Use your antibodies-online credentials, if available.
No Products on your Comparison List.
Your basket is empty.
Find out more
Show all species
Show all synonyms
Select your species and application
anti-Mouse (Murine) Antibodies:
anti-Rat (Rattus) Antibodies:
Go to our pre-filtered search.
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
Show all 122 Pubmed References
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
Show all 12 Pubmed References
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
Show all 5 Pubmed References
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
Show all 4 Pubmed References
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
Show all 3 Pubmed References
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
Show all 3 Pubmed References
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
Show all 3 Pubmed References
Human Polyclonal TARDBP Primary Antibody for ELISA, WB - ABIN451640
Zhang, Xu, Dickey, Buratti, Baralle, Bailey, Pickering-Brown, Dickson, Petrucelli: Progranulin mediates caspase-dependent cleavage of TAR DNA binding protein-43. in The Journal of neuroscience : the official journal of the Society for Neuroscience 2007
Cow (Bovine) Polyclonal TARDBP Primary Antibody for 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. in The Journal of biological chemistry 2005
Show all 2 Pubmed References
Cow (Bovine) Polyclonal TARDBP Primary Antibody for 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. in Nature neuroscience 2011
Show all 2 Pubmed References
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 (show GABPA Antibodies) 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 (show DAZAP1 Antibodies)) 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 (show UTS2R Antibodies). 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.
Amyotrophic lateral sclerosis mutations disrupt phase separation mediated by alpha-helical structure in the TDP-43 low-complexity C-terminal domain.
we demonstrated cytoplasmic TDP-43 aggregate formation in neuronal and glial cells following adenoviral transduction of WT and CTF (show NFIA Antibodies) TDP-43 under MG-132 treatment. These TDP-43 aggregates were phosphorylated and ubiquitinated and consisted of electron-dense granules.
emphasize the importance of distinguishing cerebral age-related TDP-43 with sclerosis from late-onset frontotemporal lobar degeneration with TDP-43 pathology and from advanced Alzheimer disease with TDP-43 pathology
Mutant and wild type human TDP-43 replacing the endogenous Drosophila gene reveals phosphorylation and ubiquitination in mutant lines in the absence of viability or lifespan defects.
The study establishes a functional/physical partnership between FMRP (show FMR1 Antibodies) and TDP-43 that mechanistically links several neurodevelopmental disorders and neurodegenerative diseases.
superoxide dismutase (show SOD1 Antibodies) function of SOD1 (show SOD1 Antibodies) 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 (show NFE2L2 Antibodies)/ARE pathway by reducing the expression of MafK and JDP2 (show JDP2 Antibodies) 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.
we found a significant overlap in genes that undergo both RBM17 (show RBM17 Antibodies)- and TDP-43-dependent cryptic splicing repression, many of which are associated with survival. We propose that repression of cryptic splicing by RBPs is critical for neuronal health and survival
These results establish that SMN overexpression in motor neurons slows disease onset and outcome by ameliorating pathological signs in this model of mutant TDP-43-mediated amyotrophic lateral sclerosis (ALS).
These findings suggest that TDP-43 promotes tau exon 10 inclusion and 4R-tau expression and that disease-related changes of TDP-43, truncations and mutations, affect its function in tau exon 10 splicing, possibly because of TDP-43 mislocalization to the cytoplasm.
this study suggests hemizygous TDP-43(M337V) mice as a useful animal model to study TDP-43 toxicity and further consolidates mitochondrial TDP-43 as a novel therapeutic target for TDP-43-linked neurodegenerative diseases.
Data indicate a method for site-directed single nucleotide editing in two disease-related genes, DNA binding protein (show CNBP Antibodies) tardbp and RNA binding protein fus (show FUS Antibodies).
Loss of ALS-associated TDP-43 in zebrafish causes muscle degeneration, vascular dysfunction, and reduced motor neuron axon outgrowth.
TARDBP and FUS (show FUS Antibodies) act in a pathogenic pathway that is independent of SOD1 (show SOD1 Antibodies).
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