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  
Direkt bei antikoerper-online bestellen
  • +1 877 302 8632
  • +1 888 205 9894 (toll-free)
  • Online bestellen
  • orders@antikoerper-online.de

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

  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.

  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.

  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.

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

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

  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.

  8. Fus is a binding partner of FMRP.

  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.

  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.

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

  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.

  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.

  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.

  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.

  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.

  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.

  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

  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.

  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.

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
Ausgewählte Anbieter für FUS Proteine (FUS)
Haben Sie etwas anderes gesucht?