Insulin β ChainPeptide (15-23), also referred to as INS, is an insulin-derived peptide that is specifically recognized by islet-associated T cells. The tetramer of Insulin β ChainPeptide (15-23) effectively stained the INS-reactive CTL clone G9C8; however, neither this tetramer nor the negative control tetramer (TUM) exhibited staining on the splenic CD8+ T cells obtained from NOD or 8.3-TCRαβ transgenic NOD mice.
Thrombin is a trypsin-like serine protease that is encoded by the F2 gene in humans. Thrombin is produced by the enzymatic cleavage of two sites on prothrombin by activated Factor X (Xa). Thrombin in turn acts as a serine protease that converts soluble
This peptide is a fragment of the alpha-chain of insulin amino acids 1 to 13. The insulin a-chain epitope recognized by human T cells is posttranslationally modified.
Small Cardioactive Peptide B (SCPB), a neurally active peptide, stimulates adenylate cyclase activity in particulate fractions of both heart and gill tissues with EC50s of 0.1 and 1.0 μM, respectively.
Human proinsulin, the single-chainpeptide precursor of insulin, consists of the insulin A and B chains connected by the 31 amino acid C-peptide. Cleavage of proinsulin by proteolytic enzymes produces insulin and free C-peptide.