S100A8 Human
Description
Product Specs
Product Science Overview
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 and zinc ions, which plays a crucial role in their function. S100A8 is predominantly found in the cytoplasm and/or nucleus of a wide range of cells and is involved in various cellular processes, including the regulation of inflammatory responses and immune functions .
S100A8 contains two EF-hand calcium-binding motifs, which are helix-loop-helix structural domains capable of binding calcium ions. This protein often forms a heterodimer with S100A9, another member of the S100 family, to create calprotectin. Calprotectin has a wide range of intra- and extracellular functions, including facilitating leukocyte arachidonic acid trafficking and metabolism, modulating the cytoskeleton during phagocyte migration, and activating the neutrophilic NADPH-oxidase .
S100A8 plays a prominent role in the regulation of inflammatory processes and immune responses. It can induce neutrophil chemotaxis and adhesion, which are critical steps in the immune response to infection. Additionally, S100A8 acts as an alarmin or a danger-associated molecular pattern (DAMP) molecule, stimulating innate immune cells by binding to pattern recognition receptors such as Toll-like receptor 4 (TLR4) and receptor for advanced glycation end products (AGER). This binding activates signaling pathways that amplify the pro-inflammatory cascade .
Altered expression of S100A8 is associated with various diseases, including cystic fibrosis and post-COVID-19 conditions. Its role as an oxidant scavenger helps prevent exaggerated tissue damage by scavenging oxidants, which is crucial in inflammatory diseases. Moreover, S100A8 has antimicrobial activity against bacteria and fungi, likely through the chelation of zinc ions essential for microbial growth .
