Interphotoreceptorretinoid-binding protein (668-687) is an amino acid residue of human retinoid-binding protein (IRBP 668-687) that can induce uveitis.
Interphotoreceptorretinoid-binding protein(668-687) TFA is the 668-687 amino acid residue of human Interphotoreceptorretinoidbinding protein(IRBP), which can induce uveitis.
Using specific antisera raised against synthetic peptides, we find that three distinct GTP-binding protein alpha subunits remain bound to the plasma membrane even after activation with nonhydrolyzable GTP analog. Trypsin cleaves each alpha subunit at a si
Tumor protein p53 binding protein (53BP1) has been identified in a yeast two-hybrid screen as a protein that interacts with the central DNA–binding domain of p532. Similar to breast cancer susceptibility gene 13, 4 (BRCA1; 53BP1 enhances p53-dependent tra
Vitamin D-binding protein is a multifunctional, highly expressed, polymorphic serum protein. These range from the transport of vitamin D metabolites to possible roles in the immune system and host defense. The molecular weight range, the time course of ap
InterphotoreceptorRetinoidBinding Protein Fragment (IRBP), a 20-residue peptide and major pathogenic epitope, exists in the first homologous repeat of interstitial visual pigment Binding Protein peptide (IRBP 161-180) and can induce post-uv.