TP53BP1 tudor-like region (human recombinant)

Tudor domains are small protein structural motifs of ~50 amino acids related to the "royal family" of methyl readers, which also includes chromo, MBT, PWWP, and Agenet-like domains. Tudor domains occur either alone, in tandem, or with other domains. They are found in many proteins that are involved in RNA metabolism, germ cell development, transposon silencing, DNA damage response, histone modification, and chromatin remodeling. Tudor domains recognize symmetric methylated arginine or methylated lysine residues. TP53BP1 binds both histone and non-histone substrates. Binding of TP53BP1 to dimethylated lysine 382 on p53 (p53 K382me2), as well as histone H4K20me2, through the tudor domain, has been shown to be important for TP53BP1 localization to DNA double strand breaks. This product contains the tudor domain of TP53BP1.Synonyms: 53BP1, Tumor Suppressor p53-binding Protein 1. Purity: >90%. Source: Recombinant N-terminal GST-tagged protein expressed in E. coli. Amino Acids: 1717-1972 (N- and C-terminal truncations). MW: 42.6 kDa. Formulation: (Request formulation change), 50 mM Tris-HCl, pH 8.0, containing 150 mM sodium chloride and 20% glycerol. UniProt Accession #: Q12888.