S100A8 Human, His

S100 Calcium Binding Protein A8, also known as S100A8 or calgranulin A, is a member of the S100 family of proteins. These proteins are characterized by their ability to bind calcium through EF-hand motifs, which are helix-loop-helix structural domains . S100A8 is predominantly found in the cytoplasm and/or nucleus of a wide range of cells and plays a crucial role in regulating various cellular processes, including cell cycle progression and differentiation .

S100A8 is a calcium- and zinc-binding protein that forms a heterodimer with S100A9, known as calprotectin . This heterodimer has a wide range of intra- and extracellular functions, particularly in the regulation of inflammatory processes and immune responses . S100A8 can induce neutrophil chemotaxis and adhesion, making it a significant player in the body’s defense mechanisms .

The S100A8 gene is located on chromosome 1q21 and is part of a cluster of at least 13 S100 genes . Multiple transcript variants encoding different isoforms of S100A8 have been identified, indicating the complexity and versatility of this protein .

Altered expression of S100A8 is associated with various diseases, including cystic fibrosis and inflammatory conditions . The protein’s role in inflammation and immune response makes it a potential biomarker for these diseases and a target for therapeutic interventions .

The human recombinant form of S100A8, tagged with a His (histidine) tag, is produced using recombinant DNA technology. This involves inserting the gene encoding S100A8 into an expression vector, which is then introduced into a host cell (commonly E. coli) to produce the protein. The His tag facilitates the purification of the recombinant protein through affinity chromatography, allowing for the isolation of high-purity S100A8 for research and clinical applications.