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ProteoGenix
Recombinant Proteins
Escherichia coli (E. coli)
Elisa, WB
Annexin A2 is a calcium-dependent phospholipid-binding protein that is involved in a variety of cellular processes, including membrane trafficking, cell signaling, and cell adhesion. It is also known as lipocortin II, p36, or calpactin I heavy chain, and is encoded by the ANXA2 gene. Annexin A2 is widely expressed in different tissues and cell types, and its dysregulation has been linked to various diseases, making it a potential drug target for therapeutic interventions.
Annexin A2 is a 36-kDa protein that consists of 339 amino acids. It is composed of four domains, including an N-terminal domain, a core domain, a linker domain, and a C-terminal domain. The N-terminal domain contains the calcium-binding sites, while the core domain is responsible for the phospholipid-binding activity. The linker domain connects the N-terminal and core domains, and the C-terminal domain is involved in protein-protein interactions.
The N-terminal domain of annexin A2 contains four repeats of a highly conserved 70-amino acid sequence, known as the annexin repeat motif. Each of these repeats contains a calcium-binding site, which is essential for the protein’s function. The core domain consists of five alpha-helices and a beta-sheet, which form a hydrophobic pocket for binding to phospholipids. The linker domain is flexible and allows for conformational changes in the protein. The C-terminal domain contains a binding site for the protein S100A10, which is involved in the regulation of annexin A2’s activity.
Annexin A2 is a multifunctional protein that plays a role in various cellular processes. Its main function is to bind to phospholipids in a calcium-dependent manner, which allows it to interact with membranes and regulate membrane dynamics. Annexin A2 also interacts with other proteins, such as actin, myosin, and S100A10, to participate in cell signaling and cytoskeletal organization.
One of the most well-studied functions of annexin A2 is its involvement in membrane trafficking. It has been shown to play a role in endocytosis, exocytosis, and transcytosis, which are essential processes for the transport of molecules within and between cells. Annexin A2 also participates in cell adhesion by binding to integrins and regulating their activity. This function is particularly important in processes such as cell migration and invasion.
Due to its involvement in various cellular processes, annexin A2 has been implicated in several diseases and has potential applications in drug development. For example, annexin A2 has been linked to cancer progression and metastasis, as it promotes cell migration and invasion. Therefore, targeting annexin A2 could potentially inhibit these processes and prevent cancer spread. Additionally, annexin A2 has been shown to play a role in viral infection, making it a potential target for antiviral therapies.
Annexin A2 has also been investigated as a biomarker for various diseases. Its expression has been found to be altered in conditions such as Alzheimer’s disease, cardiovascular diseases, and autoimmune disorders. Therefore, measuring annexin A2 levels could potentially serve as a diagnostic or prognostic tool for these diseases.
Furthermore, annexin A2 has been explored as a drug target for therapeutic interventions. Several studies have shown that inhibiting annexin A2’s activity can have anti-inflammatory and anti-thrombotic effects, making it a potential target for treating inflammatory and cardiovascular diseases.
In conclusion, annexin A2 is a calcium-dependent phospholipid-binding protein that plays a crucial role in various cellular processes. Its structure and activity make it a versatile protein with potential applications in drug development and disease diagnosis.
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