Concanavalin A, one of most studied lectins for the purification of glycoproteins and sugars, is selected as a model protein. In this study, a Concanavalin A imprinted poly(hydroxyethyl methacrylate) supermacroporous cryogel was prepared for the purification of Concanavalin from jack bean extract. N-Methacryloyl-L-histidine methyl ester with nickel(II) ions was used as the metal ion coordination complex. Concanavalin A imprinted cryogels were characterized by swelling degree, surface area, Fourier transform infrared spectroscopy, scanning electron microscopy and micro computed tomography measurements. Concanavalin A rebinding and desorption on Concanavalin A imprinted and non-imprinted cryogels were measured using a continuous system. Selective binding studies were carried out in the presence of Concanavalin B and bovine serum albumin. The selectivity studies were confirmed by fast protein liquid chromatography studies using jack bean extract from Canavalia ensiformis.