TARDBP Antibody, FITC conjugated
Description
Definition and Functionality
The TARDBP Antibody, FITC conjugated combines a high-affinity monoclonal or polyclonal antibody with fluorescein isothiocyanate (FITC), a fluorescent dye emitting at 519 nm (excitation: 495 nm) . This conjugation enables visualization of TDP-43 protein localization via fluorescence microscopy or flow cytometry. The antibody targets epitopes within the middle region (e.g., amino acids 200–414) or N-terminal region of TDP-43, ensuring detection of both wild-type and post-translationally modified forms (e.g., phosphorylated, ubiquitinated) .
Key Applications
Critical Notes
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Antigen Retrieval: Mandatory for paraffin-embedded tissues to resolve nuclear localization defects in ALS/FTLD samples .
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Cross-Reactivity: Tested in human, mouse, rat, and zebrafish models .
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FITC Conjugation: Enhances signal-to-noise ratio in fluorescence assays .
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Purification Methods: Affinity chromatography (e.g., Protein A/G) .
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Stability: Lyophilized or liquid formulations require light protection to prevent FITC degradation .
Disease Relevance
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ALS/FTLD Pathology: FITC-conjugated antibodies detect cytoplasmic TDP-43 aggregates, a hallmark of neurodegeneration .
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Cancer Research: TDP-43 overexpression in triple-negative breast cancer (TNBC) suggests its role in oncogenesis .
Mutational Studies
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G335D Mutation: Enhances TDP-43 aggregation and amyloid formation, linked to familial ALS .
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Q343R Mutation: Disrupts aggregation propensity, highlighting structural determinants of TDP-43 toxicity .
Validation and Quality Control
Product Specs
Target Background
TARDBP (TAR DNA-binding protein 43) is an RNA-binding protein crucial for various stages of RNA biogenesis and processing. Its two RNA recognition motifs (RRM1 and RRM2) preferentially bind GU-rich repeats, primarily found within long introns and the 3' untranslated regions (UTRs) of mRNAs. This binding regulates the splicing of numerous coding and non-coding RNAs, including those encoding proteins vital for neuronal survival and those implicated in neurodegenerative diseases. TARDBP maintains mitochondrial homeostasis by modulating mitochondrial transcript processing, influences mRNA stability by recruiting the CNOT7/CAF1 deadenylase complex to mRNA 3' UTRs (resulting in poly(A) tail shortening), and contributes to cell survival by associating with stalled ribosomes in stress granules (SGs) in response to oxidative stress. It also participates in skeletal muscle development and regeneration through cytoplasmic myo-granule formation and binding to mRNAs encoding sarcomeric proteins. Furthermore, TARDBP regulates circadian clock periodicity by stabilizing CRY1 and CRY2 proteins in an FBXL3-dependent manner and negatively regulates CDK6 expression. Finally, it modulates the expression of HDAC6, ATG7, and VCP in a PPIA/CYPA-dependent manner.
- TDP-43 deposition contributes to targeted RNA instability in amyotrophic lateral sclerosis (ALS) and frontotemporal dementia. PMID: 30030424
- CHCHD10 mutations are implicated in cytoplasmic TDP-43 accumulation and compromised synaptic integrity. PMID: 28585542
- A transgenic mouse model (TAR6/6) exhibits high CNS hTDP-43 expression, increased microgliosis, motor deficits, and ALS/FTLD pathologies including cytoplasmic and insoluble TDP-43, reflecting both pathological expression and relevant post-translational modifications. PMID: 29787578
- Research highlights the role of contact-independent cell-to-cell transfer of TDP-43 and SOD1 in ALS. PMID: 28711596
- GADD34, a phosphatase regulator, acts as a kinase scaffold in response to chronic oxidative stress, recruiting CK1 and oxidized TDP-43 to facilitate its phosphorylation, a feature observed in TDP-43 proteinopathies. PMID: 29109149
- Impaired RNA metabolism due to TDP-43 loss of function is proposed as a pathogenic mechanism underlying HSPB8 toxicity, leading to muscle and nerve degeneration. PMID: 29029362
- Introduction of SOD1(G93A) and TDP43(A315T) ALS-related mutations alters the subcellular expression and localization of RNAs within neurons, exhibiting soma and axon spatial specificity. This research provides a comprehensive profile of mRNA and miRNA expression in two ALS models at the subcellular level. PMID: 28300211
- Structural details are provided elucidating the role of the well-folded TDP-43 N-terminal domain (NTD) in splicing and its link to liquid-liquid phase separation. PMID: 29438978
- TDP43 significantly alters splicing events with splicing factor SRSF3 in triple-negative breast cancer. PMID: 29581274
- A patient with Motor Neuron Disease and Frontotemporal Dementia harbored a mutation in the TARDBP gene. PMID: 29886477
- TDP-43/pTDP-43 deposition is observed in skin nerves of ALS patients. While the mechanisms remain unclear, its detection is noteworthy and deposition may occur in both ALS and aging. PMID: 29804146
- ALS and FTD patients show higher TDP-43 and tauT levels compared to controls. A combined biomarker formula (TDP-43 x tauT / tauP-181) effectively discriminates between ALS/FTD and controls. PMID: 28848086
- TDP-43 turnover and toxicity are partly dependent on the endocytosis pathway. TDP-43 inhibits endocytosis and co-localizes with endocytic proteins, including in ALS patient tissue. PMID: 29233983
- Frontotemporal lobar degeneration (FTLD)-TDP and FTLD-FUS affect a more selective neuronal population than FTLD-tau. PMID: 28984110
- A high frequency of the TARDBP p.M337V mutation is reported in familial ALS in south-eastern China, with patients exhibiting a benign course and prolonged survival. PMID: 29621978
- Two cases of apparently sporadic ALS are described, each associated with mutations in SOD1 and TARDP genes. PMID: 27494151
- Two common patterns of TDP-43 and tau protein misfolding are identified in human brain aging. In the absence of significant Alzheimer's disease pathology, cerebral age-related TDP-43 with sclerosis (CARTS) cases often show tau neurofibrillary tangles in hippocampal dentate granule neurons. PMID: 28281308
- Depletion of TAF15, FUS, and TDP-43 in human-induced pluripotent stem cell-derived motor neurons affects distinct sets of genes. PMID: 27378374
- TDP-43 mislocalization to axons precedes cell death in cortical neurons, and cytoskeletal structure/function is impaired by both wild-type and mutant TDP-43 constructs in vitro. PMID: 29787572
- TDP-43 impairs the induction of protective stress genes by reducing Chd1 chromatin remodeler recruitment. PMID: 29153328
- A TARDBP mutation causes amyotrophic lateral sclerosis. PMID: 29478603
- Cytoplasmic TDP-43 mislocalization and aggregation are hallmarks of ALS and frontotemporal lobar degeneration. TDP-43, an RNA-binding protein with a prion-like domain, promotes TDP-43 misfolding. [review] PMID: 27920024
- SOD1 mutations account for 20% of familial ALS and 1.9% of sporadic ALS, while FUS mutations cause 13.3% of familial ALS cases; TARDBP mutations are rare in both familial and sporadic ALS. PMID: 27604643
- An alpha-helical region (residues 320-340) in the TDP-43 C-terminal domain is crucial for self-association and liquid-liquid phase separation (LLPS). Analysis of ALS-related TDP-43 mutants (G298S, M337V, and Q331K) reveals that this phase separation is driven by hydrophobic interactions but inhibited by electrostatic repulsion. PMID: 28988034
- This study did not find oxidative phosphorylation defects in TDP-43 mutants. PMID: 28482850
- FUS and TDP43 colocalize with active RNA polymerase II at DNA damage sites along with BRCA1, participating in the prevention or repair of R-loop-associated DNA damage. PMID: 27849576
- TDP-43 pathology is associated with age and exacerbated by concomitant Alzheimer's disease pathology. PMID: 27495267
- The TARDBP A382T mutation reduces cellular stress response due to loss of TDP-43 function in stress granule nucleation, without altering TDP-43 localization. PMID: 28172957
- TDP-43 competes with other splicing factors for cryptic exon binding and can repress cryptic exon inclusion. PMID: 28549443
- TDP-43 deposition is observed in the olfactory bulb in Alzheimer's disease, albeit infrequently and late in the disease course. PMID: 26810591
- ALS-linked TDP-43 mutations expressed at moderate levels, mimicking endogenous TDP-43, cause non-cell autonomous toxicity. Reducing mutant TDP-43Q331K synthesis delayed disease onset, reduced nuclear morphology abnormalities, and mitigated motor neuron death. PMID: 28357566
- Cryptic exon incorporation occurs in Alzheimer's disease brains with TDP-43 pathology and in neurons lacking cytoplasmic inclusions but showing nuclear TDP-43 clearance. PMID: 28332094
- TDP-43 acetylation triggers pathology in cultured cells and mouse skeletal muscle, cleared via an HSF1-dependent chaperone mechanism. PMID: 28724966
- Physiological TDP-43 oligomerization is mediated by its N-terminal domain, forming functional dynamic oligomers that counteract pathological aggregation. PMID: 28663553
- PFN1 mutations induce TDP-43 accumulation and promote its conversion into an abnormal form, offering insights into TDP-43 proteinopathies and amyloid-like protein deposition. PMID: 27432186
- Altered TAR-DNA binding protein 43 (TDP-43) expression/mislocalization is observed in Niemann-Pick disease type C mouse and human neuronal models, highlighting its role in neurodegenerative disease. PMID: 27193329
- Increased TDP-43-associated hippocampal atrophy may occur up to 10 years before death in Alzheimer's disease patients. PMID: 28919059
- Impaired glutathione levels (downstream Nrf2 antioxidant) are observed in TDP-43M337V patient fibroblasts and TDP-43Q331K mice astrocytes, suggesting oxidative stress and impaired antioxidant gene translation. PMID: 28334913
- Silencing human Hrb27c (DAZAP1) orthologs corrects pre-mRNA splicing events altered by TDP-43 depletion. PMID: 28575377
- TDP-43 suppresses tau expression by promoting mRNA instability via UG repeats in its 3'-UTR, a function requiring the TDP-43 C-terminal region. TDP-43 levels negatively correlate with tau levels in human brain. PMID: 28335005
- Amyotrophic lateral sclerosis mutations disrupt phase separation mediated by the alpha-helical structure in the TDP-43 low-complexity C-terminal domain. PMID: 27545621
- Cytoplasmic TDP-43 aggregate formation (phosphorylated and ubiquitinated electron-dense granules) is observed in neuronal and glial cells following adenoviral transduction of WT and CTF TDP-43 under MG-132 treatment. PMID: 28599005
- The importance of distinguishing cerebral age-related TDP-43 with sclerosis from late-onset frontotemporal lobar degeneration with TDP-43 pathology and advanced Alzheimer's disease with TDP-43 pathology is highlighted. PMID: 28467211
- Replacing endogenous Drosophila TDP-43 with human wild-type and mutant TDP-43 reveals phosphorylation and ubiquitination in mutant lines without affecting viability or lifespan. PMID: 28686708
- A functional/physical interaction between FMRP and TDP-43 is established, linking neurodevelopmental and neurodegenerative diseases. PMID: 27518042
- TDP-43 silencing inhibits cell proliferation and metastasis in A375 and WM451 cells by suppressing GLUT4 expression and glucose uptake. PMID: 27786596
- Pathologically altered TDP-43 in Betz cells differs from that in bulbar or spinal alpha-motoneurons, with implications for disease progression. PMID: 27757524
- TDP-43-positive cytoplasmic inclusions are frequently found in the amygdala of patients with Frontotemporal Lobar Degeneration and Motor Neuron Disease. PMID: 28859337
- A range of disease-specific TDP-43 variants are generated in ALS patients, differing between sporadic and familial cases. PMID: 28122516
- Studies reveal heterogeneous structural reorganization and decreased stability of the truncated RRM2 domain. PMID: 28793209
Q&A
What is TARDBP and why is it an important research target?
TARDBP (TAR DNA-binding protein 43) functions as an RNA-binding protein with diverse roles in cellular processes. It has emerged as a significant molecule in both neurodegenerative disorders and cancer biology. In neurodegenerative contexts, TARDBP mislocalization and aggregation form the pathological hallmark of amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degeneration (FTLD) . In oncology, particularly hepatocellular carcinoma (HCC), TARDBP has transitioned from being primarily associated with neurodegeneration to being recognized for its contributions to critical cellular processes including proliferation, apoptosis, and metastasis . This protein's involvement in both disease categories makes it a compelling target for diverse research applications.
What experimental techniques can utilize FITC-conjugated TARDBP antibodies?
FITC-conjugated TARDBP antibodies are versatile tools applicable across multiple experimental approaches:
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Immunofluorescence microscopy - For subcellular localization studies, particularly when examining TARDBP mislocalization from nucleus to cytoplasm
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Flow cytometry - For quantitative assessment of TARDBP expression in cell populations
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Live cell imaging - For monitoring dynamic TARDBP localization changes
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Tissue section analysis - For examining TARDBP distribution in pathological specimens
These techniques are particularly valuable when examining TARDBP's abnormal cytoplasmic accumulation, as demonstrated in studies of both neurodegenerative disorders and cancer models .
How does TARDBP expression vary across different tissue types?
Research indicates that TARDBP expression patterns vary significantly across tissue types and disease states:
This tissue-specific expression profile should guide experimental design and interpretation when using TARDBP antibodies .
What are the key optimization parameters for immunofluorescence using FITC-conjugated TARDBP antibodies?
Optimization for TARDBP immunofluorescence requires careful attention to several parameters:
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Fixation method - Paraformaldehyde (4%) generally preserves TARDBP epitopes while maintaining cellular architecture
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Permeabilization - Critical for accessing intracellular TARDBP; Triton X-100 (0.1-0.5%) is typically effective
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Blocking conditions - BSA (3-5%) with normal serum matching the secondary antibody host
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Antibody concentration - Typically 1-10 μg/mL, requiring titration for optimal signal-to-noise ratio
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Antigen retrieval - May be necessary for formalin-fixed tissue sections
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Nuclear counterstaining - DAPI commonly used to distinguish nuclear vs. cytoplasmic TARDBP localization
When examining pathological samples, it's crucial to optimize these parameters specifically for detecting cytoplasmic TARDBP accumulation, as this antibody has demonstrated specificity for the cytoplasmic fraction of TDP43 in previous studies .
How can researchers verify the specificity of TARDBP antibody binding?
Verifying antibody specificity for TARDBP requires multiple complementary approaches:
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Positive controls - Cell lines or tissues known to express TARDBP (e.g., neuronal cells, HCC cell lines)
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Negative controls - TARDBP knockout cells or tissues
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Peptide competition assays - Pre-incubating antibody with purified TARDBP peptide should abolish specific staining
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Multiple antibody validation - Comparing staining patterns using antibodies targeting different TARDBP epitopes
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siRNA knockdown - Reduced signal following TARDBP knockdown confirms specificity
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Western blot correlation - Confirming molecular weight matches expected TARDBP size (~43 kDa)
When using domain-specific antibodies like those targeting the RRM1 domain of TARDBP, additional validation may be needed to ensure epitope accessibility in different experimental conditions .
What controls should be included when studying TARDBP mislocalization?
Given TARDBP's complex subcellular distribution patterns, particularly in pathological states, comprehensive controls are essential:
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Normal tissue controls - Demonstrating typical nuclear TARDBP localization
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Subcellular fractionation validation - Confirming antibody specificity for cytoplasmic vs. nuclear fractions
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Co-localization markers - Nuclear (e.g., DAPI) and cytoplasmic (e.g., β-tubulin) markers to confirm compartmentalization
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Disease-relevant positive controls - ALS/FTLD tissue for neurodegenerative studies; HCC tissue for cancer studies
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Treatment response controls - Samples treated with compounds known to alter TARDBP localization
Previous research has established that certain antibodies, like the E6 monoclonal antibody, specifically recognize the cytoplasmic fraction of TARDBP, making proper controls crucial for accurate interpretation .
How can FITC-conjugated TARDBP antibodies be used to investigate TARDBP's role in immune modulation?
TARDBP has been implicated in immune regulation within the tumor microenvironment. Advanced applications for studying this relationship include:
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Multiplex immunofluorescence - Co-staining TARDBP with immune markers (CD274/PD-L1, CTLA4) to analyze correlation at the cellular level
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Flow cytometry - Quantifying TARDBP expression in isolated immune cell populations
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Sorted cell analysis - Examining TARDBP expression in specific immune cell subsets isolated from tumor tissue
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Spatial transcriptomics integration - Correlating TARDBP protein localization with immune gene expression patterns
Research has shown significant positive correlations between TARDBP expression and immune checkpoint molecules CD274 and CTLA4, suggesting important regulatory connections . This correlation opens avenues for investigating combined therapeutic strategies targeting both TARDBP and checkpoint pathways to enhance anti-tumor immunity.
What methodological approaches can distinguish pathological from physiological TARDBP localization?
Distinguishing pathological from normal TARDBP distribution requires sophisticated methodological approaches:
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High-resolution confocal microscopy - Enabling precise subcellular localization analysis
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Super-resolution techniques - STORM or STED microscopy for nanoscale distribution patterns
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Live cell imaging - Tracking TARDBP dynamics in response to cellular stressors
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Quantitative image analysis - Nuclear:cytoplasmic ratio measurements across experimental conditions
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Solubility fractionation - Biochemical separation of soluble vs. aggregated TARDBP species
Studies have demonstrated that cytoplasmic mislocalization and aggregation of TARDBP are characteristic of both neurodegenerative disorders and certain cancers, making these approaches valuable for pathological investigations .
How can researchers investigate the mechanisms of TARDBP degradation using antibody-based approaches?
Investigating TARDBP degradation pathways is critical for understanding disease mechanisms and developing therapeutic strategies. Advanced methodological approaches include:
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Proteasome inhibition studies - Using MG132 to block proteasomal degradation while monitoring TARDBP levels
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Lysosomal inhibition - Applying compounds like bafilomycin A1 to evaluate lysosomal contribution
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TRIM21-dependent mechanisms - Investigating the E3 ubiquitin ligase TRIM21's role in antibody-mediated TARDBP clearance
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Pulse-chase experiments - Measuring TARDBP half-life under various experimental conditions
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Ubiquitination analysis - Immunoprecipitation followed by ubiquitin detection
Research has identified both the TRIM21/proteasome and lysosomal degradation pathways as potential mechanisms for antibody-mediated TARDBP degradation, suggesting therapeutic potential for targeting pathological TARDBP accumulation .
How might FITC-conjugated TARDBP antibodies contribute to cancer biomarker development?
Recent research positions TARDBP as a promising cancer biomarker, particularly for hepatocellular carcinoma. Emerging applications include:
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Tissue microarray analysis - High-throughput evaluation of TARDBP expression across large patient cohorts
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Liquid biopsy development - Detecting TARDBP in circulating tumor cells or exosomes
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Multiplex biomarker panels - Combining TARDBP with other prognostic markers
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Pathological staging correlation - Relating TARDBP expression patterns to tumor grade/stage
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Treatment response prediction - Evaluating TARDBP as a predictive biomarker for therapy selection
Studies indicate that TARDBP expression correlates with adverse patient outcomes in HCC, with ROC analysis demonstrating strong predictive value for HCC incidence . This positions TARDBP antibodies as valuable tools for translational cancer research.
What experimental approaches can elucidate the relationship between TARDBP and tumor mutational burden?
The correlation between TARDBP expression and tumor mutational burden (TMB) represents a significant research direction requiring sophisticated methodological approaches:
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Integrated multi-omics analysis - Correlating TARDBP protein levels with genomic mutation profiles
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Single-cell approaches - Examining TARDBP expression and mutation signatures at single-cell resolution
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CRISPR-mediated TARDBP modulation - Evaluating effects on genomic stability and mutation rates
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DNA damage response analysis - Investigating TARDBP's potential role in DNA repair mechanisms
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Longitudinal mutation accumulation studies - Tracking mutation development in relation to TARDBP expression levels
Research has demonstrated positive correlations between TARDBP expression and TMB across several cancer types, suggesting potential involvement in genomic instability mechanisms underlying cancer progression .
How can researchers investigate the relationship between TARDBP and immune checkpoint molecules?
The positive correlation between TARDBP and immune checkpoint molecules (CD274/PD-L1 and CTLA4) presents intriguing opportunities for mechanistic investigation:
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Co-immunoprecipitation studies - Examining physical interactions between TARDBP and checkpoint proteins
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Transcriptional regulation analysis - Investigating TARDBP's potential role in regulating checkpoint gene expression
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ChIP-seq/RIP-seq approaches - Mapping TARDBP binding to regulatory regions or transcripts of checkpoint genes
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Immune checkpoint blockade models - Evaluating TARDBP expression changes following checkpoint inhibition
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Patient-derived xenograft models - Testing combined targeting of TARDBP and checkpoint pathways
Research has shown that immunotherapeutic interventions targeting CD274 and CTLA-4 checkpoints have demonstrated promising efficacy across various solid tumors, with ongoing clinical trials evaluating their potential in HCC . Understanding the mechanistic connections with TARDBP could inform novel combination therapeutic approaches.
What are common pitfalls when using FITC-conjugated antibodies for TARDBP detection?
Several technical challenges may arise when using FITC-conjugated TARDBP antibodies:
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Photobleaching - FITC is relatively susceptible to photobleaching; use anti-fade mounting media and minimize exposure
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Autofluorescence - Particularly problematic in tissues with high lipofuscin content; utilize autofluorescence quenching protocols
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pH sensitivity - FITC fluorescence is optimal at alkaline pH; maintain appropriate buffer conditions
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Spectrum overlap - Plan multiplex experiments carefully to avoid bleed-through with other fluorophores
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Fixation artifacts - Certain fixatives may alter TARDBP epitope accessibility or create background
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Cytoplasmic vs. nuclear discrimination - Low-quality images may fail to distinguish these critical compartments
Methodological refinements include using longer-wavelength conjugates for tissues with high autofluorescence, optimizing fixation protocols specifically for TARDBP epitope preservation, and employing spectral unmixing for multiplex applications.
How can researchers overcome challenges in detecting cytoplasmic TARDBP inclusions?
Detection of pathological cytoplasmic TARDBP inclusions presents specific methodological challenges:
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Epitope masking - Protein aggregation may conceal antibody binding sites; optimize antigen retrieval methods
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Inclusion heterogeneity - Different types of TARDBP inclusions may require specific detection approaches
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Sensitivity limitations - Early/subtle cytoplasmic mislocalization may be difficult to detect; enhance signal amplification
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Background interference - Non-specific cytoplasmic staining can obscure true inclusions; rigorous blocking protocols
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Quantification challenges - Establish objective criteria for inclusion identification and counting
Research with antibodies targeting specific domains of TARDBP, like the RRM1 domain, has demonstrated efficacy in recognizing cytoplasmic species in both cellular systems and mouse models . These approaches can be adapted for FITC-conjugated antibodies with appropriate methodological refinements.
What experimental design considerations maximize data quality when studying TARDBP in disease models?
Optimal experimental design for TARDBP studies in disease contexts requires careful planning:
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Time course analysis - TARDBP mislocalization may be dynamic; include multiple time points
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Appropriate disease models - Select models that recapitulate human TARDBP pathology (e.g., ALS/FTLD mice for neurodegeneration, HCC xenografts for cancer)
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Cell type specificity - TARDBP pathology may affect specific cell populations; employ cell-type markers
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Quantitative metrics - Establish objective parameters (nuclear:cytoplasmic ratio, inclusion counts)
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Statistical power - Ensure sufficient sample sizes for detecting potentially subtle changes
Studies have demonstrated that intrathecal injections of antibodies against the RRM1 domain of TARDBP resulted in large neuron penetration and mitigation of cytoplasmic TARDBP mislocalization in mouse models . Similar methodological considerations should guide experiments with FITC-conjugated TARDBP antibodies.
What emerging applications might expand the utility of FITC-conjugated TARDBP antibodies?
The research landscape for TARDBP continues to evolve, suggesting several innovative applications:
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Intravital imaging - Real-time visualization of TARDBP dynamics in living organisms
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High-content screening - Large-scale evaluation of compounds affecting TARDBP localization
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Correlative light-electron microscopy - Linking fluorescence patterns to ultrastructural features
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Microfluidic single-cell analysis - High-throughput quantification of TARDBP distribution patterns
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Combinatorial therapeutic development - Monitoring TARDBP as a biomarker for response to emerging treatments
The continued refinement of both antibody technology and imaging methodologies promises to enhance our understanding of TARDBP's complex roles in both neurodegenerative disorders and cancer .
How might TARDBP research inform therapeutic development across disease areas?
TARDBP research spans disease boundaries, suggesting integrated therapeutic approaches:
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Antibody-based therapeutics - Building on findings that full-length antibodies against TARDBP can mitigate proteinopathy
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Small molecule modulators - Targeting TARDBP mislocalization or aggregation with membrane-permeable compounds
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Combined checkpoint/TARDBP targeting - Exploring synergies based on correlations between TARDBP and immune checkpoints
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TRIM21/proteasome pathway enhancement - Boosting endogenous clearance mechanisms for cytoplasmic TARDBP
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RNA-based interventions - Targeting TARDBP-regulated RNA processing events
