TRF1 binds the double-stranded telomeric repeat sequence, TAGGG. TRF1 and TRF2 are key components of vertebrate telomeres and bind to double-stranded telomeric DNA as homodimers. Dimerization involves the TRF homology (TRFH) domain, which also mediates interactions with other telomeric proteins. Fairall et al. (2001) determined the crystal structures of the dimerization domains from human TRF1 and TRF2 at 2.9- and 2.2-angstrom resolution, respectively. Despite a modest sequence identity, the 2 TRFH domains have the same entirely alpha-helical architecture, resembling a twisted horseshoe. The dimerization interfaces feature unique interactions that prevent heterodimerization. Mutational analysis of TRF1 corroborated the structural data and underscored the importance of the TRFH domain in dimerization, DNA binding, and telomere localization.
Suitable for use in Immunofluorescence, ELISA and Western Blot. Other applications not tested.
Optimal dilutions to be determined by the researcher.
Cellular Localization: Nuclear
Storage and Stability:
May be stored at 4 degrees C for short-term only. For long-term storage and to avoid repeated freezing and thawing, add sterile glycerol (40-50%), aliquot and store at -20 degrees C. Aliquots are stable for at least 3 months at -20 degrees C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.