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.

Western blot analysis: 2-4 µg/ml, Immunohistochemical analysis: 5 µg/ml

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