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Annexin VII, also known as synexin, is a member of the Annexin family characterized by Ca2 dependent phospholipid binding. Annexins have a four-fold internal repeat of about 70 amino acids that contains the Ca2 -binding sites. They also have a regulatory NH2-terminal region of 30-40 amino acids. Annexin VII mRNA has been detected in many tissues and is most abundant in brain, heart, skeletal muscle, and lung. Annexin VII mRNA exhibits a tissue dependent polymorphism due to alternative splicing which results in two different isoforms of 47kDa and 51kDa. In vitro, Annexin VII aggregates chromaffin granules and enhances membrane fusion in a Ca2 and GTP-dependent manner. Although the physiological role of Annexin VII is not completely understood, it is believed to influence and regulate Ca2 dependent events such as secretion at the plasma membrane.Immunofluorescence, Immunohistochemistry, Immunoprecipitation, Western Blotting
