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Fused in Sarcoma Proteins (FUS)

FUS encodes a multifunctional protein component of the heterogeneous nuclear ribonucleoprotein (hnRNP) complex. Additionally we are shipping FUS Antibodies (116) and FUS Kits (10) and many more products for this protein.

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

Showing 7 out of 7 products:

Catalog No. Origin Source Conjugate Images Quantity Supplier Delivery Price Details
HOST_Escherichia coli (E. coli) Mouse His tag „Crystallography Grade“ protein due to multi-step, protein-specific purification process 1 mg Log in to see 29 to 34 Days
$4,331.68
Details
HOST_Escherichia coli (E. coli) Human His tag „Crystallography Grade“ protein due to multi-step, protein-specific purification process 1 mg Log in to see 29 to 34 Days
$4,331.68
Details
HOST_Escherichia coli (E. coli) Human GST tag 50 μg Log in to see 21 to 26 Days
$341.00
Details
Yeast Human respiratory syncytial virus B His tag 50 μg Log in to see 31 to 36 Days
$341.00
Details
HOST_Escherichia coli (E. coli) Human GST tag Fused in Sarcoma (FUS) (AA 1-198), (partial) protein (GST tag) 1 mg Log in to see 56 to 66 Days
$1,842.50
Details
HOST_Escherichia coli (E. coli) Human Un-conjugated   50 μg Log in to see 16 to 21 Days
$314.29
Details
HOST_Human Human Un-conjugated   20 μg Log in to see 19 Days
$785.40
Details

FUS Proteins by Origin and Source

Origin Expressed in Conjugate
Human ,
,
Mouse (Murine)

More Proteins for Fused in Sarcoma (FUS) Interaction Partners

Human Fused in Sarcoma (FUS) interaction partners

  1. A subset of juvenile-onset familial/sporadic ALS (show IGFALS Proteins) cases with FUS gene mutations reportedly demonstrates mental retardation or learning difficulty.

  2. Study implicates phosphorylation as an additional mechanism by which nuclear transport of FUS might be regulated and potentially perturbed in ALS and FTLD.

  3. prevalence of the FUS-ERG (show ERG Proteins) gene fusion in a large cohort of pathologically and molecularly well characterized small blue round cell tumors, lacking other known gene rearrangements

  4. Study identifies a common mechanism of transport into neurites of proteins linked to the pathology of Alzheimer's disease (i.e. sAPP) and ALS (show IGFALS Proteins) (i.e. FUS, TDP-43 (show TARDBP Proteins) and SOD1 (show SOD1 Proteins))

  5. RNA binding proteins TDP-43 (show TARDBP Proteins) and FUS do not consistently fit the currently characterised inclusion models suggesting that cells have a larger repertoire for generating inclusions than currently thought.

  6. FUS-ERG is a transcriptional repressor of retinoic acid signaling. It acts in the context of a heptad of proteins (ERG, FLI1, GATA2, LYL1, LMO2, RUNX1 and TAL1) central to proper expression of genes maintaining a hematopoietic stem cell phenotype.

  7. FUS and EWS (show EWSR1 Proteins) target genes involved in pathways at the RNA regulatory level

  8. FUS mutation seems indicated in sporadic early-onset ALS patients especially if showing predominant bulbar symptoms and an aggressive disease course.

  9. Results demonstrate that ALS-mutant forms of TDP-43, FUS, and SOD1 all perturb protein transport in the early secretory pathway between ER and Golgi compartments, and imply that restoring Rab1-mediated ER-Golgi transport is a novel ALS therapeutic target

  10. FUS-DDIT3 (show DDIT3 Proteins) is uniquely regulated at the transcriptional as well as the post-translational level and that its expression level is important for myxoid liposarcoma tumour development.

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

  1. 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.

  2. 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.

  3. 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.

  4. 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.

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

  6. Study provides evidence for loss of PRMT1 (show PRMT1 Proteins) 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.

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

  8. Activation of metabotropic glutamate (show GRIN1 Proteins) receptors 1/5 in neocortical slices and isolated synaptoneurosomes increases endogenous mouse FUS and FUS(WT) protein levels but decreases the FUS(R521G) protein

  9. Study shows that neuronal aggregates formed by mutant FUS protein may aberrantly sequester survival motor neuron protein (SMN (show SMN1 Proteins)) and concomitantly cause a reduction of SMN (show STMN1 Proteins) levels in the axon, leading to axonal defects.

  10. FUS is a coregulator of MITF (show MITF Proteins) activity and provide new insights into how the RANKL (show TNFSF11 Proteins)/p38 MAPK (show MAPK14 Proteins) signaling nexus controls gene expression in osteoclasts.

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)

  • fused in sarcoma (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

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