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Human Monoclonal TARDBP Primary Antibody pour 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. dans Biochemical and biophysical research communications 2006
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Chicken Polyclonal TARDBP Primary Antibody pour 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. dans Science (New York, N.Y.) 2006
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Human Polyclonal TARDBP Primary Antibody pour ELISA, WB - ABIN565079
Johnson, McCaffery, Lindquist, Gitler: A yeast TDP-43 proteinopathy model: Exploring the molecular determinants of TDP-43 aggregation and cellular toxicity. dans Proceedings of the National Academy of Sciences of the United States of America 2008
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Polyclonal TARDBP Primary Antibody pour 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. dans Biochimica et biophysica acta 2014
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Human Polyclonal TARDBP Primary Antibody pour ICC, IF - ABIN4358265
Sharma, Burré, Südhof: CSPα promotes SNARE-complex assembly by chaperoning SNAP-25 during synaptic activity. dans Nature cell biology 2010
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Human Polyclonal TARDBP Primary Antibody pour ICC, ELISA - ABIN1003254
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. dans Journal of virology 1995
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Human Polyclonal TARDBP Primary Antibody pour ICC, ELISA - ABIN1003253
Buratti, Dörk, Zuccato, Pagani, Romano, Baralle: Nuclear factor TDP-43 and SR proteins promote in vitro and in vivo CFTR exon 9 skipping. dans The EMBO journal 2001
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Human Polyclonal TARDBP Primary Antibody pour ICC, ELISA - ABIN1031116
Yang, Lin, Robertson, Wang: Dual vulnerability of TDP-43 to calpain and caspase-3 proteolysis after neurotoxic conditions and traumatic brain injury. dans Journal of cerebral blood flow and metabolism : official journal of the International Society of Cerebral Blood Flow and Metabolism 2014
Human Polyclonal TARDBP Primary Antibody pour ELISA, WB - ABIN451640
Zhang, Xu, Dickey, Buratti, Baralle, Bailey, Pickering-Brown, Dickson, Petrucelli: Progranulin mediates caspase-dependent cleavage of TAR DNA binding protein-43. dans The Journal of neuroscience : the official journal of the Society for Neuroscience 2007
Cow (Bovine) Monoclonal TARDBP Primary Antibody pour 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. dans Molecular neurodegeneration 2012
Study shows that TDP-43 is deposited in the olfactory bulb in Alzheimer's disease, albeit of low frequency. The deposition appears to be a late occurrence compared to TDP-43 deposition in other brain regions.
ALS (Montrer IGFALS Anticorps)-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 (Montrer HSF1 Anticorps)-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 (Montrer PFN1 Anticorps) 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 (Montrer GABPA Anticorps) 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 (Montrer DAZAP1 Anticorps)) in human neuronal cell lines can correct several pre-mRNA splicing events altered by TDP-43 depletion
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 (Montrer HSF1 Anticorps) overexpression protects against TDP-43 pathology by upregulation of chaperones, especially HSP70 (Montrer HSP70 Anticorps), rather than enhancing autophagy
superoxide dismutase (Montrer SOD1 Anticorps) function of SOD1 (Montrer SOD1 Anticorps) 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 (Montrer NFE2L2 Anticorps)/ARE pathway by reducing the expression of MafK and JDP2 (Montrer JDP2 Anticorps) 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 (Montrer CNBP Anticorps) tardbp and RNA binding protein fus (Montrer FUS Anticorps).
Loss of ALS-associated TDP-43 in zebrafish causes muscle degeneration, vascular dysfunction, and reduced motor neuron axon outgrowth.
TARDBP and FUS (Montrer FUS Anticorps) act in a pathogenic pathway that is independent of SOD1 (Montrer SOD1 Anticorps).
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