Anti-S100B, clone SPM354

1 mg/ml in 1X PBS, BSA free, sodium azide free. S100 belongs to the family of calcium binding proteins. S100A and S100B proteins are two members of the S100 family. S100A is composed of an alpha and a beta chain whereas S100B is composed of two beta chains. This antibody is specific against an epitope located on the beta-chain (i.e. in S-100A and S-100B) but not on the alpha-chain of S-100 (i.e. in S-100A and S100A0). This antibody can be used to localize S-100A and S-100B in various tissue sections. S-100 protein has been found in normal melanocytes, Langerhans cells, histiocytes, chondrocytes, lipocytes, skeletal and cardiac muscle, Schwann cells, epithelial and myoepithelial cells of the breast, salivary and sweat glands, as well as in glial cells. Neoplasms derived from these cells also express S-100 protein, albeit non-uniformly. A large number of well-differentiated tumors of the salivary gland, adipose and cartilaginous tissue, and Schwann cell-derived tumors express S-100 protein. Almost all malignant melanomas and cases of histiocytosis X are positive for S-100 protein. 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]