Detection of Human TRF‑1 by Western Blot. |
Western blot shows lysates of Jurkat human leukemic T cell line and Raji human Burkitt's lymphoma cell line. Gels were loaded with 30 μg of whole cell lysate (WCL), 20 μg of cytoplasmic (Cyto), and 10 μg of nuclear extracts (Nuc). PVDF membrane was probed with 1 µg/mL Sheep Anti-Human TRF‑1 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF5300) followed by HRP-conjugated Anti-Mouse IgG Secondary Antibody (Catalog # HAF007). A specific band for TRF‑1 was detected at approximately 60 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.
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.
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