Genes involved in hormone biosynthesis and signaling. Nonspecific adsorption of proteins on solid surfaces such as vessels including disposable test tubes and microtubes frequently results in protein denaturation, leading to their inactivation as well as loss in solution. Such protein adsorption occurs during purification, shipping, storage, and routine experiments, and thus presents a serious problem in biotechnology fields, where protein recovery, stability, and purity are of fundamental importance. For example, it has been reported that immunoglobulin G is adsorbed on Teflon and stainless steel, leading to 
disruption of its tertiary structure and irreversible aggregation. Adsorption of lysozyme and ribonuclease A on silica resulted in loss of enzyme activity. Detergents have been commonly used to suppress such surface adsorption, but have disadvantages: they bind strongly to proteins and are difficult to remove from protein solutions due to micelle formation. In addition, various solution additives have been reported to suppress surface adsorption. For example, more than 3.0 M glycerol and urea were required to reduce the adsorption of RNase A by half at silica-water and air-water interfaces. Salts and sugars also decreased the amount of adsorbed RNase A on polystyrene surfaces at molar concentrations. It should be noted that these additives are effective only at high concentrations. To develop more effective additives that diminish protein adsorption to solid surfaces, especially vessels such as disposable test tubes and microtubes, we tested arginine, which is now widely used as an aggregation suppressor of proteins. Arg was first used as a solution additive to increase refolding yield of recombinant proteins, including human tissue type plasminogen activator, immunoglobulin,, interleukin-6, and interleukin-21. We have also shown that Arg enhances refolding of monomeric and oligomeric proteins, and inhibits heat-induced aggregation. It has been suggested that such effects of Arg are due to the ability to solubilize aggregation-prone denatured proteins, as also indicated by the enhancement of solubility of hydrophobic small compounds by Arg. Due to this function, Arg facilitates protein crystallization, purification, and formulation. In addition to the prevention of proteinprotein interactions, Arg also suppresses binding between proteins and column resins, improving the performance of AbMole Lesinurad chromatography. For example, Arg suppresses nonspecific binding of monoclonal antibodies to the column resins in Protein-A column, gel permeation, affinity column, ion-exchange, and MEP HyperCel chromatography. In the present study, to expand its application, we investigated the effects of Arg on protein adsorption to particles 2 mm in diameter made of polystyrene, which is a commonly-used material for vessels such as disposable test tubes and microtubes.