The family of EF-hand type Ca2+-binding proteins includes calbindin (previously designated vitamin D-dependent Ca2+-binding protein), S-100 α and β, calgranulins A (also designated MRP8), B (also designated MRP14) and C (S-100 like proteins), and the parvalbumin family members, including parvalbumin α and parvalbumin β (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 α chain and S-100 β chain. Three S-100 dimeric forms have been characterized, differing in their subunit composition of either two α chains, two β chains or one α and one β chain. S-100 localizes to the cytoplasm and nuclei of astrocytes, Schwann's cells, ependymomas and astrogliomas. S-100 is also detected in almost all benign naevi, malignant melanocytic tumours and in Langerhans cells in the skin. Calbindin, S-100 proteins and parvalbumin proteins are each expressed in neural tissues. In addition, S-100 α and β are present in a variety of other tissues, and calbindin is present in intestine and kidney.