Annexin A5, also known as Annexin V, is a member of the annexin family of proteins. These proteins are known for their ability to bind to phospholipids in a calcium-dependent manner. Annexin A5 is particularly notable for its role in binding to phosphatidylserine (PS), a phospholipid that is normally located on the inner leaflet of the cell membrane but becomes exposed on the outer leaflet during apoptosis (programmed cell death).
Annexin A5 was first discovered in the human placenta in 1979 . It is a relatively small protein, consisting of 320 amino acids and having a molecular weight of approximately 35 kDa. The protein is characterized by its ability to form a trimeric structure, which is essential for its biological functions.
Annexin A5 performs a variety of biological functions, primarily through its interaction with phosphatidylserine. Some of its key roles include:
Recombinant human Annexin A5 is produced using genetic engineering techniques. The gene encoding Annexin A5 is inserted into an expression vector, which is then introduced into a host cell (such as E. coli or yeast). The host cells produce the protein, which is subsequently purified for use in research and therapeutic applications.
Annexin A5 has several important applications in both clinical and research settings: