biological source
mouse
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.
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
Gene Information
human ... FUS(2521)
mouse ... Fus(233908)
rat ... Fus(317385)
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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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存储类别
10 - Combustible liquids
wgk
WGK 2
flash_point_f
Not applicable
flash_point_c
Not applicable
法规信息
新产品
此项目有
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 in amyotrophic lateral sclerosis and frontotemporal dementia
Mackenzie IRA, et al.
Lancet Neurology, 9(10), 995-1007 (2010)
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)
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)
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)
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