Human/Mouse/Rat Annexin A1 Alexa Fluor™ Plus 647‑conjugated Antibody

The Annexins are a family of Calcium-dependent phospholipid-binding proteins that are preferentially located on the cytosolic face of the plasma membrane. The Annexins have a molecular weight of approximately 35 to 40 kDa and consist of a unique amino terminal domain followed by a homologous C-terminal core domain containing the calcium-dependent phospholipid-binding sites. The C‑terminal domain is comprised of four 60‑70 amino acid repeats, known as annexin repeats or an endonexin fold (Annexin A6 contains 8 annexin repeats). The four annexin repeats form a highly alpha -helical, tightly packed disc known as the annexin domain, which binds to phospholipids in the membrane in a calcium-dependent manner. Members of the annexin family play a role in cytoskeletal interactions, phospholipase inhibition, regulation of cellular growth, and intracellular signal transduction pathways. Annexin A1 (ANXA1), also known as annexin I, lipocortin I, and calpactin II, is an ~ 40 kDa protein with phospholipase A2 inhibitory activity. Since phospholipase A2 is required for the biosynthesis of the potent mediators of inflammation, prostaglandins and leukotrienes, Annexin A1 may have anti-inflammatory activity. Human Annexin A1 shares 88 and 89% amino acid sequence identity with mouse and rat Annexin A1, respectively.