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Human Monoclonal TARDBP Primary Antibody for IF, IHC (p) - ABIN565080
Arai, Hasegawa, Akiyama, Ikeda, Nonaka, Mori, Mann, Tsuchiya, Yoshida, Hashizume, Oda: TDP-43 is a component of ubiquitin-positive tau-negative inclusions in frontotemporal lobar degeneration and amyotrophic lateral sclerosis. in Biochemical and biophysical research communications 2006
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Chicken Polyclonal TARDBP Primary Antibody for ICC, IF - ABIN188986
Neumann, Sampathu, Kwong, Truax, Micsenyi, Chou, Bruce, Schuck, Grossman, Clark, McCluskey, Miller, Masliah, Mackenzie, Feldman, Feiden, Kretzschmar, Trojanowski, Lee: Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis. in Science (New York, N.Y.) 2006
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Human Polyclonal TARDBP Primary Antibody for ELISA, WB - ABIN565079
Johnson, McCaffery, Lindquist, Gitler: A yeast TDP-43 proteinopathy model: Exploring the molecular determinants of TDP-43 aggregation and cellular toxicity. in Proceedings of the National Academy of Sciences of the United States of America 2008
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Polyclonal TARDBP Primary Antibody for WB - ABIN540268
De Marco, Lomartire, Mandili, Lupino, Buccinnà, Ramondetti, Moglia, Novelli, Piccinini, Mostert, Rinaudo, Chiò, Calvo: Reduced cellular Ca(2+) availability enhances TDP-43 cleavage by apoptotic caspases. in Biochimica et biophysica acta 2014
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Human Polyclonal TARDBP Primary Antibody for ICC, IF - ABIN4358265
Sharma, Burré, Südhof: CSPα promotes SNARE-complex assembly by chaperoning SNAP-25 during synaptic activity. in Nature cell biology 2010
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Human Polyclonal TARDBP Primary Antibody for ICC, ELISA - ABIN1003253
Ou, Wu, Harrich, García-Martínez, Gaynor: Cloning and characterization of a novel cellular protein, TDP-43, that binds to human immunodeficiency virus type 1 TAR DNA sequence motifs. in Journal of virology 1995
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Human Polyclonal TARDBP Primary Antibody for ICC, ELISA - ABIN1003254
Buratti, Dörk, Zuccato, Pagani, Romano, Baralle: Nuclear factor TDP-43 and SR proteins promote in vitro and in vivo CFTR exon 9 skipping. in The EMBO journal 2001
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Cow (Bovine) Monoclonal TARDBP Primary Antibody for ICC, IF - ABIN4358267
Verbeeck, Deng, Dejesus-Hernandez, Taylor, Ceballos-Diaz, Kocerha, Golde, Das, Rademakers, Dickson, Kukar: Expression of Fused in sarcoma mutations in mice recapitulates the neuropathology of FUS proteinopathies and provides insight into disease pathogenesis. in Molecular neurodegeneration 2012
Cow (Bovine) Polyclonal TARDBP Primary Antibody for IHC, WB - ABIN2780849
Buratti, Brindisi, Giombi, Tisminetzky, Ayala, Baralle: TDP-43 binds heterogeneous nuclear ribonucleoprotein A/B through its C-terminal tail: an important region for the inhibition of cystic fibrosis transmembrane conductance regulator exon 9 splicing. in The Journal of biological chemistry 2005
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Cow (Bovine) Polyclonal TARDBP Primary Antibody for IHC, WB - ABIN2780848
Estes, Boehringer, Zwick, Tang, Grigsby, Zarnescu: Wild-type and A315T mutant TDP-43 exert differential neurotoxicity in a Drosophila model of ALS. in Human molecular genetics 2011
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ALS (显示 IGFALS 抗体)-mutant linked TDP-43 mutations expressed at moderate levels in a pattern mimicking endogenous TDP-43 also cause toxicity in a non-cell autonomous manner. Eliminating mutant TDP-43Q331K synthesis in a proportion of motor neurons delayed disease onset, reduced aberrant nuclear morphology in those neurons at early disease stages, and almost eliminated age-dependent accelerated death of those motor neurons.
Study reports that cryptic exon incorporation occurred not only in Alzheimer' disease brains exhibiting TDP-43 pathology, but also in neurons lacking cytoplasmic inclusion but exhibiting nuclear clearance of TDP-43.
Acetylation of the protein triggers TDP-43 pathology in cultured cells and mouse skeletal muscle, which can be cleared through an HSF1 (显示 HSF1 抗体)-dependent chaperone mechanism that disaggregates the protein.
These studies showed that physiological oligomerization of TDP-43 is mediated through its N-terminal domain, which forms functional and dynamic oligomers antagonizing pathologic aggregation.
Expression of PFN1 (显示 PFN1 抗体) mutants induces accumulation of TDP-43, and promotes conversion of normal TDP-43 into an abnormal form. These results provide new insight into the mechanisms of TDP-43 proteinopathies and other diseases associated with amyloid-like protein deposition.
Study reports the altered expression and/or mislocalization of the TAR-DNA binding protein 43 (TDP-43) in both niemann-pick disease type C mouse and in a human neuronal model of the disease. Results extend the importance of the role of TDP-43 in neurodegenerative disease and further highlight the need to prioritize the targeting of this protein to develop novel therapeutic strategies.
This study demonstrated that increased rates of TDP-43-associated hippocampal atrophy might occur at least 10 years before death in patient with Alzheimer disease.
Authors observed impaired levels of glutathione (downstream Nrf2 (显示 GABPA 抗体) antioxidant) in TDP-43M337V patient fibroblasts and astrocyte cultures from TDP-43Q331K mice, indicative of elevated oxidative stress and failure of some upregulated antioxidant genes to be translated into protein.
removing the human orthologs of Hrb27c (DAZAP1 (显示 DAZAP1 抗体)) in human neuronal cell lines can correct several pre-mRNA splicing events altered by TDP-43 depletion
TDP-43 suppressed tau expression by promoting its mRNA instability through the UG repeats of its 3-UTR (显示 UTS2R 抗体). The C-terminal region of TDP-43 was required for this function.The level of TDP-43, which is decreased in AD brains, was found to correlate negatively with the tau level in human brain.
results suggest that regulation of the U6 snRNA expression level by TDP-43 is a key factor in the increase in cell death upon TDP-43 loss-of-function
this study shows that HSF1 (显示 HSF1 抗体) overexpression protects against TDP-43 pathology by upregulation of chaperones, especially HSP70 (显示 HSP70 抗体), rather than enhancing autophagy
superoxide dismutase (显示 SOD1 抗体) function of SOD1 (显示 SOD1 抗体) might not be required to preserve DNA integrity in motor neurons, at least when the function of TDP-43 is unaltered
The findings of this study support a role for nuclear depletion of TDP-43 in the pathogenesis of AD and provide strong rationale for developing novel therapeutics to alleviate the depletion of TDP-43 and functional antemortem biomarkers associated with its nuclear loss.
These results suggested that nuclear localization signal -tagged TDP25 (a carboxyl-terminal fragment of TDP-43) can change its structure to use ordered oligomeric but nontoxic state. Moreover, the structure of ordered oligomers as well as nuclear sequestration may be important in mediating cytotoxicity in ALS pathology.
Mutatgion M337V in TDP-43 impaired the Nrf2 (显示 NFE2L2 抗体)/ARE pathway by reducing the expression of MafK and JDP2 (显示 JDP2 抗体) proteins.
The suppression of TDP-43 mitochondrial localization abolishes WT and mutant TDP-43-induced mitochondrial dysfunction and neuronal loss, and improves phenotypes of transgenic mutant TDP-43 mice.
Data indicate a method for site-directed single nucleotide editing in two disease-related genes, DNA binding protein (显示 CNBP 抗体) tardbp and RNA binding protein fus (显示 FUS 抗体).
Loss of ALS-associated TDP-43 in zebrafish causes muscle degeneration, vascular dysfunction, and reduced motor neuron axon outgrowth.
TARDBP and FUS (显示 FUS 抗体) act in a pathogenic pathway that is independent of SOD1 (显示 SOD1 抗体).
HIV-1, the causative agent of acquired immunodeficiency syndrome (AIDS), contains an RNA genome that produces a chromosomally integrated DNA during the replicative cycle. Activation of HIV-1 gene expression by the transactivator Tat is dependent on an RNA regulatory element (TAR) located downstream of the transcription initiation site. The protein encoded by this gene is a transcriptional repressor that binds to chromosomally integrated TAR DNA and represses HIV-1 transcription. In addition, this protein regulates alternate splicing of the CFTR gene. A similar pseudogene is present on chromosome 20.
TAR DNA binding protein
, TAR DNA-binding protein 43
, Tardbp protein
, TAR DNA-binding protein-43