TARDBP was firstly found as a transcriptional repressor that binds to chromosomally integrated TAR DNA and represses HIV-1 transcription. It was also reported to regulate alternate splicing of the CFTR gene. Neumann et al. (2006) found that a hyperphosphorylated, ubiquitinated, and cleaved form of TDP43, known as pathologic TDP43, is the major disease protein in ubiquitin-positive, tau-, and alpha-synuclein-negative frontotemporal dementia (FTLD-U) and in Amyotrophic lateral sclerosis (ALS). 60019-1-Ig and 60019-2-Ig are both mouse monoclonal antibodies which were generated against N-terminal recombinant protein of human TDP43. Recently the epitope of 60019-2-Ig has been determined to locate at residues "TEDELRE"203-209aa by Hiroshi Tsuji et al. (2011). It has been reported that this antibody can stain the abnormally phosphorylated C-terminal fragments of 23-24 kDa in addition to normal TDP-43 in ALS and FTLD brains. This antibody recognize Human TDP43 only.