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It is unique among performance\u2010enhancing peptides due to the presence of a reactive maleimidopropionic acid group that covalently links the peptide to free thiols on the surface of plasma proteins. Once conjugated, CJC\u20101295 remains active in the bloodstream for significantly longer than non\u2010conjugated peptide\u2010based drugs that are rapidly excreted. Conjugation of CJC\u20101295 to plasma proteins prevents its detection by top\u2010down mass\u2010spectrometry\u2010based peptide screening protocols as it effectively becomes a macromolecular protein with an undefined molecular weight. Using a pair of monoclonal antibodies raised against the CJC\u20101295 peptide, we present an immuno\u2010polymerase chain reaction (I\u2010PCR) assay that is capable of detecting the CJC\u20101295\u2010protein conjugate at concentrations down to 0.8\u00a0pg\/mL. Detection of endogenous equine GHRH necessitated a screening threshold for CJC\u20101295 in equine plasma of 50\u00a0pg\/mL. 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