Recombinant Human TAR DNA-binding protein 43(TARDBP),partial

Code CSB-EP023129HUe0
Size US$1726
  • (Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.

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Product Details

Purity Greater than 90% as determined by SDS-PAGE.
Target Names TARDBP
Uniprot No. Q13148
Research Area Transcription
Alternative Names ALS10; OTTHUMP00000002171; OTTHUMP00000002172; OTTHUMP00000002173; TADBP_HUMAN; TAR DNA binding protein 43; TAR DNA binding protein; TAR DNA-binding protein 43; TARDBP; TDP 43; TDP-43; TDP43
Species Homo sapiens (Human)
Source E.coli
Expression Region 1-396aa
Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request.
Mol. Weight 69.9kDa
Protein Length Partial
Tag Info N-terminal GST-tagged
Form Liquid or Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol.
Note: If you have any special requirement for the glycerol content, please remark when you place the order.
If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. Our default final concentration of glycerol is 50%. Customers could use it as reference.
and FAQs
Protein FAQs
Storage Condition Store at -20°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet & COA Please contact us to get it.

Target Data

Function DNA and RNA-binding protein which regulates transcription and splicing. Involved in the regulation of CFTR splicing. It promotes CFTR exon 9 skipping by binding to the UG repeated motifs in the polymorphic region near the 3'-splice site of this exon. The resulting aberrant splicing is associated with pathological features typical of cystic fibrosis. May also be involved in microRNA biogenesis, apoptosis and cell division. Can repress HIV-1 transcription by binding to the HIV-1 long terminal repeat. Stabilizes the low molecular weight neurofilament (NFL) mRNA through a direct interaction with the 3' UTR.
Gene References into Functions
  1. TDP-43 deposition leads to targeted RNA instability in amyotrophic lateral sclerosis and frontotemporal dementia PMID: 30030424
  2. CHCHD10 mutations have a role in cytoplasmic TDP-43 accumulation and synaptic integrity PMID: 28585542
  3. Study confirms the high expression of hTDP-43 in the CNS, increased microgliosis and motor deficits, exhibiting further prominent ALS/FTLD pathologies, such as cytoplasmic and insoluble TDP-43 in TAR6/6 mice. This model represents not only pathological TDP-43 expression but also disease-relevant posttranslational changes. PMID: 29787578
  4. The relevance of contact-independent cell-to-cell transfer of TDP-43 and SOD1 in amyotrophic lateral sclerosis. PMID: 28711596
  5. Findings highlight that the phosphatase regulator, GADD34, also functions as a kinase scaffold in response to chronic oxidative stress and recruits CK1 and oxidized TDP-43 to facilitate its phosphorylation, as seen in TDP-43 proteinopathies. PMID: 29109149
  6. We identified impaired RNA metabolism, secondary to TDP-43 loss of function, as a possible pathological mechanism of HSPB8 toxicity, leading to muscle and nerve degeneration PMID: 29029362
  7. the introduction of SOD1(G93A) and TDP43(A315T), established Amyotrophic lateral sclerosis (ALS)-related mutations, changed the subcellular expression and localization of RNAs within the neurons, showing a spatial specificity to either the soma or the axon. Altogether, we provide here the first combined inclusive profile of mRNA and miRNA expression in two ALS models at the subcellular level PMID: 28300211
  8. These data provide structural detail for the established mechanistic role of the well-folded TDP-43 NTD in splicing and link this function to liquid-liquid phase separation. PMID: 29438978
  9. TDP43 alters most splicing events with splicing factor SRSF3 in triple-negative breast cancer. PMID: 29581274
  10. Of the whole cohort of patients with Motor Neuron Disease and Frontotemporal Dementia, 1 patient harboured a mutation in the TAR DNA-binding protein (TARDBP) gene. PMID: 29886477
  11. Study demonstrated TDP-43/pTDP-43 deposition in skin nerves in ALS patients. Although the mechanisms underlying TDP-43 in ALS are currently unknown, its detection is of interest, and the deposition may occur not only in ALS but also during the aging process which is based on observations of the present study. PMID: 29804146
  12. Both ALS and FTD patients presented with higher TDP-43 and tauT levels compared to the control group. The combination of biomarkers in the form of the TDP-43 x tauT / tauP-181 formula achieved the best discrimination between ALS or FTD and controls, with sensitivities and specificities >0.8. PMID: 28848086
  13. 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. PMID: 29233983
  14. more selective group of neurons appears to be affected in frontotemporal lobar degeneration (FTLD)-TDP and FTLD-FUS than in FTLD-tau PMID: 28984110
  15. 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 PMID: 29621978
  16. describe here two cases of apparently sporadic amyotrophic lateral sclerosis associated with mutations, respectively, in SOD1 and TARDP genes PMID: 27494151
  17. 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. PMID: 28281308
  18. Depletion of TAF15, FUS and TDP-43 in human-induced pluripotent stem cell-derived motor neurons affects different genes. PMID: 27378374
  19. 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. PMID: 29787572
  20. TDP-43 impairs the induction of multiple key stress genes required to protect from disease by reducing the recruitment of the chromatin remodeler Chd1 to chromatin. PMID: 29153328
  21. The mutation of TARDBP caused amyotrophic lateral sclerosis PMID: 29478603
  22. Cytoplasmic TDP-43 mislocalization and aggregation is a pathological hallmark of amyotrophic lateral sclerosis and frontotemporal lobar degeneration. TDP-43 is an RNA-binding protein with a prion-like domain that promotes TDP-43 misfolding. [review] PMID: 27920024
  23. SOD1 mutations were present in 20% of familial amyotrophic lateral sclerosis (ALS) patients and 1.9% of sporadic ALS patients, while FUS mutations were responsible for 13.3% of familial ALS cases, and TARDBP mutations were rare in either familial or sporadic ALS cases. PMID: 27604643
  24. 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-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. PMID: 28988034
  25. the present study did not demonstrate oxidative phosphorylation defects in TDP-43 mutants PMID: 28482850
  26. both FUS and TDP43 colocalize with active RNA polymerase II at sites of DNA damage along with the DNA damage repair protein, BRCA1, and FUS and TDP43 participate in the prevention or repair of R loop-associated DNA damage, a manifestation of aberrant transcription and/or RNA processing PMID: 27849576
  27. 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. PMID: 27495267
  28. 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. PMID: 28172957
  29. TDP-43 competes with other splicing factors for binding to cryptic exons and can repress cryptic exon inclusion. PMID: 28549443
  30. 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. PMID: 26810591
  31. ALS-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. PMID: 28357566
  32. 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. PMID: 28332094
  33. Acetylation of the protein triggers TDP-43 pathology in cultured cells and mouse skeletal muscle, which can be cleared through an HSF1-dependent chaperone mechanism that disaggregates the protein. PMID: 28724966
  34. 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. PMID: 28663553
  35. Expression of PFN1 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. PMID: 27432186
  36. 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. PMID: 27193329
  37. 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. PMID: 28919059
  38. Authors observed impaired levels of glutathione (downstream Nrf2 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. PMID: 28334913
  39. removing the human orthologs of Hrb27c (DAZAP1) in human neuronal cell lines can correct several pre-mRNA splicing events altered by TDP-43 depletion PMID: 28575377
  40. 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. PMID: 28335005
  41. Amyotrophic lateral sclerosis mutations disrupt phase separation mediated by alpha-helical structure in the TDP-43 low-complexity C-terminal domain. PMID: 27545621
  42. we demonstrated cytoplasmic TDP-43 aggregate formation in neuronal and glial cells following adenoviral transduction of WT and CTF TDP-43 under MG-132 treatment. These TDP-43 aggregates were phosphorylated and ubiquitinated and consisted of electron-dense granules. PMID: 28599005
  43. 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 PMID: 28467211
  44. 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. PMID: 28686708
  45. The study establishes a functional/physical partnership between FMRP and TDP-43 that mechanistically links several neurodevelopmental disorders and neurodegenerative diseases. PMID: 27518042
  46. By silencing TDP-43, authors saw significant inhibition of cell proliferation and metastasis in A375 and WM451 cells. TDP-43 knockdown could suppress glucose transporter type-4 (GLUT4) expression and reduce glucose uptake. PMID: 27786596
  47. The present study, based on 15 cases staged for pTDP-43 pathology, reports the finding that pathologically altered TDP-43 in Betz cells reacts differently than that in bulbar or spinal alpha-motoneurons. The major differences between the two types of histological profiles are discussed within the context of their possible consequences and implications for the potential further progression or spread of the pTDP-43 lesions. PMID: 27757524
  48. This study have shown that TDP-43-positive cytoplasmic inclusions were frequently found in the amygdala of pathologically and genetically confirmed cases of Frontotemporal Lobar Degeneration and Motor Neuron Disease. PMID: 28859337
  49. Results indicated that a range of disease specific TDP-43 variants are generated in amyotrophic lateral sclerosis patients with different variants being generated in sporadic and familial cases. PMID: 28122516
  50. heterogeneous structural reorganization and decreased stability of the truncated RRM2 domain PMID: 28793209
  51. These results suggest that Perry syndrome may be distinctive type of TDP-43 proteinopathy. PMID: 28789478
  52. TDP-43 accumulates in the mitochondria of neurons in subjects with ALS or frontotemporal dementia. Disease-associated mutations increase TDP-43 mitochondrial localization. In mitochondria, wild-type (WT) and mutant TDP-43 preferentially bind mitochondria-transcribed messenger RNAs (mRNAs) encoding respiratory complex I subunits ND3 and ND6, impair their expression and specifically cause complex I disassembly. PMID: 27348499
  53. TDP-43 pathologic burden in amyotrophic lateral sclerosis is associated with cognitive impairment and c9orf72-associated amyotrophic lateral sclerosis , but not duration of disease or rate of progression PMID: 28521037
  54. Data suggest that stably folded N-terminal domain (NTD) is essential for correct TDP-43 function; point mutations in TDP-43 NTD that result in amyotrophic lateral sclerosis or frontotemporal lobar degeneration also destabilize TDP-43, disrupt RNA splicing, alter dimerization/localization of TDP-43 in cells, and cause pathological TDP-43 aggregates inside cells; leucine-27 is key residue for TDP-43 NTD dimerization. PMID: 28566288
  55. Motor-neuron disease (MND)-linked RNA-binding proteins (RBPs), TDP-43, FUS, and hnRNPA2B1, bind to and induce structural alteration of UGGAAexp. These RBPs suppress UGGAAexp-mediated toxicity in Drosophila by functioning as RNA chaperones for proper UGGAAexp folding and regulation of pentapeptide repeat translation. PMID: 28343865
  56. We directly link TDP-43 loss of function toxicity to two genes with rare amyotrophic lateral sclerosis and frontotemporal lobar degeneration-causing mutations, CHMP2B and ErbB4. PMID: 27621269
  57. We report that overexpression of HSPB8 in immortalized motor neurones decreased the accumulation of TDP-25 and TDP-35 and that protection against mislocalized/truncated TDP-43 was observed for HSPB8 in Drosophila melanogaster Overexpression of HSP67Bc, the functional ortholog of human HSPB8, suppressed the eye degeneration caused by the cytoplasmic accumulation of a TDP-43 variant PMID: 27466192
  58. The extreme N-terminus of TDP-43 mediates the cytoplasmic aggregation of TDP-43 and associated toxicity in vivo. Study provides further evidence confirming the critical role of the extreme N-terminus of TDP-43 in regulating protein structure as well as mediating toxicity associated with its aggregation. PMID: 27155453
  59. This animal disease model of TDP-43 Proteinopathy mice in which mutant human TDP-43 expression causes progressive neuron loss. Also show that these rNLS8 mice have a pattern of axonal dieback and cell death that mirrors that often observed in human patients. PMID: 27445147
  60. we analyzed fast axonal transport in larval motor neurons of Drosophila models of TARDBP (TDP-43), FUS and C9orf72. We also analyzed the effect of loss-of-function mutants of the Drosophila orthologs of TDP-43 and FUS, TBPH and caz, respectively. The motor activities of larvae and adults in these models were assessed to correlate potential defects in axonal transport with locomotor deficits PMID: 27056981
  61. 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. PMID: 28487370
  62. Mutant C9ORF72 impairs mitochondria activity in a different and opposite manner compared to mutant TDP-43. TARDBP and C9ORF72 mutations might trigger cell death by impairing not only RNA metabolism, but also mitochondria activity in ALS/FTD neurons since their mitochondrial energetic metabolism depends mainly on oxidative phosphorylation. PMID: 27151080
  63. 14-3-3 eta isoform colocalizes TDP-43 on the coarse granules in the anterior horn cells of patients with sporadic amyotrophic lateral sclerosis. PMID: 27256400
  64. Pathological TAR-DNA binding protein 43 (TDP-43) is cleaved into two major groups of fragments of approximately 35-, approximately 25-kDa, and the truncation at Arg208 completely eliminates the intrinsic ability of RNA recognition motif RRM2 to fold. PMID: 28257838
  65. TDP-43 dual phosphorylation by MEK, at threonine 153 and tyrosine 155 (p-T153/Y155), was dramatically increased by the heat shock response (HSR) in human cells. PMID: 28167528
  66. Taken together, inhibition of nuclear import of TDP-43 by cytoplasmic poly-GA inclusions causally links the two main aggregating proteins in C9orf72 amyotrophic lateral sclerosis /lobar degeneration pathogenesis. PMID: 28040728
  67. The aim of this review will be to provide a general overview of TDP-43 and FUS/TLS proteins and to highlight their physiological functions--{REVIEW} PMID: 27015757
  68. Increased cytoplasmic TARDBP mRNA in affected spinal motor neurons in amyotrophic lateral sclerosis is caused by abnormal autoregulation of TDP-43. PMID: 27257061
  69. Findings suggest a mechanism in which retrotransposable element (RTE) activity contributes to neurodegeneration in TAR DNA-binding protein 43 (TDP-43)-mediated diseases such as Amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degeneration (FTLD). PMID: 28301478
  70. Possible role of deregulated DNA binding function of TDP-43 in ALS. PMID: 27693252
  71. These data suggest that Familial Amyotrophic Lateral Sclerosis-linked PFN1 mutations exacerbate TDP-43-induced neurodegeneration in a gain-of-function manner, possibly by shifting the localization of TDP-43 from nuclei to cytoplasm. PMID: 27634045
  72. Data suggest that transitions of TDP-43 among soluble, droplet, and aggregate phases are involved in pathological aggregation; TDP-43 prion-like domain appears to wobble at a cusp of the protein folding energy landscape where any number of factors can tip the balance and trigger the conversion from its native function to its pathological one. [REVIEW] PMID: 28112502
  73. Secreted PGRN is incorporated into cells via sortilin or cation-independent mannose 6-phosphate receptor, and facilitated the acidification of lysosomes and degradation of CTSDmat. Moreover, the change of PGRN levels led to a cell-type-specific increase of insoluble TDP-43. In the brain tissue of FTLD-TDP patients with PGRN deficiency, CTSD and phosphorylated TDP-43 accumulated in neurons PMID: 28073925
  74. Various degrees of TDP-43 cytoplasmic accumulation and nuclear TDP-43 depletion were achieved and the resulting cellular viability was evaluated, leading to a quantitative global analysis on the relative effects of LOF and GOF on the overall cytotoxicity. PMID: 27445339
  75. using an in vitro cellular model, we demonstrated that Drb1 co-localizes with cytoplasmic aggregates mediated by TAR DNA-binding protein 43 PMID: 27226551
  76. Data suggest that expression of TDP-43 is negligible in spermatozoa from men with primary spermatogenic dysfunction as compared to men with normozoospermia; TDP-43 may serve as biomarker in male infertility. This study was conducted in India using semen from men diagnosed with oligozoospermia, oligoasthenozoosperima, oligoteratozoospermia, oligoasthenoteratozoosperima, asthenoteratozoosperima, and teratozoospermia. PMID: 25359468
  77. The present study identified USP7 and TDP-43 as the regulators of CRY1 and CRY2, underscoring the significance of the stability control process of CRY proteins for period determination in the mammalian circadian clockwork. PMID: 27123980
  78. Two mutations G335D and Q343R within the amyloidogenic core region of TDP-43 influence its aggregation. PMID: 27030292
  79. This study demonstrated that single nucleotide TDP-43 mutation within a Taiwanese family. PMID: 26581115
  80. Molecular analysis of pathological TDP-43 aggregates in amyotrophic lateral sclerosis brains. PMID: 26980269
  81. All patients with behavioural variant Frontotemporal dementia + motor neurone disease (MND) or MND showed plentiful p62/TDP-43 positive inclusions in remaining anterior horn cells PMID: 26538301
  82. 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. PMID: 26915990
  83. 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. PMID: 26672899
  84. 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. PMID: 26723245
  85. misfolded TDP-43 is cleared by VHL/CUL2 in a step-wise manner via fragmentation. PMID: 26751167
  86. TDP-43 functions within a network of hnRNP proteins to inhibit the production of a truncated human SORT1 receptor. PMID: 26614389
  87. 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. PMID: 26757674
  88. pathological TDP-43 and FUS may exert motor neuron pathology in amyotrophic lateral sclerosis through the initiation of propagated misfolding of SOD1 PMID: 26926802
  89. we identified TDP-43 as one of the novel TNF-alpha factors and found that it bound to the LPS-responsive element in the TNF-alpha promoter to increase TNF-alpha expression. PMID: 25202836
  90. Its mutations are associated with Chinese patients with cognitive impairment in amyotrophic lateral sclerosis. PMID: 26639158
  91. TDP-43 does not critically regulate expression or splicing of tau in Alzheimer's disease suggesting that TDP-43 contributes to Alzheimer's disease through mechanisms independent of tau. PMID: 26507309
  92. Study identifies a common mechanism of transport into neurites of proteins linked to the pathology of Alzheimer's disease (i.e. sAPP) and ALS (i.e. FUS, TDP-43 and SOD1) PMID: 26605911
  93. RNA binding proteins TDP-43 and FUS do not consistently fit the currently characterised inclusion models suggesting that cells have a larger repertoire for generating inclusions than currently thought. PMID: 26293199
  94. TDP-43 does have dynamic inter-domain interactions, which are coordinated by the intrinsically-disordered prion-like domain. PMID: 27040765
  95. Data indicate that the structure of TAR DNA-binding protein-43 (TDP-43)consists of an alpha-helix and six beta-strands. PMID: 26756435
  96. Expression of mutant hTDP-43 induced neuronal degeneration with partial selectivity for motor neurons. Motor neuron loss was accompanied by abnormal neurite morphology and length. PMID: 26174443
  97. Knockdown of TDP-43 results in an increase in viral titers, suggesting a protective role for TDP-43 in CVB3 infection. PMID: 25976304
  98. results support a model whereby dFMRP can modulate the neurotoxicity caused by TDP-43 overexpression PMID: 26385636
  99. TDP-43 pathology in the basal forebrain is strongly associated with hippocampal sclerosis-aging. PMID: 26971127
  100. Results suggest that functional deficits in iTDP-43(A315T) mice are at least in part a direct and transient effect of the presence of TDP-43(A315T) and illustrate the compensatory capacity of compromised neurons once transgenic TDP-43 is removed PMID: 26437864

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Involvement in disease Amyotrophic lateral sclerosis 10 (ALS10)
Subcellular Location Nucleus
Tissue Specificity Ubiquitously expressed. In particular, expression is high in pancreas, placenta, lung, genital tract and spleen.
Database Links

HGNC: 11571

OMIM: 605078

KEGG: hsa:23435

STRING: 9606.ENSP00000240185

UniGene: Hs.300624

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