protein

Recombinant Mouse Frataxin, mitochondrial

MBS1168301

0.05 mg (E-Coli)

190 USD

Recombinant Protein

Recombinant Mouse Frataxin, mitochondrial

Frataxin

frataxin, mitochondrial; Frataxin, mitochondrial; frataxin, mitochondrial; frataxin

Fxn

Fxn; Fxn; FA; X25; FARR; Frda; Frda; Fxn

FRDA_MOUSE

E Coli or Yeast or Baculovirus or Mammalian Cell

78-207

207

LGTLDNPSSLDETAYERLAEETLDSLAEFFEDLADKPYT
LEDYDVSFGDGVLTIKLGGDLGTYVINKQTPNKQIWLSS
PSSGPKRYDWTGKNWVYSHDGVSLHELLARELTKALNTK
LDLSSLAYSGKGT

Greater than 90% as determined by SDS-PAGE.

Liquid containing glycerol; lyophilization may be available upon request.

Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

Promotes the biosynthesis of he 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. Modulates the RNA-binding activity of ACO1.

Studies of human, mouse and yeast homologues indicate a mitochondrial function for frataxin.Koutnikova H., Campuzano V., Foury F., Dolle P., Cazzalini O., Koenig M.Nat. Genet. 16:345-351(1997) Assembly and iron-binding properties of human frataxin, the protein deficient in Friedreich ataxia.Cavadini P., O'Neill H.A., Benada O., Isaya G.Hum. Mol. Genet. 11:217-227(2002) Frataxin is essential for extramitochondrial Fe-S cluster proteins in mammalian tissues.Martelli A., Wattenhofer-Donze M., Schmucker S., Bouvet S., Reutenauer L., Puccio H.Hum. Mol. Genet. 16:2651-2658(2007) The in vivo mitochondrial two-step maturation of human frataxin.Schmucker S., Argentini M., Carelle-Calmels N., Martelli A., Puccio H.Hum. Mol. Genet. 17:3521-3531(2008) The first cellular models based on frataxin missense mutations that reproduce spontaneously the defects associated with Friedreich ataxia.Calmels N., Schmucker S., Wattenhofer-Donze M., Martelli A., Vaucamps N., Reutenauer L., Messaddeq N., Bouton C., Koenig M., Puccio H.PLoS ONE 4:E6379-E6379(2009) Elucidation of the mechanism of mitochondrial iron loading in Friedreich's ataxia by analysis of a mouse mutant.Huang M.L., Becker E.M., Whitnall M., Rahmanto Y.S., Ponka P., Richardson D.R.Proc. Natl. Acad. Sci. U.S.A. 106:16381-16386(2009)

6679863

NP_032070.1

NM_008044.2

O35943

30.4kD

Metabolism Pathway (1324226); Mitochondrial Iron-sulfur Cluster Biogenesis Pathway (1324487); Porphyrin And Chlorophyll Metabolism Pathway (83219); Porphyrin And Chlorophyll Metabolism Pathway (407)

FXN: 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. Defects in FXN are the cause of Friedreich ataxia (FRDA). FRDA is an autosomal recessive, progressive degenerative disease characterized by neurodegeneration and cardiomyopathy it is the most common inherited ataxia. The disorder is usually manifest before adolescence and is generally characterized by incoordination of limb movements, dysarthria, nystagmus, diminished or absent tendon reflexes, Babinski sign, impairment of position and vibratory senses, scoliosis, pes cavus, and hammer toe. In most patients, FRDA is due to GAA triplet repeat expansions in the first intron of the frataxin gene. But in some cases the disease is due to mutations in the coding region. Belongs to the frataxin family. 2 isoforms of the human protein are produced by alternative splicing. Protein type: Motility/polarity/chemotaxis; Mitochondrial; EC 1.16.3.1. Cellular Component: cytoplasm; cytosol; mitochondrion. Molecular Function: 2 iron, 2 sulfur cluster binding; enzyme binding; ferric iron binding; ferrous iron binding; ferroxidase activity; iron-sulfur cluster binding; metal ion binding; oxidoreductase activity. Biological Process: adult walking behavior; aerobic respiration; cellular iron ion homeostasis; embryonic development ending in birth or egg hatching; heme biosynthetic process; ion transport; iron incorporation into metallo-sulfur cluster; iron ion homeostasis; iron-sulfur cluster assembly; mitochondrion organization and biogenesis; negative regulation of apoptosis; negative regulation of multicellular organism growth; negative regulation of organ growth; oxidative phosphorylation; positive regulation of axon extension; positive regulation of cell growth; positive regulation of cell proliferation; positive regulation of lyase activity; positive regulation of metalloenzyme activity; proprioception; protein autoprocessing; response to iron ion; transport

0.05 mg (E-Coli)

190 USD

0.05 mg (Yeast)

190

0.2 mg (E-Coli)

460

0.2 mg (Yeast)

460

0.5 mg (Yeast)

750