Fused in Sarcoma Proteins (FUS)

FUS encodes a multifunctional protein component of the heterogeneous nuclear ribonucleoprotein (hnRNP) complex. Additionally we are shipping FUS Antibodies (40) and FUS Kits (3) and many more products for this protein.

list all proteins Gene Name GeneID UniProt
FUS 2521 P35637
Mouse FUS FUS 233908 P56959
Rat FUS FUS 317385  
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Top FUS Proteins at antibodies-online.com

Showing 2 out of 2 products:

Catalog No. Origin Source Conjugate Images Quantity Supplier Delivery Price Details
HEK-293 Cells Human Myc-DYKDDDDK Tag Validation with Western Blot 20 μg Log in to see 2 to 3 Days
Escherichia coli (E. coli) Human GST tag Fused in Sarcoma (FUS) (AA 1-198), (partial) protein (GST tag) 1 mg Log in to see 60 to 71 Days

FUS Proteins by Origin and Source

Origin Expressed in Conjugate
Human ,

Top referenced FUS Proteins

  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

More Proteins for Fused in Sarcoma (FUS) Interaction Partners

Human Fused in Sarcoma (FUS) interaction partners

  1. In human stem (show TAF15 Proteins) cell-derived motor neurons, the RNA profile associated with concomitant loss of both TAF15 and FUS resembles that observed in the (show TAF15 Proteins)presence of the amyotrophic lateral sclerosis (ALS)-associated mutation FUS R521G, but co (show TARDBP Proteins)ntrasts with late-stage sporadic ALS patients.

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

  3. 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.

  4. 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.

  5. activation of the IGF-IR/PI3K (show PIK3CA Proteins)/Akt (show AKT1 Proteins) 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 (show DDIT3 Proteins)-dependent manner.

  6. 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.

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

  8. 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.

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

  10. 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 (show CDH23 Proteins) in mainland China is another genetic feature distinct from Caucasians.

Mouse (Murine) Fused in Sarcoma (FUS) interaction partners

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

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

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

  4. Study established that Fus1 (show TUSC2 Proteins) 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 (show TUSC2 Proteins) loss-mediated mitochondrial dysfunction, and identify the target cells and tissues in the inner ear.

  5. Authors found that FUS, EWS (show EWSR1 Proteins) and TAF15 (show TAF15 Proteins) 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 (show EWSR1 Proteins) during neuronal differentiation.

  6. 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.

  7. 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 (show FTL Proteins).

  8. 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.

  9. 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.

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

FUS Protein Profile

Protein Summary

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.

Gene names and symbols associated with Fused in Sarcoma Proteins (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

Protein level used designations for Fused in Sarcoma Proteins (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

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