expressed in E Coli and purified by using conventional chromatography techniques.

Apoptosis

SDS-PAGE

21.1 kDa (190aa), confirmed by MALDI-TOF. [Similar Products]

frataxin

frataxin, mitochondrial

Frataxin, mitochondrial

FRDA; X25; Fxn; i-FXN??[Similar Products]

This nuclear gene encodes a mitochondrial protein which belongs to the FRATAXIN family. The protein functions in regulating mitochondrial iron transport and respiration. The expansion of intronic trinucleotide repeat GAA from 8-33 repeats to >90 repeats results in Friedreich ataxia. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Jul 2016]

Promotes the biosynthesis of heme and assembly and repair of iron-sulfur clusters by delivering Fe2+ 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 Fe2+ to Fe3+; 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.

Campuzano V., et al. (1996) Science. 271 (5254):1423-7. ; Shan Y., et al. (2007) Hum Mol Genet. 16 (8):929-41. ;

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