Recombinant Human Frataxin protein (rFc Tag)

Species

Human

Purity

>90 %, SDS-PAGE

Tag

rFc Tag

Activity

not tested

Cat no : Eg4622

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Validation Data Gallery

• 

  Purity of Recombinant Human Frataxin was determined by SDS-PAGE. The protein was resolved in an SDS-PAGE in reducing (R) and non-reducing (NR) conditions and stained using Coomassie blue.

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Product Information

• Purity: >90 %, SDS-PAGE
• Endotoxin: <0.1 EU/μg protein, LAL method
• Activity:

  Not tested

• Expression: HEK293-derived Human Frataxin protein Leu42-Ala210 (Accession# Q16595-1) with a rabbit IgG Fc tag at the N-terminus.
• GeneID: 2395
• Accession: Q16595-1
• PredictedSize: 46.0 kDa
• SDS-PAGE: 48-55 kDa, reducing (R) conditions
• Formulation: Lyophilized from 0.22 μm filtered solution in PBS, pH 7.4. Normally 5% trehalose and 5% mannitol are added as protectants before lyophilization.
• Reconstitution: Briefly centrifuge the tube before opening. Reconstitute at 0.1-0.5 mg/mL in sterile water.
• Storage Conditions:
  It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
  • Until expiry date, -20℃ to -80℃ as lyophilized proteins.
  • 3 months, -20℃ to -80℃ under sterile conditions after reconstitution.
• Shipping: The product is shipped at ambient temperature. Upon receipt, store it immediately at the recommended temperature.

Background

Frataxin (FXN), also named as FRDA, X25, m81-FXN, d-FXN, m78-FXN and i-FXN, belongs to the frataxin family. Frataxin is a mitochondrial iron-binding protein involved in iron storage, detoxification, and delivery for iron sulfur-cluster assembly and heme biosynthesis. It promotes the biosynthesis of heme and assembly and repair of iron-sulfur clusters by delivering Fe2+ to proteins involved in these pathways. Frataxin 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.

References:

1. O'Neill HA. et al. (2005). J Mol Biol. 345(3):433-9.  
2. Gakh O, et al. (2008). J Biol Chem. 283(46):31500-10.
3. Das D, et al. (2019). J Biol Chem. 294(23):9276-9284.