Anti-TRF2 (Clone: ABM10H3)

TRF2 (Telomere Repeat Binding Factor 2), a subunit of the shelterin complex, binds to duplex telomeric DNA and plays a crucial role in telomere protection. TRF2 contains an N-terminal basic domain rich in glycines and arginines (the GAR domain), a central TRFH dimerization domain, a flexible linker region and a C-terminal Myb-like DNA binding domain. TRF2 undergoes extensive post-translational modification, which in turn regulates its stability, DNA binding and cellular localization. Ubiquitylation of TRF2 by Siah1, an E3 ligase, promotes TRF2 degradation and replicative senescence of human primary fibroblasts. TRF2 is phosphorylated in response to DNA damage and this phosphorylation has been implicated in DNA double strand break repair. Protein function: Binds the telomeric double-stranded 5'-TTAGGG-3' repeat and plays a central role in telomere maintenance and protection against end-to-end fusion of chromosomes. In addition to its telomeric DNA-binding role, required to recruit a number of factors and enzymes required for telomere protection, including the shelterin complex, TERF2IP/RAP1 and DCLRE1B/Apollo. Component of the shelterin complex (telosome) that is involved in the regulation of telomere length and protection. Shelterin associates with arrays of double-stranded 5'-TTAGGG-3' repeats added by telomerase and protects chromosome ends, without its protective activity, telomeres are no longer hidden from the DNA damage surveillance and chromosome ends are inappropriately processed by DNA repair pathways. Together with DCLRE1B/Apollo, plays a key role in telomeric loop (T loop) formation by generating 3' single- stranded overhang at the leading end telomeres: T loops have been proposed to protect chromosome ends from degradation and repair. Required both to recruit DCLRE1B/Apollo to telomeres and activate the exonuclease activity of DCLRE1B/Apollo. Preferentially binds to positive supercoiled DNA. Together with DCLRE1B/Apollo, required to control the amount of DNA topoisomerase (TOP1, TOP2A and TOP2B) needed for telomere replication during fork passage and prevent aberrant telomere topology. Recruits TERF2IP/RAP1 to telomeres, thereby participating in to repressing homology- directed repair (HDR), which can affect telomere length. [The UniProt Consortium]