TARDBP antibodies target the TAR DNA-binding protein 43 (TDP-43), a multifunctional RNA/DNA-binding protein encoded by the *TARDBP* gene. TDP-43 is ubiquitously expressed and plays critical roles in RNA metabolism, including splicing, transport, and stability. Structurally, it contains two RNA-recognition motifs (RRMs) and a C-terminal prion-like domain, the latter being implicated in protein aggregation.
Pathologically, TDP-43 mislocalization and cytoplasmic aggregation are hallmarks of neurodegenerative diseases, notably amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degeneration (FTLD). These aggregates are often hyperphosphorylated, ubiquitinated, or cleaved, serving as disease biomarkers. TARDBP antibodies are essential tools in research and diagnostics, enabling detection of TDP-43 pathology in cellular and tissue samples via techniques like immunohistochemistry (IHC), Western blot, and immunofluorescence.
Antibodies targeting specific TDP-43 epitopes (e.g., phosphorylated residues or disease-associated fragments) help distinguish pathological forms from normal protein. For example, antibodies like pS409/410-TDP-43 are used to identify phosphorylated aggregates in ALS/FTLD. However, variability in antibody specificity (e.g., clone 2E2-D3-A7-C6 vs. others) necessitates careful validation for experimental reproducibility.
Overall, TARDBP antibodies advance understanding of TDP-43’s dual roles in physiology and neurodegeneration, supporting therapeutic development and biomarker studies.