Fused in Sarcoma Proteine (FUS)

FUS encodes a multifunctional protein component of the heterogeneous nuclear ribonucleoprotein (hnRNP) complex. Zusätzlich bieten wir Ihnen FUS Antikörper (45) und FUS Kits (3) und viele weitere Produktgruppen zu diesem Protein an.

alle Proteine anzeigen Gen GeneID UniProt
FUS 2521 P35637
Maus FUS FUS 233908 P56959
Ratte FUS FUS 317385  
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Top FUS Proteine auf antikoerper-online.de

Showing 2 out of 2 products:

Katalog Nr. Origin Quelle Konjugat Bilder Menge Anbieter Lieferzeit Preis Details
HEK-293 Cells Human Myc-DYKDDDDK Tag Validation with Western Blot 20 μg Anmelden zum Anzeigen 11 Days
$888.80
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Escherichia coli (E. coli) Human GST tag Fused in Sarcoma (FUS) (AA 1-198), (partial) protein (GST tag) 1 mg Anmelden zum Anzeigen 60 bis 71 Tage
$1,842.50
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FUS Proteine nach Spezies und Herkunft

Origin Exprimiert in Konjugat
Human ,
,

Am meisten referenzierte FUS Proteine

  1. Human FUS Protein expressed in HEK-293 Cells - ABIN2721461 : Groen, Fumoto, Blokhuis, Engelen-Lee, Zhou, van den Heuvel, Koppers, van Diggelen, van Heest, Demmers, Kirby, Shaw, Aronica, Spliet, Veldink, van den Berg, Pasterkamp: ALS-associated mutations in FUS disrupt the axonal distribution and function of SMN. in Human molecular genetics 2013 (PubMed)
    Show all 5 Pubmed References

Weitere Proteine zu Fused in Sarcoma (FUS) Interaktionspartnern

Human Fused in Sarcoma (FUS) Interaktionspartner

  1. our study showed that a low expression of FUS1 is a common event in AML. Our conclusion is that determination of the FUS1 level has potential value for judging the prognosis of AML, and the AML prognosis may be affected by miR-378

  2. preliminary data show an intriguing expression profile of Gle1, MART3 and FUS genes in Spinal muscular atrophy (SMA), and suggest a critical role of FUS protein in the SMA pathogenesis.

  3. DNA-PK-dependent multiphosphorylation of FUS's prionlike domain does not cause cytoplasmic localization.

  4. A novel 1-bp duplication of a guanine in exon 14 of the FUS gene (c.1510dupG) was found. A G duplication at nucleotide 1510 (c.1510dupG), and creates a premature stop codon (p.G505Wfs*12)

  5. high-affinity binding of karyopherin-beta2 to the FUS C-terminal proline-tyrosine nuclear localization signal tethers the proteins together, allowing multiple, distributed weak intermolecular contacts to disrupt FUS self-association, blocking liquid-liquid phase separation

  6. analysis of two regulatory mechanisms of liquid-phase homeostasis that are disrupted in FUS-associated neurodegeneration

  7. analysis of how FUS condensation is physiologically regulated and how perturbations in these mechanisms can lead to disease

  8. These results reveal a previously unrecognized role for UBQLN2 in regulating the early stages of liquid-liquid phase separation by directly modulating the fluidity of protein-RNA complexes and the dynamics of SG formation.

  9. Overexpression of FUS or TDP-43 causes inhibition of the ubiquitin proteasome system (UPS) and toxicity, both of which are mitigated by overexpression of the Hsp40 chaperone.

  10. We demonstrate that FUS-eGFP is recruited into stress granule (SG) and that P525L profoundly alters their dynamics. With a screening campaign, we demonstrate that PI3K/AKT/mTOR pathway inhibition increases autophagy and ameliorates SG phenotypes linked to P525L FUS by reducing FUS-eGFP recruitment into SGs

  11. results suggest a role for FUS in regulating the activity of microRNA-mediated silencing.

  12. loss of nuclear FUS caused DNA nick ligation defects in motor neurons.

  13. 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.

  14. 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.

  15. 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.

  16. the abnormal stable complex of FUS-R521C/PRMT1/Nd1-L mRNA could contribute to neurodegeneration upon oxidative stress.

  17. more selective group of neurons appears to be affected in frontotemporal lobar degeneration (FTLD)-TDP and FTLD-FUS than in FTLD-tau

  18. 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.

  19. Fus is a binding partner of FMRP.

  20. 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.

Mouse (Murine) Fused in Sarcoma (FUS) Interaktionspartner

  1. results provide insights into the physiological functions of FUS as well as important pathways where mutant FUS can interfere with cellular processes and potentially contribute to the pathogenesis of ALS.

  2. results suggest a role for FUS in regulating the activity of microRNA-mediated silencing.

  3. a circuitry in which the upregulation of miR-409-3p and miR-495-3p, belonging to a brain-specific miRNA subcluster implicated in several neurodevelopmental disorders, produced the downregulation of Gria2, is reported.

  4. FUS regulates circular RNA biogenesis by binding the introns flanking the back-splicing junctions and that this control can be reproduced with artificial constructs.

  5. FUS and TAF15 exhibit similar global RNA interaction profiles in vivo, but affect a strikingly small subset of common genes. Unexpectedly, TAF15 influences a small fraction of amyotrophic lateral sclerosis events compared with TDP-43 and FUS in the mouse CNS.

  6. FUS and the ELAV-like proteins ELAVL4 and ELAVL1 control SynGAP mRNA stability in a 3'UTR length-dependent manner, resulting in the stable expression of the alternatively spliced SynGAP isoform alpha2.

  7. These two proteins were up-regulated in both HD and FUS/TLS heterozygote mice.

  8. Study established that Fus1 KO mice suffer from the age-related hearing loss (ARHL) of strial origin, making this model a valuable tool for studying mitochondrial/oxidative mechanisms of age-related hearing decline. The model describes the phenotype of premature hearing loss of strial etiology based on Fus1 loss-mediated mitochondrial dysfunction, and identify the target cells and tissues in the inner ear.

  9. Authors found that FUS, EWS and TAF15 expression is differentially regulated during brain development, both in time and in space. In particular, this study identifies a fine-tuned regulation of FUS and EWS during neuronal differentiation.

  10. Study characterizes a heterozygous knock-in mouse model of ALS and demonstrates that mutations in FUS result in a toxic gain of function leading to motor neuron disease through cell autonomous and non-cell autonomous mechanisms; shows that mutant FUS triggers toxic events in both motor neurons and neighboring cells to elicit motor neuron disease.

  11. We showed that Fus1KO mice develop multiple early aging signs including lordokyphosis, lack of vigor, inability to accumulate fat, reduced ability to tolerate stress, and premature death.

  12. 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.

  13. our findings indicate that cytoplasmic FUS mislocalization not only leads to nuclear loss of function, but also triggers motor neuron death through a toxic gain of function within motor neurons.

  14. The data of this study support the notion that expression of cytoplasmically mislocalized FUS with compromised RNA-binding capacity causes particularly prominent and harmful FUS pathology in the mouse nervous system.

  15. These results highlight the pivotal role of FUS in regulating GluA1 mRNA stability, post-synaptic function and fronto-temporal lobar degeneration-like animal behaviors.

  16. these studies establish potentially converging disease mechanisms in amyotrophic lateral sclerosis (ALS) and spinal muscular atrophy, with ALS-causative mutants acquiring properties representing both gain and loss of function.

  17. FUS/TLS depletion causes phenotypes possibly related to neuropsychiatric and neurodegenerative conditions, but distinct from ALS and ET, together with specific alterations in RNA metabolisms.

  18. It is associated with amyotrophic lateral sclerosis and its mutation causes accumulation of fus positive stress granules in neurons.

  19. Study provides evidence for loss of PRMT1 function as a consequence of cytoplasmic accumulation of FUS in the pathogenesis of amyotrophic lateral sclerosis, including changes in the histone code regulating gene transcription.

  20. our study provided evidence that a multistep process of FUS aggregation in the cell cytoplasm includes RNA-dependent and RNA-independent mechanisms.

FUS Protein Überblick

Protein Überblick

This gene encodes a multifunctional protein component of the heterogeneous nuclear ribonucleoprotein (hnRNP) complex. The hnRNP complex is involved in pre-mRNA splicing and the export of fully processed mRNA to the cytoplasm. This protein belongs to the FET family of RNA-binding proteins which have been implicated in cellular processes that include regulation of gene expression, maintenance of genomic integrity and mRNA/microRNA processing. Alternative splicing results in multiple transcript variants. Defects in this gene result in amyotrophic lateral sclerosis type 6.

Genbezeichner und Symbole assoziert mit Fused in Sarcoma Proteine (FUS)

  • FUS RNA binding protein (FUS)
  • fused in sarcoma (Fus)
  • FUS RNA binding protein (Fus)
  • fused in sarcoma (FUS)
  • ALS6 Protein
  • D430004D17Rik Protein
  • D930039C12Rik Protein
  • ETM4 Protein
  • FUS/TLS Protein
  • Fus1 Protein
  • HNRNPP2 Protein
  • POMP75 Protein
  • Tls Protein

Bezeichner auf Proteinebene für Fused in Sarcoma Proteine (FUS)

75 kDa DNA-pairing protein , RNA-binding protein FUS , fus-like protein , fusion gene in myxoid liposarcoma , heterogeneous nuclear ribonucleoprotein P2 , oncogene FUS , oncogene TLS , translocated in liposarcoma protein , fusion, derived from t(12;16) malignant liposarcoma , hnRNP P2 , pigpen protein , protein pigpen , translocated in liposarcoma , fusion , pigpen , fusion (involved in t(12;16) in malignant liposarcoma) , 16) in malignant liposarcoma) , 16) malignant liposarcoma , fusion (involved in t(12 , fusion, derived from t(12

GENE ID SPEZIES
2521 Homo sapiens
233908 Mus musculus
414144 Gallus gallus
280796 Bos taurus
317385 Rattus norvegicus
479778 Canis lupus familiaris
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