Annexins are a superfamily of 13 proteins sharing a high degree of homology. They have in common a core C-terminal domain containing calcium and phospholipid binding motifs, allowing most of them to bind to phospholipid membranes in a calcium-dependent manner. The N-terminal domains vary between family members and provide unique a function.1 Annexin A1 is an endogenous mediator of inflammation, promoting resolution in a number of ways. Normally expressed in intracellular compartments, it is drawn to the cell membrane and both induced and externalized by glucocorticoid response pathways.2,3 The glucocorticoid-induced production and relEAse of annexin A1 is the primary mEAns by which glucocorticoids function as anti-inflammatory agents. Annexin A1 inhibits the synthesis of pro-inflammatory eicosanoids by suppressing the function of sPLA2. This, in turn, limits the recruitment of neutrophils into inflammatory sites and downregulates the production of pro-inflammatory mediators by those neutrophils that enter inflammatory sites.4 MEAnwhile, proteolytic fragments generated in response to incrEAsed expression are implicated in producing a marker for phagocytosis.5 Annexin A1 also functions in the resolution of inflammation by inducing neutrophil apoptosis, and promoting neutrophil clEArance (efferocytosis) by macrophages. The pro-resolving functions of annexin A1 are mediated via binding to FPR2/ALX, a receptor it shares with the specific pro-resolving mediators lipoxin A4 (Item No. 90410) and resolvin D1 (Item No. 10012554).4 The molecules regulatory role has led to investigation of the downstrEAm effects of annexin A1, including cancer, adaptive immunity, and wound repair.6,7,8 Technical Information Synonyms p35 Annexin I ANXA1 Calpactin II Lipocortin I Purity 95% (estimated by SDS-PAGE) Source Recombinant N-terminal His-tagged protein expressed in E. coli MW 40.48 kDa Formulation PBS UniProt Accession P04083