TERF1 Antibody – Goat Polyclonal

This gene encodes a telomere specific protein which is a component of the telomere nucleoprotein complex. This protein is present at telomeres throughout the cell cycle and functions as an inhibitor of telomerase, acting in cis to limit the elongation of individual chromosome ends. The protein structure contains a C-terminal Myb motif, a dimerization domain near its N-terminus and an acidic N-terminus. Two transcripts of this gene are alternatively spliced products. [provided by RefSeq, Jul 2008]

TRF1: a telomeric repeat binding factor. Binds the telomeric double-stranded TTAGGG repeat and negatively regulates telomere length. Colocalizes with telomeric DNA in interphase and metaphase cells and is located at chromosome ends during metaphase. Involved in the regulation of the mitotic spindle. Expression is tightly regulated during the cell cycle; levels are low in G1 and S phase and increase during G2 phase and mitosis. Two splice variant isoforms have been described.

Protein type: DNA-binding

Chromosomal Location of Human Ortholog: 8q21.11

Cellular Component: chromosome, telomeric region; cytoplasm; nuclear chromosome, telomeric region; nuclear telomere cap complex; nucleolus; nucleoplasm; nucleus; spindle

Molecular Function: DNA bending activity; DNA binding; double-stranded telomeric DNA binding; microtubule binding; protein binding; protein heterodimerization activity; protein homodimerization activity; telomerase activity; telomeric DNA binding; ubiquitin binding

Biological Process: cell division; G2/M transition of mitotic cell cycle; mitosis; mitotic cell cycle spindle assembly checkpoint; negative regulation of DNA replication; negative regulation of telomerase activity; negative regulation of telomere maintenance via semi-conservative replication; negative regulation of telomere maintenance via telomerase; positive regulation of apoptosis; positive regulation of microtubule polymerization; positive regulation of mitosis; positive regulation of mitotic cell cycle; protein homooligomerization; response to drug; telomere capping; telomere clustering; telomere maintenance; telomere maintenance via telomerase; telomeric loop formation