Monoclonal Anti-TRF1 antibody produced in mouse has been used in Western blotting and enzyme linked immunosorbent assay (ELISA).
Monoclonal Anti-TRF1 (mouse IgG1 isotype) is derived from the TRF-78 hybridoma produced by the fusion of mouse myeloma cells and splenocytes from mice immunized with a human TRF1 protein produced in baculovirus. TRF1 and TRF2 (TTAGGG repeat binding factors) are two major proteins that bind to human telomers. TRF1 has a DNA binding domain with high homology to the Myb family of transcription factors. Unlike the Myb family that contains only one DNA binding motif, TRF1 has multiple of this motif.
TRF1 (TTAGGG repeat binding factor 1) has a negative effect on the length of the telomer. Overexpression of TRF1 in cancer cells that contain telomerase activity, causes the shortening of the length of their telomers. While inhibition of TRF1 causes the elongation of telomers. It was shown that the level of TRF1 in the cells does not affect the expression of the telomerase protein. This suggests that TRF1 may act directly on the activity of the telomerase protein. Tankyrase is a protein that interacts with TRF1 and its C-terminal region is homologous to poly (adenosine dinucleotide phosphate (ADP)-ribose) polymerase (PARP). In response to DNA damage, the PARP protein mediates ADP-ribose polymers of protein acceptors. In vitro studies have shown that tankyrase is responsible for that polyribosylation of TRF1, which in turn abolishes its ability to bind telomers.
