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Human TARDBP Protein expressed in HEK-293 Cells - ABIN2733240
Yang, Lin, Robertson, Wang: Dual vulnerability of TDP-43 to calpain and caspase-3 proteolysis after neurotoxic conditions and traumatic brain injury. in Journal of cerebral blood flow and metabolism : official journal of the International Society of Cerebral Blood Flow and Metabolism 2014
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ALS (show IGFALS Proteins)-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 (show HSF1 Proteins)-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 (show PFN1 Proteins) 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 (show GABPA Proteins) 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 Proteins)) 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. 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 (show HSF1 Proteins) overexpression protects against TDP-43 pathology by upregulation of chaperones, especially HSP70 (show HSP70 Proteins), rather than enhancing autophagy
superoxide dismutase (show SOD1 Proteins) function of SOD1 (show SOD1 Proteins) 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 Proteins)/ARE pathway by reducing the expression of MafK and JDP2 (show JDP2 Proteins) 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 (show CNBP Proteins) tardbp and RNA binding protein fus (show FUS Proteins).
Loss of ALS-associated TDP-43 in zebrafish causes muscle degeneration, vascular dysfunction, and reduced motor neuron axon outgrowth.
TARDBP and FUS (show FUS Proteins) act in a pathogenic pathway that is independent of SOD1 (show SOD1 Proteins).
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