Ghrelin, a 28-amino-acid peptide hormone predominantly secreted by the stomach, was discovered in 1999 as the endogenous ligand for the growth hormone secretagogue receptor (GHSR). It plays a critical role in regulating appetite, energy balance, and growth hormone release. Ghrelin exists in acylated (active) and des-acylated forms, with acylation mediated by ghrelin O-acyltransferase (GOAT) being essential for its biological activity. Its levels fluctuate with feeding states, rising during fasting to stimulate hunger and decreasing postprandially. Dysregulation of ghrelin signaling is linked to obesity, metabolic disorders, and eating-related pathologies.
GHRL antibodies are immunological tools targeting ghrelin or its related proteins (e.g., GHSR, GOAT). These antibodies enable researchers to quantify ghrelin concentrations, map its distribution in tissues, or block its activity in experimental models. Applications span basic research (e.g., studying energy homeostasis mechanisms), clinical diagnostics (assessing ghrelin in metabolic diseases), and drug development (evaluating therapeutic candidates). Challenges include distinguishing between ghrelin isoforms and ensuring specificity given structural similarities with other peptides. Both monoclonal and polyclonal variants exist, optimized for techniques like ELISA, immunohistochemistry, or Western blot. Recent studies also explore ghrelin's roles beyond metabolism, including cognitive function and stress responses, further driving antibody utility in interdisciplinary research.