Use your antibodies-online credentials, if available.
No Products on your Comparison List.
Your basket is empty.
Find out more
Show all synonyms
Select your origin of interest
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
Show all 3 Pubmed References
an alpha-helical component in the centre (residues 320-340) of the C-terminal domain is related to the protein's self-association and LLPS. Systematically analysing ALS (show IGFALS Proteins)-related TDP-43 mutants (G298S, M337V, and Q331K) in different buffer conditions at different temperatures, we prove that this phase separation is driven by hydrophobic interactions but is inhibited by electrostatic repulsion.
the present study did not demonstrate oxidative phosphorylation defects in TDP-43 mutants
both FUS (show FUS Proteins) and TDP43 colocalize with active RNA polymerase II at sites of DNA damage along with the DNA damage repair protein, BRCA1, and FUS (show FUS Proteins) and TDP43 participate in the prevention or repair of R loop-associated DNA damage, a manifestation of aberrant transcription and/or RNA processing
The data of this study suggest that TDP-43 pathology is associated with age and exacerbated by the presence of concomitant Alzheimer's disease pathology.
The A382T mutation in TARDBP caused a reduction in the ability of cells to respond to stress through loss of TDP-43 function in stress granule nucleation. The pathogenetic action revealed in study model does not seem to be mediated by changes in the localization of the TDP-43 protein.
TDP-43 competes with other splicing factors for binding to cryptic exons and can repress cryptic exon inclusion.
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 (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.
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 (show HSF1 Proteins) overexpression protects against TDP-43 pathology by upregulation of chaperones, especially HSP70 (show HSP70 Proteins), rather than enhancing autophagy
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.
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.
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.
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