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Key Documents

HPA008784

Sigma-Aldrich

Anti-FUS antibody produced in rabbit

enhanced validation

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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About This Item

UNSPSC Code:
12352203
Human Protein Atlas Number:
NACRES:
NA.41

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:
  • 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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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)
Leone Chare et al.
Journal of neurology, neurosurgery, and psychiatry, 85(8), 865-870 (2014-01-15)
To assess the impact of new clinical diagnostic criteria for frontotemporal dementia (FTD) syndromes, including primary progressive aphasias (PPA), on prior clinical diagnosis and to explore clinicopathological correlations. 178 consecutive neuropathologically ascertained cases initially diagnosed with a FTD syndrome were
Swikrity Upadhyay Baskota et al.
Laboratory investigation; a journal of technical methods and pathology, 99(7), 1068-1077 (2018-12-24)
Huntington's disease (HD) is an autosomal dominant disorder caused by a trinucleotide expansion in the huntingtin gene. Recently, a new role for tau has been implicated in the pathogenesis of HD, whereas others have argued that postmortem tau pathology findings
Dhruva Deshpande et al.
Frontiers in cellular neuroscience, 13, 256-256 (2019-06-28)
Mutations in the fused in Sarcoma (FUS) gene induce cytoplasmic FUS aggregations, contributing to the neurodegenerative disease amyotrophic lateral sclerosis (ALS) in certain cases. While FUS is mainly a nuclear protein involved in transcriptional processes with limited cytoplasmic functions, it
Manuela Neumann et al.
Acta neuropathologica, 118(5), 605-616 (2009-08-12)
Neuronal intermediate filament inclusion disease (NIFID) is an uncommon neurodegenerative condition that typically presents as early-onset, sporadic frontotemporal dementia (FTD), associated with a pyramidal and/or extrapyramidal movement disorder. The neuropathology is characterized by frontotemporal lobar degeneration with neuronal inclusions that

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