Human TRF‑1 Antibody

TRF-1 (telomeric repeat-binding factor 1; also Pin2) is a nuclear protein that participates in telomere homeostasis. Although its predicted molecular weight is 50 kDa, it runs anomalously at 60 kDa in SDS-PAGE. TRF-1 binds as a dimer to the ends of chromosomes (telomeres), where it blocks telomerase activity, promoting normal cell senescence and turnover. Human TRF-1 is 439 amino acids (aa) in length. It contains an N-terminal acidic region (aa 2‑64), a dimerization domain (aa 65‑265), an NLS (aa 337‑356), and a DNA binding HTH myb-type domain (aa 375‑432). Phosphorylation of TRF-1 at Ser435 mediates its binding to DNA. One alternate splice form shows a deletion of aa 295‑315 that may be accompanied by a 36 aa N-terminal extension. Over aa 136‑295, human TRF-1 shares 72% aa identity with mouse TRF-1.