S100A5 Mouse

S100 Calcium Binding Protein A5 (S100A5) is a member of the S100 family of proteins, which are characterized by their ability to bind calcium ions through EF-hand motifs. These proteins are involved in various cellular processes, including cell cycle progression and differentiation . The mouse recombinant form of S100A5 is produced in E. coli and is a single, non-glycosylated polypeptide chain containing 117 amino acids, with a molecular mass of approximately 13.4 kDa .

S100A5 contains two EF-hand calcium-binding motifs, which are helix-loop-helix structures that coordinate the binding of calcium ions. This protein has a significantly higher affinity for calcium ions compared to other S100 proteins, with a Ca2+ affinity 20- to 100-fold higher . Additionally, S100A5 can bind zinc (Zn2+) and copper (Cu2+) ions. The binding of Cu2+ ions is particularly strong and can impair the binding of Ca2+ ions .

S100A5 is expressed in very restricted regions of the adult brain, indicating a specialized role in neural function . The protein is localized in the cytoplasm and/or nucleus of a wide range of cells, where it participates in the regulation of cellular processes .

The primary function of S100A5 is to bind calcium ions, which is crucial for its role in cellular signaling pathways. By binding calcium, S100A5 can influence various cellular activities, including cell growth, motility, and differentiation. The ability to bind other metal ions like zinc and copper suggests additional regulatory roles in cellular metabolism and homeostasis .

The recombinant form of S100A5 (Mouse) is produced in E. coli, a common host for protein expression due to its rapid growth and ability to express high levels of recombinant proteins. The recombinant protein includes a 24 amino acid His-Tag at the N-terminus, which facilitates purification through affinity chromatography .

Recombinant S100A5 is used in various research applications to study its role in cellular processes and its potential involvement in diseases. The high affinity for calcium and other metal ions makes it a valuable tool for investigating metal ion homeostasis and signaling pathways in cells.