Recombinant Human Frataxin, Mitochondrial (FXN) Protein (His&Myc)

Name: Recombinant Human Frataxin, Mitochondrial (FXN) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-02174P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Frataxin, Mitochondrial (FXN) Protein (His&Myc) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	Q16595
Target Symbol	FXN
Synonyms	CyaY; d-FXN; FA; FARR; Frataxin mature form; Frataxin(81-210); FRDA; FRDA_HUMAN; Friedreich ataxia protein; Fxn; i-FXN; m56-FXN; m78-FXN; m81-FXN; MGC57199; X25
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-10His&C-Myc
Target Protein Sequence	MWTLGRRAVAGLLASPSPAQAQTLTRVPRPAELAPLCGRRGLRTDIDATCTPRRASSNQRGLNQIWNVKKQSVYLMNLRKSGTLGHPGSLDETTYERLAEETLDSLAEFFEDLADKPYTFEDYDVSFGSGVLTVKLGGDLGTYVINKQTPNKQIWLSSPSSGPKRYDWTGKNWVYSHDGVSLHELLAAELTKALKTKLDLSSLAYSG kDa
Expression Range	1-210aa
Protein Length	Full Length
Mol. Weight	28.1 kDa
Research Area	Tags & Cell Markers
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.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
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; 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.
Subcellular Location	Mitochondrion. Cytoplasm, cytosol.
Protein Families	Frataxin family
Database References	HGNC: 3951 OMIM: 229300 KEGG: hsa:2395 STRING: 9606.ENSP00000366482 UniGene: PMID: 29794127 Knockdown of frataxin by > 70% in human hepatoma HepG2 cells caused a 20% reduction in secreted ApoA-I PMID: 29447225 In this study, the authors demonstrate that frataxin regulates the expression of genes involved in interferon induced apoptosis, DNA damage and blood clotting regulation. PMID: 27350085 the effect of alterations in loop-1, a stretch presumably essential for FXN function, on the conformational stability and dynamics of the native state. PMID: 29097312 differentiation of these induced pluripotent stem cells into neurons also results in resilencing of the FXN gene. PMID: 27615158 The NFS1/ISD11 complex further interacts with scaffold protein ISCU and regulator protein frataxin, thereby forming a quaternary complex for Fe-S cluster formation. PMID: 28271877 Molecular dynamics flexible fitting of protein structures docked into the EM map of the model revealed a [FXN(42-210)]24.[NFS1]24.[ISD11]24.[ISCU]24 complex, consistent with the measured 1:1:1:1 stoichiometry of its four components. PMID: 27519411 By interphase, FISH we found that in comparison to the normal Frataxin sequence the replication of expanded alleles is slowed or delayed. According to molecular combing, origins never fired within the normal Frataxin allele. PMID: 27447727 The differentially expressed FXN regulates the development of congenital heart disease (CHD) and the differential expression was under the control of miRNA-145. These results might provide new insight into the understanding of CHD pathogenesis and may facilitate further therapeutic studies. PMID: 26717909 Results presented here shed light on the folding mechanism of frataxin, opening the possibility of mutating it to generate hyperstable variants without altering their folding kinetics. PMID: 26856628 relative FXN expression in the patients was found to be correlated with the levels of MDA and ferritin but not correlated with transferrin saturation PMID: 26589002 Frataxin (FXN) gene mutations lead to mitochondrial iron accumulation without total body/organ iron overload. The clinical consequences are spinocerebellar degeneration and frequent cardiomyopathy. PMID: 26596411 Our results imply that regulation of FXN protein levels is complex and that total amounts can be modulated chemically and genetically without altering the absolute amount of mature FXN protein. PMID: 26671574 In compound heterozygotes, expression of partially functional mutant frataxin delays age of onset and reduces diabetes mellitus, compared to those with no frataxin expression from the non-expanded allele. PMID: 26704351 FXN promoter function was directly measured via metabolic labeling of newly synthesized transcripts in fibroblasts, which revealed that the YG8sR mouse was significantly deficient in transcriptional initiation compared to the Y47R mouse. PMID: 26393353 Thus, Src inhibitors emerge as a new class of drugs able to promote frataxin accumulation, suggesting their possible use as therapeutics in Friedreich's Ataxia PMID: 25948553 Engineered a cell line where the presence of an exogenous, inducible FXN gene rescues the cells from the knockout of the two endogenous FXN genes. This system allows the possibility of testing the progression of disease. PMID: 26035392 The region of chromosome 9 carrying the FXN gene is prone to chromosomal rearrangements in both control and Friedreich ataxia patient cells. PMID: 26379101 Expanded GAA repeats impair FXN gene expression and reposition the FXN locus to the nuclear lamina in single cells PMID: 25814655 Findings confirm a detrimental effect of frataxin silencing, not only for astrocytes, but also for neuron-glia interactions, underlining the need to take into account the role of non-cell autonomous processes in Friedreich's ataxia. PMID: 25554687 We propose a model of premature termination of FXN transcription induced by pathogenic expanded GAA repeats that links R-loop structures, antisense transcription, and heterochromatin formation PMID: 25831023 Patients with a FXN p.R165P missense mutation progress to a less disabling disease state than typical Friedreich ataxia patients PMID: 24816001 FXN accelerates a rate-limiting sulfur transfer step in the synthesis of [2Fe-2S] clusters on the human Fe-S assembly complex. PMID: 26016518 and the distribution of Nrf2 in silenced neurons for frataxin gene. Decreased Nrf2 mRNA content and a defective activation after treatment with pro-oxidants have been evidenced in frataxin-silenced neurons PMID: 23574943 frataxin absence is associated with overexpression of cell death-related genes, cell cycle arrest and oxidative related genes, as well as DNMT1, supporting the notion that DNA repair and epigenetic mechanisms are implicated in Friedreich's ataxia disease. PMID: 25929520 The decrease of p53 function and level reduced frataxin mRNA and protein.The transcriptional activity of the human frataxin gene is enhanced by p53. PMID: 25158131 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 In Friedreich ataxia, aberrant glucose metabolism is linked to increasing age, longer GAA repeat length on the shorter allele, frataxin point mutations, and increasing Body Mass Index. PMID: 24819921 Study determined the frequencies and repeat lengths for FXN trinucleotide repeat expansions in familial and sporadic amyotrophic lateral sclerosis cohorts, as well as in healthy controls PMID: 24613765 This study provides proof of principle that an orally dosed class I HDACi can increase both FXN mRNA and acetylation of a key residue in the blood of FRDA patients. PMID: 25159818 review focuses on the emerging function of frataxin in relation to the observed alterations in mitochondrial iron metabolism in Friedreich's ataxia. PMID: 24138602 FXN promoter silencing in FRDA is dependent on the length of the expanded GAA-TR mutation. PMID: 25112975 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 dysregulated Fe-S cluster biogenesis is a primary effect of both frataxin overexpression and deficiency as in Friedreich's ataxia. PMID: 24997422 Deficient transcriptional initiation, and not elongation, is the major cause of FXN transcriptional deficiency in Friedreich ataxia. PMID: 24737321 The pathological frataxin mutation L198R yields a global destabilization of the structure. PMID: 24920569 Fe-S assembly protein and frataxin convert substrates l-cysteine, ferrous iron, and electrons into Fe-S clusters. PMID: 24971490 This early failure, aggravating frataxin deficiency in a specifically vulnerable human cell population, indicates a developmental component in Friedreich ataxia . PMID: 23879205 Increased DNA methylation at the FXN upstream GAA region, primarily 5 hmC rather than 5 mC, and decreased CTCF occupancy at the FXN 5' UTR are associated with FRDA disease-relevant human tissues. PMID: 24023969 The data presented here show that the Isu1 suppressor mimics the frataxin effects on Nfs1, explaining the bypassing activity. PMID: 24217246 suggest that iron coordination to frataxin may be significant to the Fe-S cluster biosynthesis pathway in mitochondria. PMID: 23909240 Higher frataxin levels predicted less severe neurological dysfunction and were associated with slower rates of neurological change. PMID: 23691127 This study described a novel deletion in exon 5a of the FXN gene in patient with Friedreich ataxia. PMID: 23196337 frataxin is a crucial element of one of the most essential cellular machines specialized in iron-sulfur cluster biogenesis--{REVIEW} PMID: 23859340 Our results suggest for the first time that post-transcriptional regulation of frataxin occurs through the 3'-UTR and involves miRNA targeting. PMID: 23382970 Transcription activator-like effector proteins induce the expression of the frataxin gene PMID: 22587705 local unfolding of the C-terminal region may be a critical step for the global unfolding of hFXN, and modulation of the CTR interactions may strongly affect hFXN physiological function PMID: 23049850 frataxin point mutations have complex biochemical effects that synergistically contribute to the pathophysiology of Friedreich ataxia. PMID: 23269675 The protein level of isoform III decreased in Friedreich ataxia (FRDA] patient heart, while the mRNA level of isoform II decreased more in FRDA patient cerebellum compared to total FXN mRNA. PMID: 23082224 The guanine-adenine-adenine trinucleotide repeat expansion of FXN caused Friedreich ataxia. PMID: 23334592

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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.

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