TRF2 (telomeric repeat-binding factor 2) is a homodimeric protein that binds the double-stranded 5'-TTAGGG-3' repeat in telomeres. It plays a critical role in the maintenance of telomeres, protecting telomeres against end-to-end chromosomal fusion, and recruiting a number of factors/enzymes required for telomere protection such as the shelterin complex/telosome (TRF1, TRF2, TIN2, RAP1, ACD and POT1), RAP1 and DCLRE1B. Together with DCLRE1B/Apollo, TRF2 plays a key role in T-loop formation and preventing aberrant telomere topology.
Immunohistochemistry-Paraffin: TRF2 Antibody
TRF2 also recruits TERF2IP/RAP1 to telomeres to repress unwanted homology-directed repair. To help understand how DNA damage triggers the ATM kinase pathway, Celli, et. al. used the TRF2 antibody and discovered that the process does not require overhang degradation or any other overt DNA processing event (1). Recent studies with TRF2 antibody in the Conomos’ lab found that C-type (TCAGGG) variant repeats that are found throughout telomeres are actually the structural abnormalities responsible for recruiting nuclear receptors like COUP-TF2 and TR4 in alternative lengthening of telomeres (ALT) cells (2). The TRF2 antibody was used in yeast and worm models to examine the components that complex with the KASH and SUN nuclear envelope (NE) proteins during mammalian meiosis (3). In embryonic stem cells, Chang, et. al. employed the TRF2 antibody in their co- localization studies to establish the importance of promyelocytic leukemia (PML) bodies as a scaffold and epigenetic regulators for maintaining telomeres (4). Interestingly, use of TRF2 antibody in kidney epithelial cells found that telomere shortening appears to drive a distinctive microRNA signature indicative of aggressive renal cell carcinomas (5).
Novus Biologicals offer various TRF2 reagents for your research needs including:
