Biotin-conjugated TDP-43 (C-te

Transactivation response (TAR), DNA-binding protein of 43 kDa (also known as TARDBP or TDP-43), was first isolated as a transcriptional inactivator binding to the TAR DNA element of the HIV-1 virus. Neumann et al. (2006) found that a hyperphosphorylated, ubiquitinated, and cleaved form of TARDBP, known as pathologic TDP-43, is the major component of the tau-negative and ubiquitin-positive inclusions that characterize amyotrophic lateral sclerosis (ALS) and the most common pathological subtype of frontotemporal lobar degeneration (FTLD-U). 12892-1-AP is a rabbit polyclonal antibody raised against the C-terminal amino acids of human TDP-43. This antibody recognizes the cleavage product of 20-30 kDa in addition to the native and phosphorylated forms of TDP-43. Immunohistochemical analyses of TDP-43 using this antibody detect both normal diffuse nuclear staining and insoluble inclusions in pathologic tissues. Various forms of TDP-43 exist, including 18-35 kDa of cleaved C-terminal fragments, 45-50 kDa phosphoprotein, 55 kDa glycosylated form, 75 kDa hyperphosphorylated form, and 90-300 kDa cross-linked form. (17023659,19823856,21666678,22193176)

Recently TDP-43 has been reported to be overexpressed in triple negative breast cancer (TNBC) and it may be a potential target for TNBC diagnosis and drug design. (29581274)