The growth hormone secretagogue receptor (GHSR), a G protein-coupled receptor (GPCR), plays a critical role in regulating growth hormone (GH) release, appetite, and energy metabolism. Primarily expressed in the pituitary and hypothalamus, it binds ghrelin, the "hunger hormone," to stimulate GH secretion and promote feeding behavior. GHSR exists in two isoforms: functional GHSR1a and truncated GHSR1b, with the former mediating most biological effects. Dysregulation of GHSR signaling is implicated in metabolic disorders (e.g., obesity, diabetes), cachexia, and pituitary dysfunction. GHSR antibodies are essential tools for studying receptor localization, expression patterns, and molecular interactions. Due to the hydrophobic nature of GPCRs and low endogenous GHSR expression, developing specific, high-affinity antibodies remains challenging. Current GHSR antibodies (polyclonal/monoclonal) are primarily used in techniques like immunohistochemistry, Western blotting, and flow cytometry to map neural circuits or assess receptor distribution in pathological conditions. Some antibodies target extracellular domains for functional studies, while others recognize intracellular epitopes for signaling pathway analysis. Recent advances include nanobodies and fluorescently labeled antibodies for live-cell imaging. Validated GHSR antibodies are crucial for investigating therapeutic strategies targeting ghrelin signaling, such as anti-obesity treatments. However, inconsistent commercial antibody performance necessitates rigorous validation using knockout models or orthogonal methods.