S100A9 is supplied as a sterile filtered yellowish solution.
S100 calcium-binding protein A9 (S100A9), also known as migration inhibitory factor-related protein 14 (MRP14) or calgranulin B, is a member of the S100 family of proteins. These proteins are characterized by the presence of two EF-hand calcium-binding motifs . S100A9 is predominantly found in the cytoplasm and/or nucleus of a variety of cells and plays a crucial role in regulating numerous cellular processes, including cell cycle progression and differentiation .
S100A9 forms a heterodimer with another S100 protein, S100A8, to create calprotectin . This complex is involved in the regulation of myeloid cell function by binding to Toll-like receptor 4 (TLR4) and the receptor for advanced glycation end products (RAGE) . Intracellularly, S100A9 influences mitochondrial homeostasis within neutrophils, affecting their response to bacterial pathogens .
The S100A9 protein is implicated in various physiological and pathological processes. For instance, it plays a role in the body’s response to vascular injury by promoting leukocyte recruitment and regulating vascular inflammation . Additionally, altered expression of S100A9 is associated with diseases such as cystic fibrosis .
S100A9 has been studied for its potential as a biomarker for inflammatory diseases and atherothrombosis . Its role in promoting skin regeneration through the TLR-4 pathway during tissue expansion has also been explored . These findings suggest that S100A9 could be a target for therapeutic interventions in various inflammatory and regenerative conditions.