Recombinant Mouse Frataxin, Mitochondrial (FXN) Protein (His-SUMO)

Name: Recombinant Mouse Frataxin, Mitochondrial (FXN) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-10713P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Product Overview

Description	Recombinant Mouse Frataxin, Mitochondrial (FXN) Protein (His-SUMO) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	O35943
Target Symbol	FXN
Synonyms	Fxn; FrdaFrataxin; mitochondrial; Fxn; EC 1.16.3.1) [Cleaved into: Frataxin intermediate form; Frataxin mature form]
Species	Mus musculus (Mouse)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	LGTLDNPSSLDETAYERLAEETLDSLAEFFEDLADKPYTLEDYDVSFGDGVLTIKLGGDLGTYVINKQTPNKQIWLSSPSSGPKRYDWTGKNWVYSHDGVSLHELLARELTKALNTKLDLSSLAYSGKGT
Expression Range	78-207aa
Protein Length	Full Length of Mature Protein
Mol. Weight	30.4kDa
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	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. Modulates the RNA-binding activity of ACO1.
Subcellular Location	Cytoplasm, cytosol. Mitochondrion. Note=PubMed:17597094 describes localization exclusively in mitochondria.
Protein Families	Frataxin family
Database References	KEGG: mmu:14297 STRING: 10090.ENSMUSP00000080081 UniGene: Mm.7319
Tissue Specificity	Heart, liver, skeletal muscle, kidney, spleen and thymus. Weakly expressed in the brain and lung.

Gene Functions References

This study demonstrated that mouse model of Friedreich's ataxia showed that decreased grip strength endurance time , threshold of peripheral sensitivity using Von Frey monofilaments and gait parameters. PMID: 27575947
Here, the authors show that loss of Fxn in the nervous system in mice also activates an iron/sphingolipid/PDK1/Mef2 pathway, indicating that the mechanism is evolutionarily conserved. PMID: 27901468
The in vitro antioxidant treatments trigger the axonal re-growth and the increase in stable MTs in shFxn, thus contributing to identify new neuronal targets of oxidation in this disease and providing a novel approach for antioxidant therapies. PMID: 27516386
Retinal FXN levels are increased in response to ischemia. Furthermore, elevated FXN levels had a clear neuroprotective effect as shown by increased ganglion cell survival after acute retinal ischemia/reperfusion. Frataxin's neuroprotective effect was associated with an upregulation of antioxidative enzymes. PMID: 27537261
Frataxin Deficiency Promotes Excess Microglial DNA Damage and Inflammation that Is Rescued by PJ34 PMID: 26954031
Frataxin-deficient mice, which had higher mitochondrial iron loading, showed impaired airway mucociliary clearance and higher pulmonary inflammation at baseline. PMID: 26752519
Using a mouse model of hepatic FXN deficiency in combination with mice deficient for IRP1, a key regulator of cellular iron metabolism, we show that IRP1 activation in conditions of Fe-S deficiency increases the available cytosolic labile iron pool PMID: 25651183
The Fxn KO/Mck mice tested from one to two months of age showed abnormal gait patterns accompanied by a loss in motor skills PMID: 25765157
Reduced expression of frataxin in Friedreich's ataxia leads to elevation of COX2-mediated oxylipin synthesis stimulated by increases in transcription factors that respond to increased reactive oxygen species. PMID: 25104852
Frataxin-deficient cells showed a specific inhibition of mitochondrial Complex I activity already at 70% residual frataxin levels, whereas the glutathione imbalance progressively increased after silencing. PMID: 24714088
The results support a mechanistic hypothesis in which frataxin deficiency decreases Nrf2 expression in vivo, causing the sensitivity to oxidative stress in target tissues the DRG and the cerebella, which contributes to the process of neurodegeneration. PMID: 23350650
rescue of the Friedreich ataxia knockout mutation in transgenic mice containing an FXN-EGFP genomic reporter PMID: 24667739
these results indicate that IGF-I exerts cell-context neuroprotection in frataxin deficiency that maybe therapeutically effective. PMID: 23039828
Data show that the respiratory chain defects accompanying frataxin deficiency cause progressive hyperacetylation of cardiac mitochondrial proteins due to the inhibition of SIRT3 deacetylase. PMID: 22394676
dual, pro-proliferative but chemosensitizing role in astrocytic tumors PMID: 21863062
Distribution of frataxin in eye retina of normal mice and of transgenic R7E mice with retinal degeneration PMID: 20799613
As an attempt to generate a mouse model of Friedreich ataxia, we introduced a (GAA)(230) repeat within the mouse frataxin gene by homologous recombination. PMID: 11852098
studies indicate an association between frataxin deficiency, iron deposits and cardiac fibrosis, but no obvious association between iron accumulation and neurodegeneration similar to Friedreich ataxia could be detected PMID: 12880182
frataxin has a role in cellular growth arrest and apoptosis, and its absence can cause experimental diabetes PMID: 12925693
We have generated two mouse models for FRDA that specifically develop progressive mixed cerebellar and sensory ataxia, the most prominent neurological features of Friedreich ataxia with a slowly progressive neurological degeneration PMID: 14985441
frataxin may act as a mitochondrial tumor suppressor protein PMID: 16278235
The identification of a core set of genes changing early in the FRDA pathogenesis can be a useful tool in both clarifying the disease process and in evaluating new therapeutic strategies. PMID: 16442805
Reduced expression of mitochondrial frataxin in mice exacerbates diet-induced obesity. PMID: 17404227
The fxn GAA repeat expansion mutation induces comparable epigenetic changes in human and transgenic mouse brain and heart. PMID: 18045775
loss of Fxn markedly alters cellular Fe trafficking and Fe chelation limits myocardial hypertrophy in the mutant PMID: 18621680
Frataxin deficiency causes upregulation of mitochondrial Lon and ClpP proteases and severe loss of mitochondrial Fe-S proteins. PMID: 19154341
The PPARG pathway is dysregulated in frataxin deficient mice and Friedreich's ataxia patients. PMID: 19376812
We showed that complete absence of murine frataxin in fibroblasts inhibits cell division and leads to cell death. This lethal phenotype was rescued through transgenic expression of human wild type as well as mutant (hFXN(G130V) and hFXN(I154F)) frataxin PMID: 19629184
Results enable the construction of a model explaining the cytosolic iron deficiency and mitochondrial iron loading in the absence of frataxin, which is important for understanding the pathogenesis of Friedreich's ataxia. PMID: 19805308

FAQs

Please fill out the Online Inquiry form located on the product page. Key product information has been pre-populated. You may also email your questions and inquiry requests to sales1@betalifesci.com. We will do our best to get back to you within 4 business hours.

Feel free to use the Chat function to initiate a live chat. Our customer representative can provide you with a quote immediately.

Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.