The use of highly purified immunoglobulin became among the most powerful adopted strategies in therapeutic trials nowadays. Their role as immunomodulatory and anti-inflammatory agents has widened their scope of use. A novel continuous supermacroporous monolithic cryogels embedded with histidine-epoxy-activated-sepharose beads were synthetized as a new monolithic adsorbents for the separation of immunoglobulin G from human serum. The histidine-epoxy-activated-sepharose beads were embedded into the 2-hydroxyethyl methacrylate (HEMA) cryogels present in frozen aqueous solution inside a plastic syringe. The microstructure morphology of the cryogels was characterized by swelling measurement and scanning electron microscopy. The adsorption of human IgG on the histidine-epoxy-activated-sepharose beads pHEMA cryogels appeared to follow the Langmuir-Freundlich adsorption isotherm model. The maximum IgG adsorption was observed at 4 degrees C and pH 7.4 and was found to be 26.95mg/g of cryogel which is close to that obtained experimentally (24.49mg/g). The cryogels were used for several adsorption-desorption cycles without any negligible decrease in their adsorption capacity.