InterphotoreceptorRetinoidBindingProteinFragment (IRBP), a 20-residue peptide and major pathogenic epitope, exists in the first homologous repeat of interstitial visual pigment BindingProtein peptide (IRBP 161-180) and can induce post-uv.
Amyloid A proteins (H2N-Ala-Gly-Leu-Pro-Glu-Lys-Tyr-OH) are a family of apolipoproteins associated with high-density lipoprotein in plasma. Different isoforms of SAA are expressed constitutively at different levels or in response to inflammatory stimuli.
Using specific antisera raised against synthetic peptides, we find that three distinct GTP-bindingprotein 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 bindingprotein (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-bindingprotein 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
IRBP (1-20), human is the 1-20 fragment of interphotoreceptorretinoidbindingprotein (IRBP).This peptide is a 1 to 20 amino acid fragment of the interphotoreceptorretinoidbindingprotein (IRBP). IRBP is a 140-kDa glycolipoprotein residing in the inter