This webpage contains legacy information. The product is either no longer available from the supplier or has been delisted at Labome.
product summary
company name :
Proteintech Group
product type :
antibody
product name :
FUS/TLS
catalog :
11570-1-AP
quantity :
150UL
price :
299 USD
clonality :
polyclonal
host :
domestic rabbit
conjugate :
nonconjugated
reactivity :
human, mouse
application :
western blot, ELISA, immunohistochemistry, immunocytochemistry, immunoprecipitation, flow cytometry, chromatin immunoprecipitation, RNA immunoprecipitation
citations: 43
Published Application/Species/Sample/DilutionReference
  • western blot; mouse; 1:1000; loading ...; fig 1d
Yasuda K, Clatterbuck Soper S, Jackrel M, Shorter J, Mili S. FUS inclusions disrupt RNA localization by sequestering kinesin-1 and inhibiting microtubule detyrosination. J Cell Biol. 2017;216:1015-1034 pubmed publisher
Zhu Y, Liu Y, Yang F, Chen W, Jiang J, He P, et al. All-Trans Retinoic Acid Exerts Neuroprotective Effects in Amyotrophic Lateral Sclerosis-Like Tg (SOD1*G93A)1Gur Mice. Mol Neurobiol. 2020;57:3603-3615 pubmed publisher
Pourhaghighi R, Ash P, Phanse S, Goebels F, Hu L, Chen S, et al. BraInMap Elucidates the Macromolecular Connectivity Landscape of Mammalian Brain. Cell Syst. 2020;10:333-350.e14 pubmed publisher
Han K, Wang F, Cao C, Ling H, Chen J, Chen R, et al. CircLONP2 enhances colorectal carcinoma invasion and metastasis through modulating the maturation and exosomal dissemination of microRNA-17. Mol Cancer. 2020;19:60 pubmed publisher
Ikenaka K, Ishigaki S, Iguchi Y, Kawai K, Fujioka Y, Yokoi S, et al. Characteristic Features of FUS Inclusions in Spinal Motor Neurons of Sporadic Amyotrophic Lateral Sclerosis. J Neuropathol Exp Neurol. 2020;79:370-377 pubmed publisher
Kuta R, Larochelle N, Fernandez M, Pal A, Minotti S, Tibshirani M, et al. Depending on the stress, histone deacetylase inhibitors act as heat shock protein co-inducers in motor neurons and potentiate arimoclomol, exerting neuroprotection through multiple mechanisms in ALS models. Cell Stress Chaperones. 2020;25:173-191 pubmed publisher
Shelkovnikova T, An H, Skelt L, Tregoning J, Humphreys I, Buchman V. Antiviral Immune Response as a Trigger of FUS Proteinopathy in Amyotrophic Lateral Sclerosis. Cell Rep. 2019;29:4496-4508.e4 pubmed publisher
Casci I, Krishnamurthy K, Kour S, Tripathy V, Ramesh N, Anderson E, et al. Muscleblind acts as a modifier of FUS toxicity by modulating stress granule dynamics and SMN localization. Nat Commun. 2019;10:5583 pubmed publisher
Picchiarelli G, Demestre M, Zuko A, Been M, Higelin J, Dieterlé S, et al. FUS-mediated regulation of acetylcholine receptor transcription at neuromuscular junctions is compromised in amyotrophic lateral sclerosis. Nat Neurosci. 2019;22:1793-1805 pubmed publisher
Rossaert E, Pollari E, Jaspers T, Van Helleputte L, Jarpe M, Van Damme P, et al. Restoration of histone acetylation ameliorates disease and metabolic abnormalities in a FUS mouse model. Acta Neuropathol Commun. 2019;7:107 pubmed publisher
Shi X, Wang X. LINC00473 mediates cyclin D1 expression through a balance between activation and repression signals in breast cancer cells. FEBS Lett. 2019;593:751-759 pubmed publisher
Baron D, Matheny T, Lin Y, Leszyk J, Kenna K, Gall K, et al. Quantitative proteomics identifies proteins that resist translational repression and become dysregulated in ALS-FUS. Hum Mol Genet. 2019;: pubmed publisher
He Z, Ruan X, Liu X, Zheng J, Liu Y, Liu L, et al. FUS/circ_002136/miR-138-5p/SOX13 feedback loop regulates angiogenesis in Glioma. J Exp Clin Cancer Res. 2019;38:65 pubmed publisher
Withers J, Li E, Vallery T, Yario T, Steitz J. Two herpesviral noncoding PAN RNAs are functionally homologous but do not associate with common chromatin loci. PLoS Pathog. 2018;14:e1007389 pubmed publisher
López Erauskin J, Tadokoro T, Baughn M, Myers B, McAlonis Downes M, Chillon Marinas C, et al. ALS/FTD-Linked Mutation in FUS Suppresses Intra-axonal Protein Synthesis and Drives Disease Without Nuclear Loss-of-Function of FUS. Neuron. 2018;100:816-830.e7 pubmed publisher
Wang H, Guo W, Mitra J, Hegde P, Vandoorne T, Eckelmann B, et al. Mutant FUS causes DNA ligation defects to inhibit oxidative damage repair in Amyotrophic Lateral Sclerosis. Nat Commun. 2018;9:3683 pubmed publisher
Xiong D, Wu Y, Jin C, Li J, Gu J, Liao Y, et al. Elevated FUS/TLS expression is negatively associated with E-cadherin expression and prognosis of patients with non-small cell lung cancer. Oncol Lett. 2018;16:1791-1800 pubmed publisher
Shelkovnikova T, Kukharsky M, An H, Dimasi P, Alexeeva S, Shabir O, et al. Protective paraspeckle hyper-assembly downstream of TDP-43 loss of function in amyotrophic lateral sclerosis. Mol Neurodegener. 2018;13:30 pubmed publisher
Guo L, Kim H, Wang H, Monaghan J, Freyermuth F, Sung J, et al. Nuclear-Import Receptors Reverse Aberrant Phase Transitions of RNA-Binding Proteins with Prion-like Domains. Cell. 2018;173:677-692.e20 pubmed publisher
Cykowski M, Powell S, Appel J, Arumanayagam A, Rivera A, Appel S. Phosphorylated TDP-43 (pTDP-43) aggregates in the axial skeletal muscle of patients with sporadic and familial amyotrophic lateral sclerosis. Acta Neuropathol Commun. 2018;6:28 pubmed publisher
Mitsuhashi H, Ishimaru S, Homma S, Yu B, Honma Y, Beermann M, et al. Functional domains of the FSHD-associated DUX4 protein. Biol Open. 2018;7: pubmed publisher
Kahl A, Blanco I, Jackman K, Baskar J, Milaganur Mohan H, Rodney Sandy R, et al. Cerebral ischemia induces the aggregation of proteins linked to neurodegenerative diseases. Sci Rep. 2018;8:2701 pubmed publisher
Irwin D, McMillan C, Xie S, Rascovsky K, Van Deerlin V, Coslett H, et al. Asymmetry of post-mortem neuropathology in behavioural-variant frontotemporal dementia. Brain. 2018;141:288-301 pubmed publisher
Kovacs G, Kwong L, Grossman M, Irwin D, Lee E, Robinson J, et al. Tauopathy with hippocampal 4-repeat tau immunoreactive spherical inclusions: a report of three cases. Brain Pathol. 2018;28:274-283 pubmed publisher
Lyons S, Gudanis D, Coyne S, Gdaniec Z, Ivanov P. Identification of functional tetramolecular RNA G-quadruplexes derived from transfer RNAs. Nat Commun. 2017;8:1127 pubmed publisher
Lo Bello M, Di Fini F, Notaro A, Spataro R, Conforti F, La Bella V. ALS-Related Mutant FUS Protein Is Mislocalized to Cytoplasm and Is Recruited into Stress Granules of Fibroblasts from Asymptomatic FUS P525L Mutation Carriers. Neurodegener Dis. 2017;17:292-303 pubmed publisher
Tibshirani M, Zhao B, Gentil B, Minotti S, Marques C, Keith J, et al. Dysregulation of chromatin remodelling complexes in amyotrophic lateral sclerosis. Hum Mol Genet. 2017;26:4142-4152 pubmed publisher
Hawley Z, Campos Melo D, Strong M. Novel miR-b2122 regulates several ALS-related RNA-binding proteins. Mol Brain. 2017;10:46 pubmed publisher
Shelkovnikova T, Dimasi P, Kukharsky M, An H, Quintiero A, Schirmer C, et al. Chronically stressed or stress-preconditioned neurons fail to maintain stress granule assembly. Cell Death Dis. 2017;8:e2788 pubmed publisher
Scekic Zahirovic J, Oussini H, Mersmann S, Drenner K, Wagner M, Sun Y, et al. Motor neuron intrinsic and extrinsic mechanisms contribute to the pathogenesis of FUS-associated amyotrophic lateral sclerosis. Acta Neuropathol. 2017;133:887-906 pubmed publisher
Kar A, Vargas J, Chen C, Kowalak J, Gioio A, Kaplan B. Molecular determinants of cytochrome C oxidase IV mRNA axonal trafficking. Mol Cell Neurosci. 2017;80:32-43 pubmed publisher
Homma S, Beermann M, Yu B, BOYCE F, Miller J. Nuclear bodies reorganize during myogenesis in vitro and are differentially disrupted by expression of FSHD-associated DUX4. Skelet Muscle. 2016;6:42 pubmed
Chen Y, Deng J, Wang P, Yang M, Chen X, Zhu L, et al. PINK1 and Parkin are genetic modifiers for FUS-induced neurodegeneration. Hum Mol Genet. 2016;25:5059-5068 pubmed publisher
Kapeli K, Pratt G, Vu A, Hutt K, Martinez F, Sundararaman B, et al. Distinct and shared functions of ALS-associated proteins TDP-43, FUS and TAF15 revealed by multisystem analyses. Nat Commun. 2016;7:12143 pubmed publisher
Van den Bossche T, Sleegers K, Cuyvers E, Engelborghs S, Sieben A, De Roeck A, et al. Phenotypic characteristics of Alzheimer patients carrying an ABCA7 mutation. Neurology. 2016;86:2126-33 pubmed publisher
Schoen M, Reichel J, Demestre M, Putz S, Deshpande D, Proepper C, et al. Super-Resolution Microscopy Reveals Presynaptic Localization of the ALS/FTD Related Protein FUS in Hippocampal Neurons. Front Cell Neurosci. 2015;9:496 pubmed publisher
Lim S, Choi W, Oh K, Xue Y, Choi J, Kim S, et al. Directly converted patient-specific induced neurons mirror the neuropathology of FUS with disrupted nuclear localization in amyotrophic lateral sclerosis. Mol Neurodegener. 2016;11:8 pubmed publisher
He J, Huang L, Qiu H, Li J, Luo L, Li Y, et al. A new design of a lentiviral shRNA vector with inducible co-expression of ARGONAUTE 2 for enhancing gene silencing efficiency. Cell Biosci. 2015;5:67 pubmed publisher
Muresan V, Ladescu Muresan Z. Shared Molecular Mechanisms in Alzheimer's Disease and Amyotrophic Lateral Sclerosis: Neurofilament-Dependent Transport of sAPP, FUS, TDP-43 and SOD1, with Endoplasmic Reticulum-Like Tubules. Neurodegener Dis. 2016;16:55-61 pubmed publisher
King A, Troakes C, Smith B, Nolan M, Curran O, Vance C, et al. ALS-FUS pathology revisited: singleton FUS mutations and an unusual case with both a FUS and TARDBP mutation. Acta Neuropathol Commun. 2015;3:62 pubmed publisher
Robinson H, Deykin A, Bronovitsky E, Ovchinnikov R, Ustyugov A, Shelkovnikova T, et al. Early lethality and neuronal proteinopathy in mice expressing cytoplasm-targeted FUS that lacks the RNA recognition motif. Amyotroph Lateral Scler Frontotemporal Degener. 2015;16:402-9 pubmed publisher
Bakkar N, Kousari A, Kovalik T, Li Y, Bowser R. RBM45 Modulates the Antioxidant Response in Amyotrophic Lateral Sclerosis through Interactions with KEAP1. Mol Cell Biol. 2015;35:2385-99 pubmed publisher
Tibshirani M, Tradewell M, Mattina K, Minotti S, Yang W, Zhou H, et al. Cytoplasmic sequestration of FUS/TLS associated with ALS alters histone marks through loss of nuclear protein arginine methyltransferase 1. Hum Mol Genet. 2015;24:773-86 pubmed publisher
product information
CatalogNo :
11570-1-AP
AntigenName :
FUS/TLS
Package :
150UL
Price :
299 USD
Exsists20ul :
20ul trial size available
FullName :
fusion (involved in t(12;16) in malignant liposarcoma)
Immunogen :
Recombinant Protein
Species :
human, mouse, rat
Host :
Rabbit
IsConjugated :
Unconjugated
AntigenSpecies :
human
Application :
WB, RIP, IP, IHC, IF, FC, chIP, ELISA
Clonlity :
Polyclonal
IsoType :
IgG
Synonyms :
75 kDa DNA pairing protein, FUS, FUS1, FUS-CHOP, hnRNP P2, Oncogene FUS, Oncogene TLS, POMp75, RNA binding protein FUS, TLS, TLS/CHOP
PrimaryOrSecondary :
Primary
AntibodyBuffer :
PBS with 0.1% sodium azide and 50% glycerol pH 7.3.
GenBankNo :
BC026062
Category :
Binding Proteins;Cytoskeleton/Scaffold Proteins;Neurology;Oncogene(s) and Tumor Suppressor(s);
PurifyMethod :
Antigen affinity purification
NewAb :
False
IsSellable :
True
Feature :
siRNA
AppTiter :
FC 1:0 ; IF 1:50 ; IHC 1:200 ; IP 1:1000 ; WB 1:2000 ;
company information
Proteintech Group
2201 W. Campbell Park Dr. STE12
Chicago, IL 60612
Proteintech@ptglab.com
https://www.ptglab.com
1-312-455-8498
headquarters: USA
At Proteintech, we produce every single antibody we sell; we do not rely on or supply to any other antibody providers: our products are unique and we are 100% accountable for each one. We realize this accountability by validating in-house, providing extensive technical support and guaranteeing your success: in addition to helping you troubleshoot your experiment, we will offer you a full cash refund if you are in any way dissatisfied. We can guarantee satisfaction because we have confidence in our products, confidence cultivated by the science behind our antibodies: we make them using as much of the native protein as possible, and purifying them using affinity purification with the original antigen. We carry out antibody production over a 102-day period, which allows for better antigen fitting to MHC molecules and affinity maturation in the host. This approach results in higher affinity antibodies with greater sensitivity, which you can use in any application and in multiple species.
You can only buy Proteintech antibodies directly from Proteintech or via one of its approved distributors — when you receive your antibody and see the Proteintech logo on the vial, know that you hold something that is truly unique.