S100 Calcium Binding Protein A8, also known as S100A8, is a member of the S100 family of proteins. These proteins are characterized by their ability to bind calcium ions through EF-hand motifs, which are helix-loop-helix structural domains . S100A8 is predominantly expressed in cells of the myeloid lineage, such as neutrophils and monocytes .
S100A8 is a small protein with a molecular mass of approximately 10.3 kDa . It contains two EF-hand calcium-binding motifs, which are crucial for its function . The protein is mainly localized in the cytoplasm but can translocate to the plasma membrane or be released into the extracellular environment upon cellular activation .
S100A8 plays a significant role in the regulation of inflammatory processes and the immune response . It can induce neutrophil chemotaxis and adhesion, which are essential for the immune system’s response to infection and injury . S100A8 often forms a heterodimer with S100A9, another member of the S100 family, to create a complex known as calprotectin . This complex has a wide range of intra- and extracellular functions, including the regulation of leukocyte adhesion and migration, promotion of cytokine and chemokine production, and antimicrobial activity .
Altered expression of S100A8 is associated with various diseases, including cystic fibrosis and psoriasis . In cystic fibrosis, the protein’s expression is significantly increased, which may contribute to the chronic inflammation observed in patients . Additionally, S100A8 has been implicated in the pathogenesis of other inflammatory diseases and certain cancers .
Recombinant S100A8 (Mouse) is produced using Escherichia coli expression systems . The recombinant protein is used in various research applications, including studies on inflammation, immune response, and cancer . It is available in different formulations and concentrations, with high purity levels confirmed by SDS-PAGE analysis .