Fused in Sarcoma Proteine (FUS)

FUS encodes a multifunctional protein component of the heterogeneous nuclear ribonucleoprotein (hnRNP) complex. Zusätzlich bieten wir Ihnen FUS Antikörper (40) 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 2 bis 3 Tage
$814.00
Details
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
Details

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 3 Pubmed References

Weitere Proteine zu Fused in Sarcoma (FUS) Interaktionspartnern

Human Fused in Sarcoma (FUS) Interaktionspartner

  1. FUS P525L mutation alters transcriptome and microRNA pathways in motor neurons with implications for ALS pathogenesis.

  2. 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.

  3. 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.

  4. activation of the IGF-IR/PI3K (zeige PIK3CA Proteine)/Akt (zeige AKT1 Proteine) 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 (zeige DDIT3 Proteine)-dependent manner.

  5. 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.

  6. Depletion of SAFB1 (zeige SAFB Proteine) reduced FUS's localization to chromatin-bound fraction and splicing activity, suggesting SAFB1 (zeige SAFB Proteine) could tether FUS to chromatin compartment thorough N-terminal DNA-binding motif. Moreover, FUS interacts with another nuclear matrix-associated (zeige SMARCA5 Proteine) protein, Matrin3.

  7. 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.

  8. both FUS and TDP43 (zeige TARDBP Proteine) colocalize with active RNA polymerase II at sites of DNA damage along with the DNA damage repair protein, BRCA1, and FUS and TDP43 (zeige TARDBP Proteine) participate in the prevention or repair of R loop-associated DNA damage, a manifestation of aberrant transcription and/or RNA processing

  9. 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 (zeige CDH23 Proteine) in mainland China is another genetic feature distinct from Caucasians.

  10. The impairment of PARP-dependent DNA damage response (DDR (zeige DDR1 Proteine)) 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.

Mouse (Murine) Fused in Sarcoma (FUS) Interaktionspartner

  1. FUS and the ELAV (zeige ELAVL4 Proteine)-like proteins ELAVL4 (zeige ELAVL4 Proteine) and ELAVL1 (zeige ELAVL1 Proteine) control SynGAP (zeige SYNGAP1 Proteine) mRNA stability in a 3'UTR length-dependent manner, resulting in the stable expression of the alternatively spliced SynGAP (zeige SYNGAP1 Proteine) isoform alpha2.

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

  3. Study established that Fus1 (zeige TUSC2 Proteine) 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 (zeige TUSC2 Proteine) loss-mediated mitochondrial dysfunction, and identify the target cells and tissues in the inner ear.

  4. Authors found that FUS, EWS (zeige EWSR1 Proteine) and TAF15 (zeige TAF15 Proteine) 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 (zeige EWSR1 Proteine) during neuronal differentiation.

  5. 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.

  6. 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 (zeige FTL Proteine).

  7. 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.

  8. 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.

  9. These results highlight the pivotal role of FUS in regulating GluA1 (zeige GRIA1 Proteine) mRNA stability, post-synaptic function and fronto-temporal lobar degeneration-like animal behaviors.

  10. 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.

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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