HPA008784
Anti-FUS antibody produced in rabbit
Prestige Antibodies® Powered by Atlas Antibodies, affinity isolated antibody, buffered aqueous glycerol solution
Synonym(s):
Anti-ALS6, Anti-FUS1, Anti-HNRNPP2, Anti-TLS, Anti-hnRNP-P2
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All Photos(9)
About This Item
Recommended Products
biological source
rabbit
Quality Level
conjugate
unconjugated
antibody form
affinity isolated antibody
antibody product type
primary antibodies
clone
polyclonal
product line
Prestige Antibodies® Powered by Atlas Antibodies
form
buffered aqueous glycerol solution
species reactivity
mouse, rat, human
enhanced validation
RNAi knockdown
orthogonal RNAseq
Learn more about Antibody Enhanced Validation
technique(s)
immunoblotting: 0.04-0.4 μg/mL
immunofluorescence: 0.25-2 μg/mL
immunohistochemistry: 1:1000-1:2500
immunogen sequence
SSQSSYGQQSSYPGYGQQPAPSSTSGSYGSSSQSSSYGQPQSGSYSQQPSYGGQQQSYGQQQSYNPPQGYGQQNQYNSSSGGGGGGGGGGNYGQDQSSMSSGGGSGGGYGNQDQSGGGGSGGYGQQDR
UniProt accession no.
shipped in
wet ice
storage temp.
−20°C
target post-translational modification
unmodified
Gene Information
human ... FUS(2521)
General description
FUS (fused in sarcoma) is a DNA/RNA binding protein, which contains a nuclear localization sequence in its C-terminal. A QGSY (glutamine-glycine-serine-tyrosine)-rich region is localized to its N-terminal, which plays an essential role in the self-assembly of this protein. It was first identified in liposarcomas as a fusion protein.
Immunogen
FUS RNA binding protein
Application
Anti-FUS antibody produced in rabbit, a Prestige Antibody, is developed and validated by the Human Protein Atlas (HPA) project . Each antibody is tested by immunohistochemistry against hundreds of normal and disease tissues. These images can be viewed on the Human Protein Atlas (HPA) site by clicking on the Image Gallery link. The antibodies are also tested using immunofluorescence and western blotting. To view these protocols and other useful information about Prestige Antibodies and the HPA, visit sigma.com/prestige.
Biochem/physiol Actions
Mutations in FUS (fused in sarcoma) gene result in a subset of familial amyotrophic lateral sclerosis (ALS). This disease is characterized by the accumulation of FUS aggregates in the cytosol due to mutations clustered in its nuclear localization sequence. This protein is multifunctional and plays multiple roles in the metabolism of RNA. In liposarcomas, the N-terminal of this protein fuses with the N-terminal of the CHOP (CCAAT-enhancer-binding protein homologous protein) transcription factor, which results in tumorigenesis through the activation of oncogenes. This protein is associated with the pathogenesis of neurodegeneration, and its inactivation influences the homeostasis of cells. Inactivation of this protein leads to an elevation in the phosphorylation og histone H3, which leads to cell arrest, thus, impacting cell proliferation.
Features and Benefits
Prestige Antibodies® are highly characterized and extensively validated antibodies with the added benefit of all available characterization data for each target being accessible via the Human Protein Atlas portal linked just below the product name at the top of this page. The uniqueness and low cross-reactivity of the Prestige Antibodies® to other proteins are due to a thorough selection of antigen regions, affinity purification, and stringent selection. Prestige antigen controls are available for every corresponding Prestige Antibody and can be found in the linkage section.
Every Prestige Antibody is tested in the following ways:
Every Prestige Antibody is tested in the following ways:
- IHC tissue array of 44 normal human tissues and 20 of the most common cancer type tissues.
- Protein array of 364 human recombinant protein fragments.
Linkage
Corresponding Antigen APREST86697
Physical form
Solution in phosphate-buffered saline, pH 7.2, containing 40% glycerol and 0.02% sodium azide
Legal Information
Prestige Antibodies is a registered trademark of Merck KGaA, Darmstadt, Germany
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
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Storage Class Code
10 - Combustible liquids
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
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Carol Dobson-Stone et al.
Acta neuropathologica, 125(4), 523-533 (2013-01-23)
Numerous families exhibiting both frontotemporal dementia (FTD) and amyotrophic lateral sclerosis (ALS) have been described, and although many of these have been shown to harbour a repeat expansion in C9ORF72, several C9ORF72-negative FTD-ALS families remain. We performed neuropathological and genetic
Liuqing Yang et al.
Proceedings of the National Academy of Sciences of the United States of America, 111(50), 17809-17814 (2014-12-03)
Amyotrophic lateral sclerosis (ALS) is a progressive neurodegenerative disease. Fused in sarcoma (FUS) is a DNA/RNA binding protein and mutations in FUS cause a subset of familial ALS. Most ALS mutations are clustered in the C-terminal nuclear localization sequence of
Very early-onset frontotemporal dementia with no family history predicts underlying fused in sarcoma pathology.
Clement T Loy et al.
Brain : a journal of neurology, 133(Pt 12), e158-e158 (2010-08-10)
Hazel Urwin et al.
Acta neuropathologica, 120(1), 33-41 (2010-05-22)
Through an international consortium, we have collected 37 tau- and TAR DNA-binding protein 43 (TDP-43)-negative frontotemporal lobar degeneration (FTLD) cases, and present here the first comprehensive analysis of these cases in terms of neuropathology, genetics, demographics and clinical data. 92%
Han-Xiang Deng et al.
Annals of neurology, 67(6), 739-748 (2010-06-03)
Amyotrophic lateral sclerosis (ALS) is a fatal disorder of motor neuron degeneration. Most cases of ALS are sporadic (SALS), but about 5 to 10% of ALS cases are familial (FALS). Recent studies have shown that mutations in FUS are causal
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