Anti-S-100(beta-subunit) (Clone: SH-B1)

S100 protein is a 21,000-Da component first isolated from brain by Moore(1965). Immunocytochemical studies demonstrated that S100 protein is produced by a wide variety of normal and neoplastic cells of mesodermal, neuroectodermal, and epithelial origin(Herrera et al., 1988). The S100 molecule is a dimer, thus there are 3 forms of S100: alpha-alpha, known as S-100a(0), alpha-beta, known as S-100a, and beta-beta, known as S-100b. S100 genes are clustered on human chromosome 1q21. S-100 protein expression by primary and metastatic adenocarcinomas. Protein function: Weakly binds calcium but binds zinc very tightly- distinct binding sites with different affinities exist for both ions on each monomer. Physiological concentrations of potassium ion antagonize the binding of both divalent cations, especially affecting high-affinity calcium-binding sites. Binds to and initiates the activation of STK38 by releasing autoinhibitory intramolecular interactions within the kinase. Interaction with AGER after myocardial infarction may play a role in myocyte apoptosis by activating ERK1/2 and p53/TP53 signaling. Could assist ATAD3A cytoplasmic processing, preventing aggregation and favoring mitochondrial localization. May mediate calcium-dependent regulation on many physiological processes by interacting with other proteins, such as TPR-containing proteins, and modulating their activity. [The UniProt Consortium]