TDP-43, a heterogeneous nuclear ribonucleoprotein, was identified as a component of ubiquitin-positive and tau-negative inclusions observed in cases of frontotemporal lobar degeneration (FTLD-U) and amyotrophic lateral sclerosis (ALS). Immunochemical analyses using antibodies generated against phospho- and non-phosphopeptides of human TDP-43 revealed that abnormally phosphorylated full-length TDP-43 (45 kDa), C-terminal fragments (~25 kDa) and smearing substances are deposited as intracellular inclusions in affected regions of FTLD-U and ALS cases.

These antibodies are powerful tools for biochemical and immunohistochemical analyses of neurodegenerative diseases and for evaluation of cellular or animal models of TDP-43 proteinopathy.

TDP-43, a heterogeneous nuclear ribonucleoprotein, was identified as a component of ubiquitin-positive and tau-negative inclusions observed in cases of frontotemporal lobar degeneration (FTLD-U) and amyotrophic lateral sclerosis (ALS). Immunochemical analyses using antibodies generated against phospho- and non-phosphopeptides of human TDP-43 revealed that abnormally phosphorylated full-length TDP-43 (45 kDa), C-terminal fragments (~25 kDa) and smearing substances are deposited as intracellular inclusions in affected regions of FTLD-U and ALS cases.

These antibodies are powerful tools for biochemical and immunohistochemical analyses of neurodegenerative diseases and for evaluation of cellular or animal models of TDP-43 proteinopathy.