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 :
TDP-43 (C-terminal)
catalog :
12892-1-AP
quantity :
150UL
price :
299 USD
clonality :
polyclonal
host :
domestic rabbit
conjugate :
nonconjugated
reactivity :
human, mouse
application :
western blot, ELISA, immunohistochemistry, immunocytochemistry, immunoprecipitation, chromatin immunoprecipitation, immunohistochemistry - frozen section, immunohistochemistry knockout validation
citations: 63
Published Application/Species/Sample/DilutionReference
  • immunohistochemistry knockout validation; mouse; 1:150; loading ...; fig 1c
Laclair K, Donde A, Ling J, Jeong Y, Chhabra R, Martin L, et al. Depletion of TDP-43 decreases fibril and plaque β-amyloid and exacerbates neurodegeneration in an Alzheimer's mouse model. Acta Neuropathol. 2016;132:859-873 pubmed
  • immunohistochemistry; human; loading ...; fig 1i
Zhang P, Fan B, Yang P, Temirov J, Messing J, Kim H, et al. Chronic optogenetic induction of stress granules is cytotoxic and reveals the evolution of ALS-FTD pathology. elife. 2019;8: pubmed publisher
  • western blot; human; loading ...; fig 4a
  • immunohistochemistry - frozen section; mouse; loading ...; fig 7a
  • western blot; mouse; loading ...; fig 4a, 4c
Lee Y, Huang W, Lin J, Kao T, Lin H, Lee K, et al. Znf179 E3 ligase-mediated TDP-43 polyubiquitination is involved in TDP-43- ubiquitinated inclusions (UBI) (+)-related neurodegenerative pathology. J Biomed Sci. 2018;25:76 pubmed publisher
  • western blot; mouse; 1:2000; loading ...; fig 3a
Maziuk B, Apicco D, Cruz A, Jiang L, Ash P, da Rocha E, et al. RNA binding proteins co-localize with small tau inclusions in tauopathy. Acta Neuropathol Commun. 2018;6:71 pubmed publisher
  • immunocytochemistry; human; loading ...; fig 2e
Becker L, Huang B, Bieri G, Ma R, Knowles D, Jafar Nejad P, et al. Therapeutic reduction of ataxin-2 extends lifespan and reduces pathology in TDP-43 mice. Nature. 2017;544:367-371 pubmed publisher
  • immunocytochemistry; mouse; fig 1b
  • western blot; mouse; fig 1c
Leal Lasarte M, Franco J, Labrador Garrido A, Pozo D, Roodveldt C. Extracellular TDP-43 aggregates target MAPK/MAK/MRK overlapping kinase (MOK) and trigger caspase-3/IL-18 signaling in microglia. FASEB J. 2017;31:2797-2816 pubmed publisher
  • immunocytochemistry; human; loading ...; fig 6g
Boeynaems S, Bogaert E, Kovacs D, Konijnenberg A, Timmerman E, Volkov A, et al. Phase Separation of C9orf72 Dipeptide Repeats Perturbs Stress Granule Dynamics. Mol Cell. 2017;65:1044-1055.e5 pubmed publisher
  • western blot; human; 1:2500; loading ...; fig 5a
Wobst H, Wesolowski S, Chadchankar J, Delsing L, Jacobsen S, Mukherjee J, et al. Cytoplasmic Relocalization of TAR DNA-Binding Protein 43 Is Not Sufficient to Reproduce Cellular Pathologies Associated with ALS In vitro. Front Mol Neurosci. 2017;10:46 pubmed publisher
  • western blot; mouse; 1:1000; loading ...; fig 3s1
Celona B, Dollen J, Vatsavayai S, Kashima R, Johnson J, Tang A, et al. Suppression of C9orf72 RNA repeat-induced neurotoxicity by the ALS-associated RNA-binding protein Zfp106. elife. 2017;6: pubmed publisher
  • western blot; human; loading ...; fig 9f
Suzuki H, Matsuoka M. The Lysosomal Trafficking Transmembrane Protein 106B Is Linked to Cell Death. J Biol Chem. 2016;291:21448-21460 pubmed
  • western blot; mouse; 1:1000; loading ...; fig 1b
Shiihashi G, Ito D, Yagi T, Nihei Y, Ebine T, Suzuki N. Mislocated FUS is sufficient for gain-of-toxic-function amyotrophic lateral sclerosis phenotypes in mice. Brain. 2016;139:2380-94 pubmed publisher
  • immunocytochemistry; mouse; 1:500; fig 3
  • immunohistochemistry; mouse; 1:500; fig 6
  • western blot; mouse; 1:1000; fig 1
Rodriguez Ortiz C, Flores J, Valenzuela J, Rodriguez G, Zumkehr J, Tran D, et al. The Myoblast C2C12 Transfected with Mutant Valosin-Containing Protein Exhibits Delayed Stress Granule Resolution on Oxidative Stress. Am J Pathol. 2016;186:1623-34 pubmed publisher
Romano G, Klima R, Feiguin F. TDP-43 prevents retrotransposon activation in the Drosophila motor system through regulation of Dicer-2 activity. BMC Biol. 2020;18:82 pubmed publisher
Laclair K, Zhou Q, Michaelsen M, Wefers B, Brill M, Janjić A, et al. Congenic expression of poly-GA but not poly-PR in mice triggers selective neuron loss and interferon responses found in C9orf72 ALS. Acta Neuropathol. 2020;140:121-142 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
Strah N, Romano G, Introna C, Klima R, Marzullo M, Ciapponi L, et al. TDP-43 promotes the formation of neuromuscular synapses through the regulation of Disc-large expression in Drosophila skeletal muscles. BMC Biol. 2020;18:34 pubmed publisher
Khosravi B, LaClair K, Riemenschneider H, Zhou Q, Frottin F, Mareljic N, et al. Cell-to-cell transmission of C9orf72 poly-(Gly-Ala) triggers key features of ALS/FTD. EMBO J. 2020;39:e102811 pubmed publisher
Tang F, Zhao L, Zhao Y, Sun D, Zhu X, Mei L, et al. Coupling of terminal differentiation deficit with neurodegenerative pathology in Vps35-deficient pyramidal neurons. Cell Death Differ. 2020;: pubmed publisher
Lanznaster D, Bourgeais J, Bruno C, Hergesheimer R, Thepault R, Vourc H P, et al. TDP-43-Mediated Toxicity in HEK293T Cells: A Fast and Reproducible Protocol To Be Employed in the Search of New Therapeutic Options against Amyotrophic Lateral Sclerosis. Cells. 2019;9: pubmed publisher
Yuva Aydemir Y, Almeida S, Krishnan G, Gendron T, Gao F. Transcription elongation factor AFF2/FMR2 regulates expression of expanded GGGGCC repeat-containing C9ORF72 allele in ALS/FTD. Nat Commun. 2019;10:5466 pubmed publisher
Suzuki H, Shibagaki Y, Hattori S, Matsuoka M. C9-ALS/FTD-linked proline-arginine dipeptide repeat protein associates with paraspeckle components and increases paraspeckle formation. Cell Death Dis. 2019;10:746 pubmed publisher
Deng Z, Lim J, Wang Q, Purtell K, Wu S, Palomo G, et al. ALS-FTLD-linked mutations of SQSTM1/p62 disrupt selective autophagy and NFE2L2/NRF2 anti-oxidative stress pathway. Autophagy. 2019;:1-15 pubmed publisher
Donde A, Sun M, Ling J, Braunstein K, Pang B, Wen X, et al. Splicing repression is a major function of TDP-43 in motor neurons. Acta Neuropathol. 2019;: pubmed publisher
Sugai A, Kato T, Koyama A, Koike Y, Konno T, Ishihara T, et al. Non-genetically modified models exhibit TARDBP mRNA increase due to perturbed TDP-43 autoregulation. Neurobiol Dis. 2019;130:104534 pubmed publisher
Tsunemi T, Perez Rosello T, Ishiguro Y, Yoroisaka A, Jeon S, Hamada K, et al. Increased lysosomal exocytosis induced by lysosomal Ca2+ channel agonists protects human dopaminergic neurons from α-synuclein toxicity. J Neurosci. 2019;: pubmed publisher
Choi S, López González R, Krishnan G, Phillips H, Li A, Seeley W, et al. C9ORF72-ALS/FTD-associated poly(GR) binds Atp5a1 and compromises mitochondrial function in vivo. Nat Neurosci. 2019;22:851-862 pubmed publisher
Wang B, Maxwell B, Joo J, Gwon Y, Messing J, Mishra A, et al. ULK1 and ULK2 Regulate Stress Granule Disassembly Through Phosphorylation and Activation of VCP/p97. Mol Cell. 2019;74:742-757.e8 pubmed publisher
Coudert L, Nonaka T, Bernard E, Hasegawa M, Schaeffer L, Leblanc P. Phosphorylated and aggregated TDP-43 with seeding properties are induced upon mutant Huntingtin (mHtt) polyglutamine expression in human cellular models. Cell Mol Life Sci. 2019;76:2615-2632 pubmed publisher
Gasset Rosa F, Lu S, Yu H, Chen C, Melamed Z, Guo L, et al. Cytoplasmic TDP-43 De-mixing Independent of Stress Granules Drives Inhibition of Nuclear Import, Loss of Nuclear TDP-43, and Cell Death. Neuron. 2019;102:339-357.e7 pubmed publisher
Mann J, Gleixner A, Mauna J, Gomes E, DeChellis Marks M, Needham P, et al. RNA Binding Antagonizes Neurotoxic Phase Transitions of TDP-43. Neuron. 2019;102:321-338.e8 pubmed publisher
Zhang Y, Guo L, Gonzales P, Gendron T, Wu Y, Jansen West K, et al. Heterochromatin anomalies and double-stranded RNA accumulation underlie C9orf72 poly(PR) toxicity. Science. 2019;363: pubmed publisher
Masaki K, Sonobe Y, Ghadge G, Pytel P, Roos R. TDP-43 proteinopathy in Theiler's murine encephalomyelitis virus infection. PLoS Pathog. 2019;15:e1007574 pubmed publisher
Fourier A, Escal J, Bernard E, Lachman I, Perret Liaudet A, Leblanc P, et al. Development of an automated capillary nano-immunoassay-Simple Western assay-to quantify total TDP43 protein in human platelet samples. Anal Bioanal Chem. 2019;411:267-275 pubmed publisher
Ash P, Dhawan U, Boudeau S, Lei S, Carlomagno Y, Knobel M, et al. Heavy Metal Neurotoxicants Induce ALS-Linked TDP-43 Pathology. Toxicol Sci. 2019;167:105-115 pubmed publisher
Jeon G, Shim Y, Lee D, Kim J, Kang M, Ahn S, et al. Pathological Modification of TDP-43 in Amyotrophic Lateral Sclerosis with SOD1 Mutations. Mol Neurobiol. 2019;56:2007-2021 pubmed publisher
Vogler T, Wheeler J, Nguyen E, Hughes M, Britson K, Lester E, et al. TDP-43 and RNA form amyloid-like myo-granules in regenerating muscle. Nature. 2018;563:508-513 pubmed publisher
Liu C, Leng B, Li Y, Jiang H, Duan W, Guo Y, et al. Diallyl Trisulfide Protects Motor Neurons from the Neurotoxic Protein TDP-43 via Activating Lysosomal Degradation and the Antioxidant Response. Neurochem Res. 2018;43:2304-2312 pubmed publisher
Suzuki H, Shibagaki Y, Hattori S, Matsuoka M. The proline-arginine repeat protein linked to C9-ALS/FTD causes neuronal toxicity by inhibiting the DEAD-box RNA helicase-mediated ribosome biogenesis. Cell Death Dis. 2018;9:975 pubmed publisher
Cicardi M, Cristofani R, Rusmini P, Meroni M, Ferrari V, Vezzoli G, et al. Tdp-25 Routing to Autophagy and Proteasome Ameliorates its Aggregation in Amyotrophic Lateral Sclerosis Target Cells. Sci Rep. 2018;8:12390 pubmed publisher
Clemen C, Winter L, Strucksberg K, Berwanger C, Türk M, Kornblum C, et al. The heterozygous R155C VCP mutation: Toxic in humans! Harmless in mice?. Biochem Biophys Res Commun. 2018;503:2770-2777 pubmed publisher
Kasu Y, Alemu S, Lamari A, Loew N, Brower C. The N Termini of TAR DNA-Binding Protein 43 (TDP43) C-Terminal Fragments Influence Degradation, Aggregation Propensity, and Morphology. Mol Cell Biol. 2018;38: pubmed publisher
Salvatori I, Ferri A, Scaricamazza S, Giovannelli I, Serrano A, Rossi S, et al. Differential toxicity of TAR DNA-binding protein 43 isoforms depends on their submitochondrial localization in neuronal cells. J Neurochem. 2018;146:585-597 pubmed publisher
Wang K, Qu X, Liu S, Yang X, Bie F, Wang Y, et al. Identification of aberrantly expressed F-box proteins in squamous-cell lung carcinoma. J Cancer Res Clin Oncol. 2018;144:1509-1521 pubmed publisher
Maucuer A, Desforges B, Joshi V, Boca M, Kretov D, Hamon L, et al. Microtubules as platforms for probing liquid-liquid phase separation in cells - application to RNA-binding proteins. J Cell Sci. 2018;131: pubmed publisher
Bennett C, Dastidar S, Ling S, Malik B, Ashe T, Wadhwa M, et al. Senataxin mutations elicit motor neuron degeneration phenotypes and yield TDP-43 mislocalization in ALS4 mice and human patients. Acta Neuropathol. 2018;136:425-443 pubmed publisher
Mackenzie I, Nicholson A, Sarkar M, Messing J, Purice M, Pottier C, et al. TIA1 Mutations in Amyotrophic Lateral Sclerosis and Frontotemporal Dementia Promote Phase Separation and Alter Stress Granule Dynamics. Neuron. 2017;95:808-816.e9 pubmed publisher
Prudencio M, Gonzales P, Cook C, Gendron T, Daughrity L, Song Y, et al. Repetitive element transcripts are elevated in the brain of C9orf72 ALS/FTLD patients. Hum Mol Genet. 2017;26:3421-3431 pubmed publisher
Osuru H, Pramoonjago P, Abhyankar M, Swanson E, Roker L, Cathro H, et al. Immunolocalization of TAR DNA-binding protein of 43?kDa (TDP-43) in mouse seminiferous epithelium. Mol Reprod Dev. 2017;84:675-685 pubmed publisher
Zhuang J, Wen X, Zhang Y, Shan Q, Zhang Z, Zheng G, et al. TDP-43 upregulation mediated by the NLRP3 inflammasome induces cognitive impairment in 2 2',4,4'-tetrabromodiphenyl ether (BDE-47)-treated mice. Brain Behav Immun. 2017;65:99-110 pubmed publisher
Wobst H, Delsing L, Brandon N, Moss S. Truncation of the TAR DNA-binding protein 43 is not a prerequisite for cytoplasmic relocalization, and is suppressed by caspase inhibition and by introduction of the A90V sequence variant. PLoS ONE. 2017;12:e0177181 pubmed publisher
Ash P, Stanford E, Al Abdulatif A, Ramirez Cardenas A, Ballance H, Boudeau S, et al. Dioxins and related environmental contaminants increase TDP-43 levels. Mol Neurodegener. 2017;12:35 pubmed publisher
Schludi M, Becker L, Garrett L, Gendron T, Zhou Q, Schreiber F, et al. Spinal poly-GA inclusions in a C9orf72 mouse model trigger motor deficits and inflammation without neuron loss. Acta Neuropathol. 2017;134:241-254 pubmed publisher
Ditsworth D, Maldonado M, McAlonis Downes M, Sun S, Seelman A, Drenner K, et al. Mutant TDP-43 within motor neurons drives disease onset but not progression in amyotrophic lateral sclerosis. Acta Neuropathol. 2017;133:907-922 pubmed publisher
Jeong Y, Ling J, Lin S, Donde A, Braunstein K, Majounie E, et al. Tdp-43 cryptic exons are highly variable between cell types. Mol Neurodegener. 2017;12:13 pubmed publisher
Manghera M, Ferguson Parry J, Douville R. TDP-43 regulates endogenous retrovirus-K viral protein accumulation. Neurobiol Dis. 2016;94:226-36 pubmed publisher
Wang G, Yang H, Yan S, Wang C, Liu X, Zhao B, et al. Cytoplasmic mislocalization of RNA splicing factors and aberrant neuronal gene splicing in TDP-43 transgenic pig brain. Mol Neurodegener. 2015;10:42 pubmed publisher
Chou C, Alexeeva O, Yamada S, Pribadi A, Zhang Y, Mo B, et al. PABPN1 suppresses TDP-43 toxicity in ALS disease models. Hum Mol Genet. 2015;24:5154-73 pubmed publisher
Goossens J, Vanmechelen E, Trojanowski J, Lee V, Van Broeckhoven C, van der Zee J, et al. TDP-43 as a possible biomarker for frontotemporal lobar degeneration: a systematic review of existing antibodies. Acta Neuropathol Commun. 2015;3:15 pubmed publisher
Paré B, Touzel Deschênes L, Lamontagne R, Lamarre M, Scott F, Khuong H, et al. Early detection of structural abnormalities and cytoplasmic accumulation of TDP-43 in tissue-engineered skins derived from ALS patients. Acta Neuropathol Commun. 2015;3:5 pubmed publisher
Raitano S, Ordovas L, De Muynck L, Guo W, Espuny Camacho I, Geraerts M, et al. Restoration of progranulin expression rescues cortical neuron generation in an induced pluripotent stem cell model of frontotemporal dementia. Stem Cell Reports. 2015;4:16-24 pubmed publisher
Suzuki H, Matsuoka M. Overexpression of nuclear FUS induces neuronal cell death. Neuroscience. 2015;287:113-24 pubmed publisher
Han H, Wei W, Duan W, Guo Y, Li Y, Wang J, et al. Autophagy-linked FYVE protein (Alfy) promotes autophagic removal of misfolded proteins involved in amyotrophic lateral sclerosis (ALS). In Vitro Cell Dev Biol Anim. 2015;51:249-63 pubmed publisher
Suzuki H, Shibagaki Y, Hattori S, Matsuoka M. Nuclear TDP-43 causes neuronal toxicity by escaping from the inhibitory regulation by hnRNPs. Hum Mol Genet. 2015;24:1513-27 pubmed publisher
product information
CatalogNo :
12892-1-AP
AntigenName :
TDP-43 (C-terminal)
Package :
150UL
Price :
299 USD
Exsists20ul :
20ul trial size available
FullName :
TAR DNA binding protein
Immunogen :
Recombinant Protein
Species :
drosophila, human, monkey, mouse, rat, zebrafish
Host :
Rabbit
IsConjugated :
Unconjugated
AntigenSpecies :
human
Application :
WB, IP, IHC, IF, chIP, ELISA
Clonlity :
Polyclonal
IsoType :
IgG
Synonyms :
ALS10, TAR DNA binding protein, TAR DNA binding protein 43, TARDBP, TDP 43, TDP43
PrimaryOrSecondary :
Primary
AntibodyBuffer :
PBS with 0.1% sodium azide and 50% glycerol pH 7.3.
GenBankNo :
BC001487
Category :
Binding Proteins;Cytoskeleton/Scaffold Proteins;Disease Related;Metabolism;Neurology;
PurifyMethod :
Antigen affinity purification
NewAb :
False
IsSellable :
True
Feature :
siRNA
AppTiter :
IF 1:100 ; IHC 1:1000 ; IP 1:1000 ; WB 1:800 ;
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.