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Mouse Anti-FXN Recombinant Antibody (1E11) (CBMAB-F2744-CQ)

This product is a mouse antibody that recognizes FXN. The antibody 1E11 can be used for immunoassay techniques such as: WB, FC, ELISA, IF.
See all FXN antibodies

Summary

Host Animal
Mouse
Specificity
Human
Clone
1E11
Antibody Isotype
IgG1, κ
Application
WB, FC, ELISA, IF

Basic Information

Immunogen
Recombinant human Frataxin (42-210aa) purified from E. coli
Specificity
Human
Antibody Isotype
IgG1, κ
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Concentration
1 mg/mL
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

Target

Full Name
Frataxin
Introduction
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.
Entrez Gene ID
2395
UniProt ID
Q16595
Alternative Names
Frataxin; Friedreich Ataxia Protein; FRDA; X25; Frataxin, Mitochondrial; Friedreich Ataxia;
Function
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.
Biological Process
Adult walking behavior Source: Ensembl
Cellular iron ion homeostasis Source: BHF-UCL
Cellular response to hydrogen peroxide Source: UniProtKB
Embryo development ending in birth or egg hatching Source: Ensembl
Heme biosynthetic process Source: BHF-UCL
Ion transport Source: UniProtKB-KW
Iron incorporation into metallo-sulfur cluster Source: BHF-UCL
Iron-sulfur cluster assembly Source: FlyBase
Mitochondrion organization Source: Ensembl
Negative regulation of apoptotic process Source: UniProtKB
Negative regulation of multicellular organism growth Source: Ensembl
Negative regulation of organ growth Source: Ensembl
Negative regulation of release of cytochrome c from mitochondria Source: UniProtKB
Oxidative phosphorylation Source: Ensembl
Positive regulation of aconitate hydratase activity Source: BHF-UCL
Positive regulation of catalytic activity Source: BHF-UCL
Positive regulation of cell growth Source: BHF-UCL
Positive regulation of cell population proliferation Source: BHF-UCL
Positive regulation of lyase activity Source: UniProtKB
Positive regulation of succinate dehydrogenase activity Source: BHF-UCL
Proprioception Source: Ensembl
Protein autoprocessing Source: BHF-UCL
Regulation of ferrochelatase activity Source: BHF-UCL
Response to iron ion Source: BHF-UCL
Cellular Location
Mitochondrion; Cytosol. PubMed:18725397 reports localization exclusively in mitochondria.
Involvement in disease
Friedreich ataxia (FRDA):
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.
PTM
Processed in two steps by mitochondrial processing peptidase (MPP). MPP first cleaves the precursor to intermediate form and subsequently converts the intermediate to yield frataxin mature form (frataxin(81-210)) which is the predominant form. The additional forms, frataxin(56-210) and frataxin(78-210), seem to be produced when the normal maturation process is impaired; their physiological relevance is unsure.

Hackett, P. T., Jia, X., Li, L., & Ward, D. M. (2022). Posttranslational regulation of mitochondrial frataxin and identification of compounds that increase frataxin levels in Friedreich’s ataxia. Journal of Biological Chemistry, 298(6).

Medina-Carbonero, M., Sanz-Alcázar, A., Britti, E., Delaspre, F., Cabiscol, E., Ros, J., & Tamarit, J. (2022). Mice harboring the FXN I151F pathological point mutation present decreased frataxin levels, a Friedreich ataxia-like phenotype, and mitochondrial alterations. Cellular and Molecular Life Sciences, 79(2), 74.

Culley, M. K., Zhao, J., Tai, Y. Y., Tang, Y., Perk, D., Negi, V., ... & Chan, S. Y. (2021). Frataxin deficiency promotes endothelial senescence in pulmonary hypertension. The Journal of Clinical Investigation, 131(11).

Doni, D., Rigoni, G., Palumbo, E., Baschiera, E., Peruzzo, R., De Rosa, E., ... & Costantini, P. (2021). The displacement of frataxin from the mitochondrial cristae correlates with abnormal respiratory supercomplexes formation and bioenergetic defects in cells of Friedreich ataxia patients. The FASEB Journal, 35(3), e21362.

Li, J., Li, Y., Wang, J., Gonzalez, T. J., Asokan, A., Napierala, J. S., & Napierala, M. (2020). Defining transcription regulatory elements in the human Frataxin gene: implications for gene therapy. Human gene therapy, 31(15-16), 839-851.

Du, J., Zhou, Y., Li, Y., Xia, J., Chen, Y., Chen, S., ... & Wang, Y. (2020). Identification of Frataxin as a regulator of ferroptosis. Redox Biology, 32, 101483.

Maio, N., Jain, A., & Rouault, T. A. (2020). Mammalian iron–sulfur cluster biogenesis: recent insights into the roles of frataxin, acyl carrier protein and ATPase-mediated transfer to recipient proteins. Current opinion in chemical biology, 55, 34-44.

Patra, S., & Barondeau, D. P. (2019). Mechanism of activation of the human cysteine desulfurase complex by frataxin. Proceedings of the National Academy of Sciences, 116(39), 19421-19430.

Fox, N. G., Yu, X., Feng, X., Bailey, H. J., Martelli, A., Nabhan, J. F., ... & Han, S. (2019). Structure of the human frataxin-bound iron-sulfur cluster assembly complex provides insight into its activation mechanism. Nature communications, 10(1), 2210.

Britti, E., Delaspre, F., Feldman, A., Osborne, M., Greif, H., Tamarit, J., & Ros, J. (2018). Frataxin‐deficient neurons and mice models of Friedreich ataxia are improved by TAT‐MTS cs‐FXN treatment. Journal of cellular and molecular medicine, 22(2), 834-848.

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For research use only. Not intended for any clinical use.

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