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SAB4200478

Sigma-Aldrich

Monoclonal Anti-FUS antibody produced in mouse

clone FUS-4, tissue culture supernatant

Synonym(s):

Monoclonal Anti-75 kDa DNA-pairing protein, Monoclonal Anti-ALS6, Monoclonal Anti-FUS1, Monoclonal Anti-HNRNPP2, Monoclonal Anti-POMP75, Monoclonal Anti-TLS, Monoclonal Anti-fused in sarcoma, Monoclonal Anti-fusion gene in myxoid liposarcoma, Monoclonal Anti-heterogeneous nuclear ribonucleoprotein P2, Monoclonal Anti-translocated in liposarcoma protein

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About This Item

UNSPSC Code:
12352203
NACRES:
NA.41

biological source

mouse

Quality Level

200

conjugate

unconjugated

antibody form

tissue culture supernatant

antibody product type

primary antibodies

clone

FUS-4, monoclonal

form

buffered aqueous solution

mol wt

antigen ~70 kDa

species reactivity

mouse, human, rat

technique(s)

immunohistochemistry: 1:500-1:1000 using formalin-fixed and paraffin embedded rat cerebellum.
indirect immunofluorescence: 1:200-1:400 using using HeLa or HepG2 cells.
western blot: 1:1000-1:2000 using lysates of G361 cells.

isotype

IgM

UniProt accession no.

P35637

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... FUS(2521)
mouse ... Fus(233908)
rat ... Fus(317385)

General description

Monoclonal Anti-FUS (mouse IgM isotype) is derived from the hybridoma FUS-4 produced by the fusion of mouse myeloma cells and splenocytes from BALB/c mice immunized with a synthetic peptide corresponding to an internal sequence of human FUS, conjugated to KLH. Fused in sarcoma (FUS), also known as translocated in liposarcoma (TLS), ribonucleoprotein (RNP)-P2, amyotrophic lateral sclerosis-6 (ALS6), is a RNA/DNA binding protein. FUS is normally located predominantly in the nucleus whereas, pathological FUS inclusions are mostly found in the cytosol of neurons and glia cells.

Immunogen

synthetic peptide corresponding to an internal sequence of human FUS, conjugated to KLH. The corresponding sequence is identical in monkey and differs by 3 amino acids in mouse and rat.

Application

Monoclonal Anti-FUS antibody produced in mouse has been used in various immunochemical techniques including:
  • immunoblotting
  • immunofluorescence
  • immunohistochemistry

Biochem/physiol Actions

Fused in sarcoma (FUS) plays a vital role in transcription, RNA splicing and transport and is implicated in multiple diseases. Mutations in TAR DNA binding protein 43 (TDP-43) and FUS is associated with the development of amyotrophic lateral sclerosis (ALS) and fronto-temporal lobar degeneration (FLTD) including ubiquitin-positive inclusions (FLTDU). The majority of the FUS mutations has been recognized in C-terminal nuclear localization signal (NLS). FUS has been implicated in a broadening spectrum of neurodegenerative disorders. FUS has been identified as a component of inclusion bodies in patients with Huntington′s disease (HD) and spinocerebellar ataxias (SCA1-3).

Physical form

Culture supernatant solution containing 15 mM sodium azide.

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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wgk_germany

WGK 2

flash_point_f

Not applicable

flash_point_c

Not applicable

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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ALS/FTD-linked mutation in FUS suppresses intra-axonal protein synthesis and drives disease without nuclear loss-of-function of FUS
Lopez-Erauskin J, et al.
Neuron, 100(4), 816-830 (2018)
TDP-43 and FUS/TLS: emerging roles in RNA processing and neurodegeneration
Lagier-Tourenne C, et al.
Human Molecular Genetics, 19(R1), R46-R64 (2010)
TDP-43 and FUS in amyotrophic lateral sclerosis and frontotemporal dementia
Mackenzie IRA, et al.
Lancet Neurology, 9(10), 995-1007 (2010)
Gain of Additional BIRC3 Protein Functions through xn-3-t6a-UTR-Mediated Protein Complex Formation
Lee SH and Mayr C
Molecular Cell, 74(4), 701-712 (2019)
A Membraneless Organelle Associated with the Endoplasmic Reticulum Enables 3'UTR-Mediated Protein-Protein Interactions
Ma W and Mayr C
Cell, 175(6), 1492-1506 (2018)
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