Recombinant Human RNA-binding protein FUS(FUS)

Code CSB-YP009069HU
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Source Yeast
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Code CSB-EP009069HU
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Source E.coli
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Code CSB-EP009069HU-B
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Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-BP009069HU
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Source Baculovirus
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Code CSB-MP009069HU
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Source Mammalian cell
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Product Details

Purity >85% (SDS-PAGE)
Target Names FUS
Uniprot No. P35637
Alternative Names 75 kDa DNA pairing protein; 75 kDa DNA-pairing protein; ALS6; Amyotrophic lateral sclerosis 6; fus; FUS CHOP; Fus like protein; FUS_HUMAN; FUS1; Fused in sarcoma; Fusion (involved in t(12,16) in malignant liposarcoma); Fusion derived from t(12,16) malignant liposarcoma; Fusion gene in myxoid liposarcoma; Heterogeneous nuclear ribonucleoprotein P2; hnRNP P2; hnRNPP2; Oncogene FUS; Oncogene TLS; POMp75; RNA binding protein FUS; RNA-binding protein FUS; TLS; TLS CHOP; Translocated in liposarcoma; Translocated in liposarcoma protein
Species Homo sapiens (Human)
Expression Region 1-526
Target Protein Sequence MASNDYTQQA TQSYGAYPTQ PGQGYSQQSS QPYGQQSYSG YSQSTDTSGY GQSSYSSYGQ SQNTGYGTQS TPQGYGSTGG YGSSQSSQSS YGQQSSYPGY GQQPAPSSTS GSYGSSSQSS SYGQPQSGSY SQQPSYGGQQ QSYGQQQSYN PPQGYGQQNQ YNSSSGGGGG GGGGGNYGQD QSSMSSGGGS GGGYGNQDQS GGGGSGGYGQ QDRGGRGRGG SGGGGGGGGG GYNRSSGGYE PRGRGGGRGG RGGMGGSDRG GFNKFGGPRD QGSRHDSEQD NSDNNTIFVQ GLGENVTIES VADYFKQIGI IKTNKKTGQP MINLYTDRET GKLKGEATVS FDDPPSAKAA IDWFDGKEFS GNPIKVSFAT RRADFNRGGG NGRGGRGRGG PMGRGGYGGG GSGGGGRGGF PSGGGGGGGQ QRAGDWKCPN PTCENMNFSW RNECNQCKAP KPDGPGGGPG GSHMGGNYGD DRRGGRGGYD RGGYRGRGGD RGGFRGGRGG GDRGGFGPGK MDSRGEHRQD RRERPY
Protein Length Full length protein
Tag Info The following tags are available.
N-terminal His-tagged
Tag-Free
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form Lyophilized powder
Buffer before Lyophilization Tris/PBS-based buffer, 6% Trehalose, pH 8.0
Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting
and FAQs
Protein FAQs
Storage Condition Store at -20°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet Please contact us to get it.

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Target Background

Function
(From Uniprot)
Binds both single-stranded and double-stranded DNA and promotes ATP-independent annealing of complementary single-stranded DNAs and D-loop formation in superhelical double-stranded DNA. May play a role in maintenance of genomic integrity.
Gene References into Functions
  1. loss of nuclear FUS caused DNA nick ligation defects in motor neurons. PMID: 30206235
  2. The herein presented data uncover a novel mechanism by which the fusion oncogene FUS-CHOP actively promotes invasion in myxoid and round cell liposarcoma through the activation of a SRC/FAK/RHO/ROCK signaling axis. PMID: 29190494
  3. When FUS was overexpressed and then de novo synthesis was blocked with ActD, the decay rate of LATS1/2 was slower in the FUS-overexpressed cells than in control cells. PMID: 30308519
  4. Motor neuron cultures exposed to mutant FUS (mutFUS)conditioned medium (ACM), but not wild-type FUS ACM, undergo significant cell loss, which is preceded by progressive degeneration of neurites. We found that Tumor TNFalpha is secreted into ACM of mutFUS-expressing astrocytes. Accordingly, mutFUS astrocyte-mediated motor neuron toxicity is blocked by targeting soluble TNFalpha with neutralizing antibodies. PMID: 29380416
  5. the abnormal stable complex of FUS-R521C/PRMT1/Nd1-L mRNA could contribute to neurodegeneration upon oxidative stress. PMID: 28094300
  6. more selective group of neurons appears to be affected in frontotemporal lobar degeneration (FTLD)-TDP and FTLD-FUS than in FTLD-tau PMID: 28984110
  7. Taken together, FUS RNA-recognition motif appears to play a crucial role in exaggerating the physiological/reversible self-assembly into pathological/irreversible fibrillization, thus contributing to manifestation of FUS cytotoxicity. PMID: 28432364
  8. Fus is a binding partner of FMRP. PMID: 28424484
  9. Study demonstrates that FUS mutants, but not WT forms, impair fast axonal transport (FAT) in brain tissue of patients with ALS, through a mechanism dependent on activation of p38 MAPK. PMID: 28273913
  10. In human stem cell-derived motor neurons, the RNA profile associated with concomitant loss of both TAF15 and FUS resembles that observed in the presence of the amyotrophic lateral sclerosis (ALS)-associated mutation FUS R521G, but contrasts with late-stage sporadic ALS patients. PMID: 27378374
  11. FUS P525L mutation alters transcriptome and microRNA pathways in motor neurons with implications for ALS pathogenesis. PMID: 28988989
  12. This study showed that in fibroblasts of FUS P525L mutation carriers, FUS mislocalized to the cytoplasm where it redistributed into stress granules with likely a dose effect. PMID: 29035885
  13. Results find that mutant but not wild-type FUS decreased dendritic growth, mRNA levels, and protein synthesis in dendrites. These data suggest that cytoplasmic FUS aggregates trap mRNA and its transporters, impairing dendritic mRNA trafficking and translation, in turn leading to the disruption of dendritic homeostasis and the development of frontotemporal dementia phenotypes. PMID: 28928015
  14. activation of the IGF-IR/PI3K/Akt signaling system is a common pattern in MLS which appears to be transcriptionally controlled, at least in part by induction of IGF2 gene transcription in a FUS-DDIT3-dependent manner. PMID: 28637688
  15. SOD1 mutations were present in 20% of familial amyotrophic lateral sclerosis (ALS) patients and 1.9% of sporadic ALS patients, while FUS mutations were responsible for 13.3% of familial ALS cases, and TARDBP mutations were rare in either familial or sporadic ALS cases. PMID: 27604643
  16. Depletion of SAFB1 reduced FUS's localization to chromatin-bound fraction and splicing activity, suggesting SAFB1 could tether FUS to chromatin compartment thorough N-terminal DNA-binding motif. Moreover, FUS interacts with another nuclear matrix-associated protein, Matrin3. PMID: 27731383
  17. A molecular docking and dynamics study concluded that R521C and R521H mutations in FUS result in weak binding with Karyopherin-beta2 leading to amyotrophic lateral sclerosis. PMID: 27381509
  18. both FUS and TDP43 colocalize with active RNA polymerase II at sites of DNA damage along with the DNA damage repair protein, BRCA1, and FUS and TDP43 participate in the prevention or repair of R loop-associated DNA damage, a manifestation of aberrant transcription and/or RNA processing PMID: 27849576
  19. FUS mutations were significantly more common among mainland Chinese patients than those among Caucasian populations (p=6.8x10-3). The high frequency of FUS mutations in FALS and SALS in mainland China is another genetic feature distinct from Caucasians. PMID: 26519472
  20. The impairment of PARP-dependent DNA damage response (DDR) signaling due to mutations in the FUS nuclear localization sequence induces additional cytoplasmic FUS mislocalization which in turn results in neurodegeneration and FUS aggregate formation in amyotrophic lateral sclerosis. PMID: 29362359
  21. ALS-associated mutations enhance FUS protein propagation in Drosophila neurons. PMID: 28429234
  22. juvenile ALS linked to FUS mutations represent a specific entity different from both classical juvenile ALS and adult ALS linked to FUS gene PMID: 28054830
  23. Motor neurons expressing FUS with the P525L or the R521H mutation showed cytoplasmic mislocalization of FUS, hypoexcitability, and axonal transport defects. PMID: 29021520
  24. Results suggest that RBM45 serves as a negative regulator to prevent FUS-mediated excessive recruitment of HDAC1 to the sites of DNA damage. PMID: 29140459
  25. The review describes the main physiological functions of FUS and considers evidence for each of the theories of amyotrophic lateral sclerosis pathogenesis. PMID: 28707655
  26. Authors used solid-state nuclear magnetic resonance methods to characterize the molecular structure of self-assembling fibrils formed by the LC domain of the fused in sarcoma (FUS) RNA-binding protein. From the 214-residue LC domain of FUS (FUS-LC), a segment of only 57 residues forms the fibril core, while other segments remain dynamically disordered. PMID: 28942918
  27. Nuclear magnetic resonance spectroscopy demonstrates the intrinsically disordered structure of FUS's nearly uncharged, aggregation-prone, yeast prion-like, low sequence-complexity domain is preserved after phosphorylation. PMID: 28790177
  28. Long noncoding RNA SchLAH functions through interaction with fused in sarcoma protein (FUS). PMID: 28196303
  29. Focus on the recent advances on approaches to uncover the mechanisms of wild type and mutant FUS proteins during development and in neurodegeneration (review). PMID: 27033831
  30. FUS-induced reductions to ER-mitochondria associations and are linked to activation of glycogen synthase kinase-3beta (GSK-3beta), a kinase already strongly associated with ALS/FTD. PMID: 27418313
  31. Motor-neuron disease (MND)-linked RNA-binding proteins (RBPs), TDP-43, FUS, and hnRNPA2B1, bind to and induce structural alteration of UGGAAexp. These RBPs suppress UGGAAexp-mediated toxicity in Drosophila by functioning as RNA chaperones for proper UGGAAexp folding and regulation of pentapeptide repeat translation. PMID: 28343865
  32. we analyzed fast axonal transport in larval motor neurons of Drosophila models of TARDBP (TDP-43), FUS and C9orf72. We also analyzed the effect of loss-of-function mutants of the Drosophila orthologs of TDP-43 and FUS, TBPH and caz, respectively. The motor activities of larvae and adults in these models were assessed to correlate potential defects in axonal transport with locomotor deficits PMID: 27056981
  33. These findings suggest a possible pathomechanism for amyotrophic lateral sclerosis in which mutated FUS inhibits correct splicing of minor introns in mRNAs encoding proteins required for motor neuron survival. PMID: 27252488
  34. This study revealed a characteristic phenotype in FUS/TLS-linked FALS patients in Japan. PMID: 26823199
  35. The aim of this review will be to provide a general overview of TDP-43 and FUS/TLS proteins and to highlight their physiological functions--{REVIEW} PMID: 27015757
  36. Mouse model that overexpresses FUS without a nuclear localization signal (DeltaNLS-FUS) shows progressive motor deficits/ALS phenotype PMID: 27368346
  37. Possible role of deregulated DNA binding function of FUS in ALS. PMID: 27693252
  38. Our in vivo studies of the hFUS-Q290X mutation in Drosophila link motor dysfunction to impairment in the GABAergic pathway. Our findings would facilitate further efforts in unravelling the pathophysiology of Essential tremor PMID: 27395408
  39. FUS is glycosylated with a high stoichiometry not only in the neural cells but also in the non-neural cell lines. PMID: 27903134
  40. The results of this study suggested that FUS mutations are the most frequent genetic cause in early-onset sporadic ALS patients of Chinese origin. PMID: 26972116
  41. Data show that induced pluripotent stem cells (iPSC)-derived motor neurons mimicked several neurodegenerative phenotypes including mis-localization of fused-in sarcoma (FUS) gene product into cytosolic. PMID: 26997647
  42. miR-141 and the FUS gene, which are inversely correlated, play significant functional roles in regulating human neuroblastoma. PMID: 26936280
  43. pathological TDP-43 and FUS may exert motor neuron pathology in amyotrophic lateral sclerosis through the initiation of propagated misfolding of SOD1 PMID: 26926802
  44. iNeurons may provide a more reliable model for investigating FUS mutations with disrupted NLS for understanding FUS-associated proteinopathies in amyotrophic lateral sclerosis PMID: 26795035
  45. A subset of juvenile-onset familial/sporadic ALS cases with FUS gene mutations reportedly demonstrates mental retardation or learning difficulty. PMID: 26984092
  46. Study implicates phosphorylation as an additional mechanism by which nuclear transport of FUS might be regulated and potentially perturbed in ALS and FTLD. PMID: 26403203
  47. Study identifies a common mechanism of transport into neurites of proteins linked to the pathology of Alzheimer's disease (i.e. sAPP) and ALS (i.e. FUS, TDP-43 and SOD1) PMID: 26605911
  48. RNA binding proteins TDP-43 and FUS do not consistently fit the currently characterised inclusion models suggesting that cells have a larger repertoire for generating inclusions than currently thought. PMID: 26293199
  49. Wild-type and mutant hFUS proteins induced neuronal degeneration with partial selectivity for motor neurons. Motor neuron loss was accompanied by abnormal neurite morphology and length. PMID: 26174443
  50. FUS mutation seems indicated in sporadic early-onset ALS patients especially if showing predominant bulbar symptoms and an aggressive disease course. PMID: 26362943

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Involvement in disease Angiomatoid fibrous histiocytoma (AFH); Amyotrophic lateral sclerosis 6, with or without frontotemporal dementia (ALS6); Tremor, hereditary essential 4 (ETM4)
Subcellular Location Nucleus
Protein Families RRM TET family
Tissue Specificity Ubiquitous.
Database Links

HGNC: 4010

OMIM: 137070

KEGG: hsa:2521

STRING: 9606.ENSP00000254108

UniGene: Hs.46894

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  Email: [email protected]
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