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- Antibody Data
- Antigen structure
- References [12]
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- Western blot [1]
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- Product number
- 60160-1-Ig - Provider product page
- Provider
- Proteintech Group
- Proper citation
- Proteintech Cat#60160-1-Ig, RRID:AB_10666169
- Product name
- FUS/TLS antibody
- Antibody type
- Monoclonal
- Description
- KD/KO validated FUS/TLS antibody (Cat. #60160-1-Ig) is a mouse monoclonal antibody that shows reactivity with human, mouse, rat, pig and has been validated for the following applications: FC, IF, IHC, IP, ELISA.
- Reactivity
- Human, Mouse, Rat, Porcine
- Host
- Mouse
- Conjugate
- Unconjugated
- Isotype
- IgG
- Antibody clone number
- 3A10B5
- Vial size
- 20ul, 150ul
Submitted references Hippocampal Sclerosis in Frontotemporal Dementia: When Vascular Pathology Meets Neurodegeneration.
RBM45 associates with nuclear stress bodies and forms nuclear inclusions during chronic cellular stress and in neurodegenerative diseases.
Self-assembly of FUS through its low-complexity domain contributes to neurodegeneration.
Motor neuron degeneration in spastic paraplegia 11 mimics amyotrophic lateral sclerosis lesions.
A novel missense mutation of CMT2P alters transcription machinery.
PINK1 and Parkin are genetic modifiers for FUS-induced neurodegeneration.
FUS Interacts with HSP60 to Promote Mitochondrial Damage.
Poly-A binding protein-1 localization to a subset of TDP-43 inclusions in amyotrophic lateral sclerosis occurs more frequently in patients harboring an expansion in C9orf72.
Hu antigen R (HuR) is a positive regulator of the RNA-binding proteins TDP-43 and FUS/TLS: implications for amyotrophic lateral sclerosis.
Topography of FUS pathology distinguishes late-onset BIBD from aFTLD-U.
The RNA-binding protein Fus directs translation of localized mRNAs in APC-RNP granules.
Transportin 1 accumulates specifically with FET proteins but no other transportin cargos in FTLD-FUS and is absent in FUS inclusions in ALS with FUS mutations.
Sieben A, Van Langenhove T, Vermeiren Y, Gossye H, Praet M, Vanhauwaert D, Cousaert C, Engelborghs S, Raedt R, Boon P, Santens P, De Deyn PP, Bracke KR, De Meulemeester K, Van Broeckhoven C, Martin JJ, Bjerke M
Journal of neuropathology and experimental neurology 2021 Mar 22;80(4):313-324
Journal of neuropathology and experimental neurology 2021 Mar 22;80(4):313-324
RBM45 associates with nuclear stress bodies and forms nuclear inclusions during chronic cellular stress and in neurodegenerative diseases.
Collins M, Li Y, Bowser R
Acta neuropathologica communications 2020 Jun 26;8(1):91
Acta neuropathologica communications 2020 Jun 26;8(1):91
Self-assembly of FUS through its low-complexity domain contributes to neurodegeneration.
Matsumoto T, Matsukawa K, Watanabe N, Kishino Y, Kunugi H, Ihara R, Wakabayashi T, Hashimoto T, Iwatsubo T
Human molecular genetics 2018 Apr 15;27(8):1353-1365
Human molecular genetics 2018 Apr 15;27(8):1353-1365
Motor neuron degeneration in spastic paraplegia 11 mimics amyotrophic lateral sclerosis lesions.
Denora PS, Smets K, Zolfanelli F, Ceuterick-de Groote C, Casali C, Deconinck T, Sieben A, Gonzales M, Zuchner S, Darios F, Peeters D, Brice A, Malandrini A, De Jonghe P, Santorelli FM, Stevanin G, Martin JJ, El Hachimi KH
Brain : a journal of neurology 2016 Jun;139(Pt 6):1723-34
Brain : a journal of neurology 2016 Jun;139(Pt 6):1723-34
A novel missense mutation of CMT2P alters transcription machinery.
Hu B, Arpag S, Zuchner S, Li J
Annals of neurology 2016 Dec;80(6):834-845
Annals of neurology 2016 Dec;80(6):834-845
PINK1 and Parkin are genetic modifiers for FUS-induced neurodegeneration.
Chen Y, Deng J, Wang P, Yang M, Chen X, Zhu L, Liu J, Lu B, Shen Y, Fushimi K, Xu Q, Wu JY
Human molecular genetics 2016 Dec 1;25(23):5059-5068
Human molecular genetics 2016 Dec 1;25(23):5059-5068
FUS Interacts with HSP60 to Promote Mitochondrial Damage.
Deng J, Yang M, Chen Y, Chen X, Liu J, Sun S, Cheng H, Li Y, Bigio EH, Mesulam M, Xu Q, Du S, Fushimi K, Zhu L, Wu JY
PLoS genetics 2015 Sep;11(9):e1005357
PLoS genetics 2015 Sep;11(9):e1005357
Poly-A binding protein-1 localization to a subset of TDP-43 inclusions in amyotrophic lateral sclerosis occurs more frequently in patients harboring an expansion in C9orf72.
McGurk L, Lee VM, Trojanowksi JQ, Van Deerlin VM, Lee EB, Bonini NM
Journal of neuropathology and experimental neurology 2014 Sep;73(9):837-45
Journal of neuropathology and experimental neurology 2014 Sep;73(9):837-45
Hu antigen R (HuR) is a positive regulator of the RNA-binding proteins TDP-43 and FUS/TLS: implications for amyotrophic lateral sclerosis.
Lu L, Zheng L, Si Y, Luo W, Dujardin G, Kwan T, Potochick NR, Thompson SR, Schneider DA, King PH
The Journal of biological chemistry 2014 Nov 14;289(46):31792-31804
The Journal of biological chemistry 2014 Nov 14;289(46):31792-31804
Topography of FUS pathology distinguishes late-onset BIBD from aFTLD-U.
Lee EB, Russ J, Jung H, Elman LB, Chahine LM, Kremens D, Miller BL, Branch Coslett H, Trojanowski JQ, Van Deerlin VM, McCluskey LF
Acta neuropathologica communications 2013 May 9;1(9):1-11
Acta neuropathologica communications 2013 May 9;1(9):1-11
The RNA-binding protein Fus directs translation of localized mRNAs in APC-RNP granules.
Yasuda K, Zhang H, Loiselle D, Haystead T, Macara IG, Mili S
The Journal of cell biology 2013 Dec 9;203(5):737-46
The Journal of cell biology 2013 Dec 9;203(5):737-46
Transportin 1 accumulates specifically with FET proteins but no other transportin cargos in FTLD-FUS and is absent in FUS inclusions in ALS with FUS mutations.
Neumann M, Valori CF, Ansorge O, Kretzschmar HA, Munoz DG, Kusaka H, Yokota O, Ishihara K, Ang LC, Bilbao JM, Mackenzie IR
Acta neuropathologica 2012 Nov;124(5):705-16
Acta neuropathologica 2012 Nov;124(5):705-16
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Supportive validation
- Submitted by
- Proteintech Group (provider)
- Main image
- Experimental details
- K-562 cells were subjected to SDS PAGE followed by western blot with 60160-1-Ig(FUS antibody) at dilution of 1:1000
- Sample type
- cell line
