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Anti-Frataxin [2FRA-1G2]

Info

Applications ELISA IF WB
Antigen/Gene or Protein Targets  Frataxin 
Reactivity Human
Relevance The monoclonal anti-FRATAXIN antibody, clone 2FRA‐1G2 recognises human Frataxin. Frataxin is localized to the mitochondrion. The function of frataxin is not entirely clear, but it seems to be involved in assembly of iron-sulfur clusters. It has been proposed to act as either an iron chaperone or an iron storage protein. Its mRNA is predominantly expressed in tissues with a high metabolic rate (including liver, kidney, brown fat and heart). Reduced expression of frataxin is the cause of Friedreich's ataxia (FRDA), a lethal neurodegenerative disease. An overexpression of frataxin in Drosophila has shown an increase in antioxidant capability, resistance to oxidative stress insults and longevity.
Host Mouse
Immunogen TrpE‐Frataxin full length
Subclass IgG1 kappa
Notes Available in 100ul unit as ascites.

Recommended dilutions : 1/5000 for western blot 1/100‐1/1000 for immunofluorescence
Research Area Cancer, Cell Type or Organelle Marker, Epigenetics & Nuclear Signalling, Metabolism, Neurobiology

References: 15 entries

Koutnikova et al. 1998. Hum Mol Genet. 7(9):1485-9. PMID: 9700204.

Maturation of wild-type and mutated frataxin by the mitochondrial processing peptidase.

Europe PMC ID: 9700204

Bidichandani et al. 1998. Am J Hum Genet. 62(1):111-21. PMID: 9443873.

The GAA triplet-repeat expansion in Friedreich ataxia interferes with transcription and may be associated with an unusual DNA structure.

Europe PMC ID: 9443873

Rötig et al. 1997. Nat Genet. 17(2):215-7. PMID: 9326946.

Campuzano et al. 1997. Hum Mol Genet. 6(11):1771-80. PMID: 9302253.

Rötig et al. 1997. Nat Genet. 17(2):215-7. PMID: 9326946.

Aconitase and mitochondrial iron-sulphur protein deficiency in Friedreich ataxia.

Europe PMC ID: 9326946

Frataxin is reduced in Friedreich ataxia patients and is associated with mitochondrial membranes.

Europe PMC ID: 9302253

Foury et al. 1997. FEBS Lett. 411(2-3):373-7. PMID: 9271239.

Deletion of the yeast homologue of the human gene associated with Friedreich's ataxia elicits iron accumulation in mitochondria.

Europe PMC ID: 9271239

Babcock et al. 1997. Science. 276(5319):1709-12. PMID: 9180083.

Regulation of mitochondrial iron accumulation by Yfh1p, a putative homolog of frataxin.

Europe PMC ID: 9180083

Campuzano et al. 1996. Science. 271(5254):1423-7. PMID: 8596916.

Friedreich's ataxia: autosomal recessive disease caused by an intronic GAA triplet repeat expansion.

Europe PMC ID: 8596916


Add a reference

References: 15 entries

Koutnikova et al. 1998. Hum Mol Genet. 7(9):1485-9. PMID: 9700204.

Maturation of wild-type and mutated frataxin by the mitochondrial processing peptidase.

Europe PMC ID: 9700204

Bidichandani et al. 1998. Am J Hum Genet. 62(1):111-21. PMID: 9443873.

The GAA triplet-repeat expansion in Friedreich ataxia interferes with transcription and may be associated with an unusual DNA structure.

Europe PMC ID: 9443873

Rötig et al. 1997. Nat Genet. 17(2):215-7. PMID: 9326946.

Campuzano et al. 1997. Hum Mol Genet. 6(11):1771-80. PMID: 9302253.

Rötig et al. 1997. Nat Genet. 17(2):215-7. PMID: 9326946.

Aconitase and mitochondrial iron-sulphur protein deficiency in Friedreich ataxia.

Europe PMC ID: 9326946

Frataxin is reduced in Friedreich ataxia patients and is associated with mitochondrial membranes.

Europe PMC ID: 9302253

Foury et al. 1997. FEBS Lett. 411(2-3):373-7. PMID: 9271239.

Deletion of the yeast homologue of the human gene associated with Friedreich's ataxia elicits iron accumulation in mitochondria.

Europe PMC ID: 9271239

Babcock et al. 1997. Science. 276(5319):1709-12. PMID: 9180083.

Regulation of mitochondrial iron accumulation by Yfh1p, a putative homolog of frataxin.

Europe PMC ID: 9180083

Campuzano et al. 1996. Science. 271(5254):1423-7. PMID: 8596916.

Friedreich's ataxia: autosomal recessive disease caused by an intronic GAA triplet repeat expansion.

Europe PMC ID: 8596916


Add a reference

References: 15 entries

Koutnikova et al. 1998. Hum Mol Genet. 7(9):1485-9. PMID: 9700204.

Maturation of wild-type and mutated frataxin by the mitochondrial processing peptidase.

Bidichandani et al. 1998. Am J Hum Genet. 62(1):111-21. PMID: 9443873.

The GAA triplet-repeat expansion in Friedreich ataxia interferes with transcription and may be associated with an unusual DNA structure.

Rötig et al. 1997. Nat Genet. 17(2):215-7. PMID: 9326946.

Campuzano et al. 1997. Hum Mol Genet. 6(11):1771-80. PMID: 9302253.

Rötig et al. 1997. Nat Genet. 17(2):215-7. PMID: 9326946.

Aconitase and mitochondrial iron-sulphur protein deficiency in Friedreich ataxia.

Frataxin is reduced in Friedreich ataxia patients and is associated with mitochondrial membranes.

Foury et al. 1997. FEBS Lett. 411(2-3):373-7. PMID: 9271239.

Deletion of the yeast homologue of the human gene associated with Friedreich's ataxia elicits iron accumulation in mitochondria.

Babcock et al. 1997. Science. 276(5319):1709-12. PMID: 9180083.

Regulation of mitochondrial iron accumulation by Yfh1p, a putative homolog of frataxin.

Campuzano et al. 1996. Science. 271(5254):1423-7. PMID: 8596916.

Friedreich's ataxia: autosomal recessive disease caused by an intronic GAA triplet repeat expansion.


Add a reference


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