The enzyme family of DNA polymerases plays a fundamental role in the replication, repair, and recombination of nucleic acid. Its members include DNA Polymerase b (Pol b), DNA Polymerase g (Pol g), and DNA Polymerase m (Pol m). TdT is a very unique and fascinating member of this family because, unlike all other DNA polymerases, TdT synthesizes DNA from only single-stranded DNA. This unusual ability to work in a completely template-independent manner was discovered early on (TdT was one of the first activities found in mammals) but not well understood1. An excellent summary of the history, structure, and function of TdT can be found in Motea and Berdis' review2. It is now evident that such random nucleotide addition allows V(D)J recombination and therefore drives the evolution, flexibility, and diversity of the vertebrate immune system.
Immunocytochemistry/Immunofluorescence: TdT Antibody
Without TdT, the body could not generate the sophisticated multitude of immunoglobulins and T-cell antigen receptors required for innate immunity as demonstrated by McElhinny’s group3. TdT expression is specifically limited to primary lymphoid tissues such as the thymus and bone marrow4,5. There is an accumulated body of data to suggest that changes in TdT expression and activity modulate cancer initiation, tumor progression, and chemotherapy response. For example, it is overexpressed in ALL and AML (reviewed by Motea). Additionally, it appears to be an efficient method for labeling double-stranded DNA breaks both in vivo and in vitro through assays such as TUNEL.
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