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FUS encodes a multifunctional protein component of the heterogeneous nuclear ribonucleoprotein (hnRNP) complex. Additionally we are shipping FUS Kits (10) and FUS Proteins (7) and many more products for this protein.
Showing 10 out of 120 products:
Human Polyclonal FUS Primary Antibody for ICC, IF - ABIN151997
Neumann, Rademakers, Roeber, Baker, Kretzschmar, Mackenzie: A new subtype of frontotemporal lobar degeneration with FUS pathology. in Brain : a journal of neurology 2009
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Human Polyclonal FUS Primary Antibody for ICC, IF - ABIN151993
Hume, Sasmono, Himes, Sharma, Bronisz, Constantin, Ostrowski, Ross: The Ewing sarcoma protein (EWS) binds directly to the proximal elements of the macrophage-specific promoter of the CSF-1 receptor (csf1r) gene. in Journal of immunology (Baltimore, Md. : 1950) 2008
Show all 7 references for ABIN151993
Human Monoclonal FUS Primary Antibody for IF, WB - ABIN968508
Hallier, Lerga, Barnache, Tavitian, Moreau-Gachelin: The transcription factor Spi-1/PU.1 interacts with the potential splicing factor TLS. in The Journal of biological chemistry 1998
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Human Polyclonal FUS Primary Antibody for ICC, IF - ABIN251039
Vance, Scotter, Nishimura, Troakes, Mitchell, Kathe, Urwin, Manser, Miller, Hortobágyi, Dragunow, Rogelj, Shaw: ALS mutant FUS disrupts nuclear localization and sequesters wild-type FUS within cytoplasmic stress granules. in Human molecular genetics 2013
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Human Polyclonal FUS Primary Antibody for ICC, IF - ABIN151994
Tan, Manley: TLS inhibits RNA polymerase III transcription. in Molecular and cellular biology 2009
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Human Polyclonal FUS Primary Antibody for EIA, FACS - ABIN952406
Kim, Shanware, Bowler, Tibbetts: Amyotrophic lateral sclerosis-associated proteins TDP-43 and FUS/TLS function in a common biochemical complex to co-regulate HDAC6 mRNA. in The Journal of biological chemistry 2010
Show all 2 references for ABIN952406
Chicken Polyclonal FUS Primary Antibody for IHC, WB - ABIN2778717
Sato, Idogawa, Honda, Fujii, Kawashima, Takekuma, Hoshika, Hirohashi, Yamada: Beta-catenin interacts with the FUS proto-oncogene product and regulates pre-mRNA splicing. in Gastroenterology 2005
A subset of juvenile-onset familial/sporadic ALS (show IGFALS Antibodies) cases with FUS gene mutations reportedly demonstrates mental retardation or learning difficulty.
Study implicates phosphorylation as an additional mechanism by which nuclear transport of FUS might be regulated and potentially perturbed in ALS and FTLD.
prevalence of the FUS-ERG (show ERG Antibodies) gene fusion in a large cohort of pathologically and molecularly well characterized small blue round cell tumors, lacking other known gene rearrangements
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 Antibodies) (i.e. FUS, TDP-43 (show TARDBP Antibodies) and SOD1 (show SOD1 Antibodies))
RNA binding proteins TDP-43 (show TARDBP Antibodies) and FUS do not consistently fit the currently characterised inclusion models suggesting that cells have a larger repertoire for generating inclusions than currently thought.
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.
FUS and EWS (show EWSR1 Antibodies) target genes involved in pathways at the RNA regulatory level
FUS mutation seems indicated in sporadic early-onset ALS patients especially if showing predominant bulbar symptoms and an aggressive disease course.
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
FUS-DDIT3 (show DDIT3 Antibodies) 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.
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.
These results highlight the pivotal role of FUS in regulating GluA1 (show GRIA1 Antibodies) mRNA stability, post-synaptic function and fronto-temporal lobar degeneration-like animal behaviors.
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/TLS depletion causes phenotypes possibly related to neuropsychiatric and neurodegenerative conditions, but distinct from ALS and ET, together with specific alterations in RNA metabolisms.
It is associated with amyotrophic lateral sclerosis and its mutation causes accumulation of fus positive stress granules in neurons.
Study provides evidence for loss of PRMT1 (show PRMT1 Antibodies) 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.
our study provided evidence that a multistep process of FUS aggregation in the cell cytoplasm includes RNA-dependent and RNA-independent mechanisms.
Activation of metabotropic glutamate (show GRIN1 Antibodies) receptors 1/5 in neocortical slices and isolated synaptoneurosomes increases endogenous mouse FUS and FUS(WT) protein levels but decreases the FUS(R521G) protein
Study shows that neuronal aggregates formed by mutant FUS protein may aberrantly sequester survival motor neuron protein (SMN (show SMN1 Antibodies)) and concomitantly cause a reduction of SMN (show STMN1 Antibodies) levels in the axon, leading to axonal defects.
FUS is a coregulator of MITF (show MITF Antibodies) activity and provide new insights into how the RANKL (show TNFSF11 Antibodies)/p38 MAPK (show MAPK14 Antibodies) signaling nexus controls gene expression in osteoclasts.
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.
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 (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