Use your antibodies-online credentials, if available.
No Products on your Comparison List.
Your basket is empty.
Find out more
HIV-1, the causative agent of acquired immunodeficiency syndrome (AIDS), contains an RNA genome that produces a chromosomally integrated DNA during the replicative cycle. Additionally we are shipping TAR DNA Binding Protein Kits (23) and TAR DNA Binding Protein Proteins (14) and many more products for this protein.
Showing 10 out of 241 products:
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 references for ABIN188986
Human Polyclonal TARDBP Primary Antibody for EIA, IF - ABIN500883
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 references for ABIN500883
Human Monoclonal TARDBP Primary Antibody for EIA, IHC (p) - ABIN317572
Kabashi, Valdmanis, Dion, Spiegelman, McConkey, Vande Velde, Bouchard, Lacomblez, Pochigaeva, Salachas, Pradat, Camu, Meininger, Dupre, Rouleau: TARDBP mutations in individuals with sporadic and familial amyotrophic lateral sclerosis. in Nature genetics 2008
Show all 2 references for ABIN317572
Chicken 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 references for ABIN2780848
Chicken 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 references for ABIN2780849
Human Polyclonal TARDBP Primary Antibody for IF, WB - ABIN318898
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
Human Polyclonal TARDBP Primary Antibody for IF, IHC (p) - ABIN657685
Kim, Shanware, Bowler, Tibbetts: Amyotrophic lateral sclerosis-associated proteins TDP-43 and FUS/TLS function in a common biochemical complex to co-regulate HDAC6 mRNA. in The Journal of biological chemistry 2010
Human Polyclonal TARDBP Primary Antibody for ELISA, WB - ABIN334503
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
Two mutations G335D and Q343R within the amyloidogenic core region of TDP-43 influence its aggregation.
This study demonstrated that single nucleotide TDP-43 mutation within a Taiwanese family.
Molecular analysis of pathological TDP-43 aggregates in amyotrophic lateral sclerosis brains.
All patients with behavioural variant Frontotemporal dementia + motor neurone disease (MND (show CLN8 Antibodies)) or MND (show CLN8 Antibodies) showed plentiful p62 (show GTF2H1 Antibodies)/TDP-43 positive inclusions in remaining anterior horn cells
TDP-43 within neurons plays an essential role of mRNA transport into distal neurites for local translation, and thus, dysfunctions of TDP-43 cause neural diseases such as amyotrophic lateral sclerosis and frontotemporal lobar degeneration.
a combination of TDP-43 and an motor neuron degeneration factors can be used to reflect abnormal RNA metabolism in WBCs and thus be useful as ALS-onset biomarkers.
both phosphorylated and calpain-cleaved TDP-43 fragments persist intracellularly for a length of time that is sufficient for self-aggregation, thereby serving as seeds for inclusions.
misfolded TDP-43 is cleared by VHL (show VHL Antibodies)/CUL2 (show CUL2 Antibodies) in a step-wise manner via fragmentation.
TDP-43 functions within a network of hnRNP (show HNRNPC Antibodies) proteins to inhibit the production of a truncated human SORT1 (show SORT1 Antibodies) receptor.
These observations point to the need to elucidate the novel sequestration mechanism and details of the toxicity of the misfolded and aggregation-prone TDP43 CTFs (as well as the RNA binding and nuclear retention) in order to identify possible preventive interventions against ALS.
TDP-43 functions within a network of hnRNP (show HNRNPH2 Antibodies) proteins to inhibit the production of a truncated human SORT1 (show SORT1 Antibodies) receptor.
Data demonstrate the existence of a physiological decrease of TDP-43/TBPH levels with aging in brain tissue both in wild-type mice and flies, showing that it is an evolutionary conserved phenomenon
This study demonistrated that proprioceptive nerve endings in muscles revealed early and alterations at Ia/II proprioceptive nerve endings in muscle spindles and in the absence of alterations in alpha-motor axons in TDP43(A315T) transgenic mice.
UBQLN2 (show UBQLN2 Antibodies) dysregulation in neurons can drive NF-kappaB (show NFKB1 Antibodies) activation and cytosolic TDP-43 aggregation.
These findings demonstrate a role for PABPN1 (show PABPN1 Antibodies) in rescuing several cytopathological features of TDP-43 proteinopathy by increasing the turnover of pathologic proteins.
identifies DDX58 (show DDX58 Antibodies) and MTHFSD as two TDP-43 targets that are misregulated in amyotrophic lateral sclerosis. 1
Valproate Attenuates 25-kDa C-Terminal Fragment of TDP-43-Induced Neuronal Toxicity via Suppressing Endoplasmic Reticulum Stress and Activating Autophagy.
we observed a glial reaction and an activity-dependent modification of Shh (show SHH Antibodies), Noggin (show NOG Antibodies), and Numb (show NUMB Antibodies) proteins. we found that Shh (show SHH Antibodies) and Noggin (show NOG Antibodies) could affect motor performance and that these proteins could be associated with both TDP-43 and Numb (show NUMB Antibodies)
The ability of TDP-43 to promote CD14 (show CD14 Antibodies)-mediated activation of microglial NF-kappaB (show NFKB1 Antibodies) and AP-1 (show JUN Antibodies) pathways, as well as the NLRP3 (show NLRP3 Antibodies) inflammasome.
Depletion of TDP-43 leads to a dramatic reduction in the RNA processing and the protein levels of IL-6 (show IL6 Antibodies) in serum.
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