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The present work demonstrates the selective recognition of myoglobin in human serum in the presence of various competitive proteins such as lysozyme, cytochrome c and hemoglobin by using molecularly imprinted affinity cryogels. The imprinted affinity cryogels towards myoglobin were prepared by using cryopolymerization technique. For this purpose, N-methacryloylamido antipyrine (MAAP)-Ce(III) and myoglobin were used as the complex functional monomer and template molecule, respectively. (MAAP)-Ce(III) complex functional in the imprinted cryogel provided a luminescence feature to the cryogel and the detection of the myoglobin was successfully achieved by UV-VIS-Near Infrared (UV-VIS-NIR) Spectroscopy. The effects of some variables such as initial myoglobin concentration, temperature, pH and ionic strength on myoglobin binding to the prepared cryogels were studied. The myoglobin binding capacity of the prepared cryogels was determined to be 68 mgg−1. Myoglobin binding to the cryogels in the presence of competitive proteins lysozyme, cytochrome c and hemoglobin were also performed. The imprinted cryogels exhibited high selectivity towards myoglobin and the obtained binding order under competitive conditions was myoglobin > lysozyme > cytochrome c > hemoglobin.