The family of EF-hand type Ca2+-binding proteins includes calbindin (previously designated vitamin D-dependent Ca 2+-binding protein), S-100 (alpha) and (beta), calgranulins A (also designated MRP8), B (also designated MRP14) and C (S-100 like proteins), and the parvalbumin family members, including parvalbumin (alpha) and parvalbumin (beta) (also designated oncomodulin). The S-100 protein is involved in the regulation of cellular processes such as cell cycle progression and differentiation. Research also indicates that the S-100 protein may function in the activation of Ca2+ induced Ca2+ release, inhibition of microtubule assembly and inhibition of protein kinase C mediated phosphorylation. Two S-100 subunits, sharing 60% sequence identity, have been described as S-100(alpha) chain and S-100(beta) chain. Three S-100 dimeric forms have been characterized, differing in their subunit composition of either two (alpha) chains, two (beta) chains or one (alpha) and one (beta) chain.