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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
Cow (Bovine) Polyclonal TARDBP Primary Antibody pour IHC, WB - ABIN2780848
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. dans The Journal of biological chemistry 2005
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Cow (Bovine) Polyclonal TARDBP Primary Antibody pour IHC, WB - ABIN2780849
Polymenidou, Lagier-Tourenne, Hutt, Huelga, Moran, Liang, Ling, Sun, Wancewicz, Mazur, Kordasiewicz, Sedaghat, Donohue, Shiue, Bennett, Yeo, Cleveland: Long pre-mRNA depletion and RNA missplicing contribute to neuronal vulnerability from loss of TDP-43. dans Nature neuroscience 2011
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Both ALS (Montrer IGFALS Anticorps) and FTD (Montrer FTL Anticorps) patients presented with higher TDP-43 and tauT (Montrer TAUT Anticorps) levels compared to the control group. The combination of biomarkers in the form of the TDP-43 x tauT (Montrer TAUT Anticorps) / tauP-181 formula achieved the best discrimination between ALS (Montrer IGFALS Anticorps) or FTD (Montrer FTL Anticorps) and controls, with sensitivities and specificities >0.8.
TDP-43 turnover and toxicity depend in part upon the endocytosis pathway. TDP-43 inhibits endocytosis, and co-localizes strongly with endocytic proteins, including in amyotrophic lateral sclerosis patient tissue.
more selective group of neurons appears to be affected in frontotemporal lobar degeneration (FTLD)-TDP and FTLD-FUS (Montrer FUS Anticorps) than in FTLD-tau
study found a high frequency of the TARDBP p.M337 V mutation in familial amyotrophic lateral sclerosis (ALS) in south-eastern China; the TARDBP-linked ALS patients showed a benign disease course and prolonged survival
describe here two cases of apparently sporadic amyotrophic lateral sclerosis associated with mutations, respectively, in SOD1 (Montrer SOD1 Anticorps) and TARDP genes
Study indicates that there are at least two common patterns of TDP-43 and tau protein misfolding in human brain aging. In patients lacking substantial Alzheimer's disease pathology, cerebral age-related TDP-43 with sclerosis (CARTS) cases tend to have tau neurofibrillary tangles in the hippocampal dentate granule neurons, providing a potential proxy indicator of CARTS.
Dep (Montrer FUS Anticorps)letion of (Montrer TAF15 Anticorps)TAF15, FUS and TDP-43 in human-induced pluripotent stem cell-derived motor neurons affects different genes.
TDP-43 mislocalisation into axons precedes cell death in cortical neurons, and that cytoskeletal structure and function is impaired by expression of either TDP-43 wild-type or mutant constructs in vitro.
TDP-43 impairs the induction of multiple key stress genes required to protect from disease by reducing the recruitment of the chromatin remodeler Chd1 (Montrer CHD1 Anticorps) to chromatin.
The mutation of TARDBP caused amyotrophic lateral sclerosis
FUS (Montrer FUS Anticorps) and TAF15 (Montrer TAF15 Anticorps) exhibit similar global RNA interaction profiles in vivo, but affect a strikingly small subset of common genes. Unexpectedly, TAF15 (Montrer TAF15 Anticorps) influences a small fraction of amyotrophic lateral sclerosis events compared with TDP-43 and FUS (Montrer FUS Anticorps) in the mouse CNS.
Increased excitatory synaptic inputs and dendritic spine densities is associated with TDP-43(Q331K) mutation resulting in amyotrophic lateral sclerosis.
Given the close association of stress granules and TDP-43, we wondered whether internalisation of SOD1 (Montrer SOD1 Anticorps) aggregates stimulated TDP-43 cytosolic aggregate structures. Addition of recombinant mutant G93A SOD1 (Montrer SOD1 Anticorps) aggregates to NSC-34 cells was found to trigger a rapid shift of TDP-43 to the cytoplasm where it was still accumulated after 48 h.
The mutated TDP-43 has a significant pathological effect at the dendritic spine that is associated with attenuated neural transmission.
Studied expression and localization of TAR DNA-binding protein 43 (TDP-43) in mouse seminiferous epithelium. Found TDP-43 is expressed by both germ cells and Sertoli cells and appears to have a role in specific stages of spermatogenesis.
TDP-43 overexpression decreases amyloid-Beta plaque deposition while increasing abnormal tau aggregation.
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
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.
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