|Detection of Human/Mouse/Rat Annexin A7 by Western Blot. Western blot shows lysates of Jurkat human acute T cell leukemia cell line, HeLa human cervical epithelial carcinoma cell line, C2C12 mouse myoblast cell line, and L6 rat myoblast cell line. PVDF membrane was probed with 1 µg/mL of Human/Mouse/Rat Annexin A7 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF3926) followed by HRP-conjugated Anti-Goat IgG Secondary Antibody (Catalog # HAF017). A specific band was detected for Annexin A7 at approximately 50 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 2.|
Annexin A7 (ANXA7), also known as Annexin VII and Synexin (SNX), is a 50.3 kDa member of the Annexin protein family. The Annexins are a family of Calcium‑dependent phospholipid-binding proteins that are preferentially located on the cytosolic face of the plasma membrane. The Annexin’s have a molecular weight of approximately 35‑40 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 (aa) 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 A7 was identified as a calcium-dependent membrane-binding protein that not only fuses membranes but also acts as a voltage-dependent calcium channel. Identification of alternate mRNA splicing indicates two Annexin A7 isoforms differing in the N-terminal domain. Human Annexin A7 shares 92% identity with mouse and rat Annexin A7.