Recombinant Human Mitofusin-2 (MFN2) Protein (His)

Name: Recombinant Human Mitofusin-2 (MFN2) Protein (His)
Brand: Beta LifeScience
SKU: BLC-02048P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Mitofusin-2 (MFN2) Protein (His) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Activity	Not tested.
Uniprotkb	O95140
Target Symbol	MFN2
Synonyms	(Transmembrane GTPase MFN2)
Species	Homo sapiens (Human)
Expression System	in vitro E.coli expression system
Tag	N-10His
Target Protein Sequence	MSLLFSRCNSIVTVKKNKRHMAEVNASPLKHFVTAKKKINGIFEQLGAYIQESATFLEDTYRNAELDPVTTEEQVLDVKGYLSKVRGISEVLARRHMKVAFFGRTSNGKSTVINAMLWDKVLPSGIGHTTNCFLRVEGTDGHEAFLLTEGSEEKRSAKTVNQLAHALHQDKQLHAGSLVSVMWPNSKCPLLKDDLVLMDSPGIDVTTELDSWIDKFCLDADVFVLVANSESTLMQTEKHFFHKVSERLSRPNIFILNNRWDASASEPEYMEEVRRQHMERCTSFLVDELGVVDRSQAGDRIFFVSAKEVLNARIQKAQGMPEGGGALAEGFQVRMFEFQNFERRFEECISQSAVKTKFEQHTVRAKQIAEAVRLIMDSLHMAAREQQVYCEEMREERQDRLKFIDKQLELLAQDYKLRIKQITEEVERQVSTAMAEEIRRLSVLVDDYQMDFHPSPVVLKVYKNELHRHIEEGLGRNMSDRCSTAITNSLQTMQQDMIDGLKPLLPVSVRSQIDMLVPRQCFSLNYDLNCDKLCADFQEDIEFHFSLGWTMLVNRFLGPKNSRRALMGYNDQVQRPIPLTPANPSMPPLPQGSLTQEEFMVSMVTGLASLTSRTSMGILVVGGVVWKAVGWRLIALSFGLYGLLYVYERLTWTTKAKERAFKRQFVEHASEKLQLVISYTGSNCSHQVQQELSGTFAHLCQQVDVTRENLEQEIAAMNKKIEVLDSLQSKAKLLRNKAGWLDSELNMFTHQYLQPSR
Expression Range	1-757aa
Protein Length	Full Length
Mol. Weight	87.9 kDa
Research Area	Cancer
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	Mitochondrial outer membrane GTPase that mediates mitochondrial clustering and fusion. Mitochondria are highly dynamic organelles, and their morphology is determined by the equilibrium between mitochondrial fusion and fission events. Overexpression induces the formation of mitochondrial networks. Membrane clustering requires GTPase activity and may involve a major rearrangement of the coiled coil domains (Probable). Plays a central role in mitochondrial metabolism and may be associated with obesity and/or apoptosis processes. Plays an important role in the regulation of vascular smooth muscle cell proliferation. Involved in the clearance of damaged mitochondria via selective autophagy (mitophagy). Is required for PRKN recruitment to dysfunctional mitochondria. Involved in the control of unfolded protein response (UPR) upon ER stress including activation of apoptosis and autophagy during ER stress. Acts as an upstream regulator of EIF2AK3 and suppresses EIF2AK3 activation under basal conditions.
Subcellular Location	Mitochondrion outer membrane; Multi-pass membrane protein.
Protein Families	TRAFAC class dynamin-like GTPase superfamily, Dynamin/Fzo/YdjA family, Mitofusin subfamily
Database References	HGNC: 16877 OMIM: 601152 KEGG: hsa:9927 STRING: 9606.ENSP00000235329 UniGene: PMID: 29212658 Mfn2 protects dopaminergic neurons exposed to paraquat both in vitro and in vivo: Implications for idiopathic Parkinson's disease. PMID: 28215578 this study provides novel insights into the tumor progression associated with MFN2 deficiency and suggests that the importance of mTORC2 inhibitor in the treatment of MFN2 downregulated cancer patients. PMID: 28176801 Collectively, the present study demonstrated mitochondrial fission as a tumor suppression process that is regulated by the HIF/miR125a/Mfn2 pathways, acting to restrict PANC1 cell survival, energy metabolism and migration, with potential implications for novel approaches for PC therapy. PMID: 29749475 a critical role of Mfn2 in CD4(+) T cell apoptosis in sepsis and the underlying mechanism of autophagy deficiency. PMID: 29358849 Loss of Yap reduced SIRT1 expression and inhibited Mfn2-mediated mitophagy. Collectively, our results identified Hippo-Yap as a tumor promoter in gastric cancer that was mediated via activation of the SIRT1/Mfn2/mitophagy axis, with potential applications to gastric cancer therapy involving cancer survival and migration. PMID: 29436693 The overexpression of Mfn2 could trigger cervical tumour apoptosis in vitro and in vivo, which was related to the mitochondrial pathway, and may provide a new treatment target for cervical carcinoma. PMID: 29587277 Data suggest that mitofusin-2 (MFN2) may be involved in cervical cancer pathogenesis as an oncogene and might serve as a biomarker of cervical squamous cell carcinoma (SCC). PMID: 29848692 This study detected a compound heterozygous MFN2 mutation in a patient with a severe phenotype and the co-occurrence of MFN2 and PMP22 mutations in a patient with an uncommon phenotype. PMID: 28660751 The research findings indicate that the inhibition of microRNA-214 promotes the epithelial mesenchymal transition process and contributes to bladder wall fibrosis by up-regulating Mitofusin 2, thus leading to the occurrence of interstitial cystitis in postmenopausal women. PMID: 28729638 report of two patients with pure axonal peripheral neuropathy who are carrying novel compound heterozygous mutations in MFN2 gene PMID: 28215760 The heterozygous mutation c.2251C>T was identified in exon 19 of the MFN2 gene, presumably leading to the truncation of the MFN2 protein (p.Gln751Ter). The mutation co-segregated completely with the disease within the family PMID: 27154191 In this Chinese Han population a novel Charcot-Marie-Tooth disease-associated gene mutations including the MFN2 (c.497C>T) was discovered. PMID: 27862672 Mosaicism and missense mutation in MFN2 lead to severe Charcot-Marie-Tooth disease in a daughter, with minimal clinical features in the father. PMID: 28063088 These findings suggest that specific MFN2 mutations cause tissue-selective mitochondrial dysfunction with increased adipocyte proliferation and survival and confirm a novel form of excess adiposity with paradoxical suppression of leptin expression. PMID: 28414270 This study identified a new mitochondria reprogramming pathway influencing breast cancer progression through SH3GL2 and MFN2. These proteins were frequently lost in breast cancer, which was traceable in the circulating exosomes. PMID: 26888829 MFN2 expression was lower in patients with heart failure with preserved ejection fraction compared to controls. PMID: 27179829 Mitofusin 2 - one of a few proteins involved in a maintenance of an appropriate mitochondrial architecture, and in the consequence in the regulation of mitochondrial metabolism and calcium signalling, the controlling of the mitochondrial DNA level, and the regulation of cell proliferation and differentiation is the focus. [REVIEW] PMID: 28132466 Our patient with MFN2-related CMT2 expands the clinical and mutational spectrum of individuals with autosomal recessive CMT2 and identifies a new clinical feature that warrants further observation. PMID: 26955893 It has been shown that mitofusin-2 is modified with K6-linked polyubiquitin in a HUWE1-dependent manner. PMID: 28943312 Studied association of genetic variants of the MAVS, MITA and MFN2 genes with leprosy in Han Chinese from Southwest China; found no association between the variants and susceptibility to leprosy. PMID: 27553710 MFN2 gene polymorphisms (rs873457, rs2336384, rs1474868, rs4846085 and rs2236055) may be associated with acute liver failure and the rs873457 and rs4846085 polymorphisms are correlated with the risk and prognosis of acute liver failure. PMID: 28513770 SLC25A46 is a new component in mitochondrial dynamics that serves as a regulator for MFN1/2 oligomerization. PMID: 28057766 Presenilin 2 (PS2), mutations in which underlie familial Alzheimer's disease (FAD), promotes endoplasmic reticulum-mitochondria coupling only in the presence of mitofusin 2 (Mfn2). PMID: 27239030 PGC-1alpha enhances Mfn2 transcription, but also leads to increased degradation of the Mfn2 protein, a key ubiquitylation target of Parkin on mitochondria. In vivo, Parkin has significant protective effects on the survival and function of nigral dopaminergic neurons in which the chronic expression of PGC-1alpha is induced PMID: 28053050 Exome sequencing identified MFN2 SNVs in two of the individuals. Neuropathy-associated CNV outside of the PMP22 locus is rare in Charcot-Marie-Tooth (CMT) disease . Nevertheless, there is potential clinical utility in testing for CNVs and exome sequencing in CMT cases negative for the CMT1A duplication. PMID: 26378787 Smad2 is a key scaffold, allowing RIN1 to act as a GTP exchange factor for MFN2-GTPase activation to promote mitochondrial ATP synthesis and suppress superoxide production during mitochondrial fusion. PMID: 27184078 our results suggest that KAP1 Ser473 phosphorylation acts through MFN2 reduction to restrict mitochondrial hyperfusion, thereby contributing to cancer cell survival under conditions of sustained metabolic stress PMID: 27364555 Mfn2 downregulation or the exogenous expression of normal Parkin restored cytosolic Ca(2+) transients in fibroblasts from patients with PARK2 mutations, a catalytically inactive Parkinson's disease (PD)-related Parkin variant had no effect. Parkin is directly involved in regulating ER-mitochondria contacts and provide new insight into the role of the loss of Parkin function in PD development PMID: 27206984 siRNA knockdown of mitofusin-2 (Mfn2), a protein that is involved in the tethering of endoplasmic reticulum and mitochondria, leads to increased contact between the two organelles. PMID: 27203684 Taken together, these data suggest that the striking reduction in mitochondria in MNs expressing mutant MFN2 is not the result of impaired biogenesis, but more likely the consequence of enhanced mitophagy. PMID: 27506976 our findings indicate miR-106a as an important factor to promote hypertrophic progress and suggest miR-106a as a new molecular target for the treatment of pathological hypertrophy. The present study also uncovered a novel relationship between miR-106a and Mfn2, with Mfn2 as a downstream signaling mediator of miR-106a. PMID: 27565029 The results of the present study demonstrated that Resveratrol may protect bronchial epithelial cells from cigarette smoke -induced apoptosis in vitro by preventing mitochondrial dysfunction, and MFN2 may be associated with the anti-apoptotic functions of RSV in HBE cells. PMID: 28406974 Low MFN2 expression in hepatocellular carcinoma indicated a worse overall survival. PMID: 27389277 Low expression of MFN2 is associated with lung adenocarcinoma. PMID: 26733181 Between 1999 and 2012, the genetic diagnosis of MFN2 mutation was made in 11 children who were treated in our department for different neurological symptoms. We found 5 different mutations in the MFN2 gene in 6 unrelated families PMID: 26686600 We report four novel mutations and four rare missense variants of MFN2 in Charcot-Marie-Tooth disease 2A families in mainland China PMID: 26801520 The results of this study suggested that the MFN2 gene should be considered in Polish hereditary motor-sensory neuropathiey II patients. PMID: 26581383 These results suggest that defects in Mfn2 could cause mitochondrial dysfunction and decrease trophoblastic cells' viability PMID: 26942197 This study demonstrated that Mfn2 gene polymorphisms were associated with essential hypertension in northern Han Chinese population, especially in male subjects PMID: 26816493 Report exposes a novel role for Shh in regulating mitochondrial dynamics and rescue the metabolic profile of tumor cells through regulation of mitofusin 1 and 2. PMID: 26446920 family study of early onset severe axonal Charcot-Marie-Tooth disease with dominant inheritance - SNP mutation in MFN2 PMID: 26916081 Our findings provide new insight into the mechanism underlying Mitofusin-2 regulation and the potential role of miR-761 in tocellular carcinoma, making it a potential candidate for use in HCC therapy in the future PMID: 26845057 HMGB1 can trigger apoptosis of T lymphocytes through mitochondrial death pathway associated with [Ca(2+)]i elevation. Mfn2 plays a pivotal role in this process, and it might be a novel therapeutic target in T cell apoptosis related disorders. PMID: 24662494 downregulationof expression is caused by activation of resting peripheral blood T cells PMID: 26566676 Mutations in the gene encoding MFN2 are associated with Charcot-Marie-Tooth disease type 2A and MFN2 is involved in several intracellular pathways that interact to regulate the mitochondrial network within cells. PMID: 26143526 These findings show that homozygous mutations at p.R707W in MFN2 are a novel cause of multiple symmetrical lipomatosis. PMID: 26085578 A deletion of exons 7 and 8 is a founder mutation in MFN2 in the UK population. PMID: 26114802 increased expression of miR-214 observed in a Huntington disease cell model could target MFN2, altered mitochondrial morphology and deregulated cell cycle PMID: 26307536 Mitofusin-2 over-expression leads to dysregulation of cell cycle and cell invasion in lung adenocarcinoma. PMID: 25796500

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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.

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