Recombinant Human Annexin V/ANXA5 protein

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

Annexin V also known as ANXA5 is a protein with a mass of approximately 35-36 kDa. This protein belongs to the annexin family which includes proteins capable of binding to phospholipids in a calcium-dependent manner. Annexin V is mostly expressed in placental tissue though it can be found in various other tissues like the vascular endothelium. Researchers often utilize annexin V for staining dead cells or identifying apoptosis using assays such as annexin V FITC or 7-AAD staining. It forms part of the annexin V binding buffer which enhances its binding affinity.

Biological function summary

Annexin V has an important role in cell membrane dynamics and signaling. The protein does not function as part of a larger complex but its ability to bind negatively charged phospholipids like phosphatidylserine makes it important in apoptosis. During apoptosis phosphatidylserine translocates to the outer leaflet of the plasma membrane where annexin V marks these apoptotic cells. This property enables annexin V-based assays to detect early stages of apoptosis.

Pathways

Annexin V involvement is seen in pathways associated with blood coagulation and apoptosis. In the apoptosis pathway annexin V interacts with apoptotic markers to identify dying cells. It relates to proteins such as caspases which are key executors of apoptosis. In coagulation annexin V has been shown to interact with prothrombinase complex and can affect calcium ion concentration thereby influencing blood clotting processes.

Annexin V plays a role in antiphospholipid syndrome and cardiovascular diseases. Annexin V has been researched for its connection to antiphospholipid antibodies where it affects normal annexin V function impacting clot formation. In cardiovascular diseases annexin V can interact with proteins such as thrombomodulin influencing thrombotic and atherosclerotic pathways. Understanding these interactions helps researchers develop potential therapeutic approaches for related conditions.