The gene septin-2 (SEPT2) is mapped to human chromosome 2q37. It belongs to a conserved family of guanosine triphosphate binding proteins required for cell division. SEPT2 is present at the mid-body, the cleavage furrow and the central spindle of cells undergoing cytokinesis. In metaphase cells, SEPT2 is present within the microtubule spindle. SEPT2 is widely expressed with highest levels in brain tissues.
Synonyms: Anti-Protein NEDD5; Anti-Septin-2
Storage: -20C
Application: Anti-SEPT2 antibody produced in rabbit, a Prestige Antibody, is developed and validated by the Human Protein Atlas (HPA) project (www.proteinatlas.org). Each antibody is tested by immunohistochemistry against hundreds of normal and disease tissues. These images can be viewed on the Human Protein Atlas (HPA) site by clicking on the Image Gallery link. The antibodies are also tested using immunofluorescence and western blotting. To view these protocols and other useful information about Prestige Antibodies and the HPA, visit sigma.com/prestige.
Biochem Physiol Actions: At metaphase septin-2 (SEPT2) is crucial for maintaining CENP-E (Centromere-associated protein E) at kinetochores, required for chromosome congression. In anaphase, SEPT2 is needed for chromosome segregation and spindle elongation. SEPT2 forms a complex with SEPT7 and SEPT9. All three together are present along the length of the axoneme in the primary cilium of retinal pigmented epithelial cells. The complex is crucial for ciliogenesis. SEPT2 is recruited to the site of bacterial entry next to actin and is involved in bacterial invasion of Listeria and Shigella. SEPT2 is up-regulated in human hepatoma carcinoma cells (HCC). Casein kinase-2 mediated phosphorylation of SEPT2 is important for proliferation of HCC.
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