Anti-phospho TIN2 (Ser295) Antibody

The telomere-associated protein 1 interacting nuclear factor 2 (TIN2, TINF2, DKCA3) is a 40kDa protein critical to telomere function. TIN2 has no known enzymatic activity, but interacts with double-stranded and single-stranded telomeric DNA-binding proteins. Specifically, TIN2 directly binds to the telomeric dsDNA-binding proteins TRF1 and TRF2, and to TPP1, which forms a heterodimer with the telomeric ssDNA-binding protein POT1. TIN2 functions in telomere length as TIN2 knockdown results in moderate telomere elongation, as well as destabilization of TRF1 and TRF2. Complete knockout of TIN2 causes severe telomere dysfunction. The action of TIN2 is at least partially mediated by phosphorylation. TIN2 is phosphorylated at S295 and S330 amino acids. The level of phosphorylated TIN2 is up regulated during mitosis. The consequence of TIN2 phosphorylation during mitosis remains to be determined as initial results using non-phosphorylated mutants failed to show any differences between mutants and wildtype phenotypes. Phospho-TIN2 (S295) is created by phosphorylating TIN2 by the kinase RSK2.

Epitope: Phosphorylated S295

Linear peptide corresponding to human TIN2 .

Anti-phospho TIN2 (Ser295) antibody is an antibody against phospho TIN2 (Ser295) for use in western blotting.

Western Blotting Analysis: A 1:500 dilution from a representative lot detected TIN2 in 10 µg of HeLa cell lysate transfected with TIN2 AA mutant and HeLa cell lysate transfected with TIN2 wild-type.
Western Blotting Analysis: A representative lot detected TIN2 in nocodazole treated HeLa cell lysate (Yang, S., and Counter, C. M., PLoS One. 8(8):e71697).

Evaluated by Western Blotting in Hela acid extract cell lysate.

Western Blotting Analysis: A 1:500 dilution of this antibody detected TIN2 in 10 µg of Hela acid extract cell lysate.

~40 kDa observed. Uniprot describes 3 isoforms produced by alternative splicing at ~50 kDa (Isoform 1), ~39 kDa (Isoform 2), and ~15 kDa (Isoform 3). Uncharacterized band(s) may appear in some lysates.