Anti-SNX9 Antibody, clone 6C6 clone 6C6, from rat

Sorting nexin-9 (UniProt: Q9Y5X1; also known as SH3 and PX domain-containing protein 1, Protein SDP1, SH3 and PX domain-containing protein 3A, SNX9) is encoded by the SNX9 (also known as SH3PX1, SH3PXD3A) gene (Gene ID: 51429) in human. SNX9 is widely expressed, with highest levels reported in heart and placenta, and lowest levels in thymus and peripheral blood leukocytes. SNX9 is localized at sites of endocytosis at the cell membrane and is detected on newly formed macropinosomes. It is transiently recruited to clathrin-coated pits at a late stage of clathrin-coated vesicle formation. SNX9 can exist as a homo dimer or homo oligomer and can also heterodimerize with SNX18. It displays four phosphatidylinositol 4,5-bisphosphate binding sites. It has a SH3 domain (aa 1-63), a SNX-type Phox homology (PX) domain (aa 250-361), and a BAR domain (aa 292-595). The PX domain mediates its interaction with membranes enriched in phosphatidylinositol phosphate. SNX9 can stimulate the GTPase activity of dynamin and both its SH3 domain and more C-terminal domains are required to efficiently stimulate this GTPase activity. Although it has high affinity for phosphatidylinositol 4,5-bisphosphate, but can also bind to membranes enriched in other phosphatidylinositol phosphates. SNX9 can be phosphorylated on tyrosine residues by TNK2 and phosphorylation promotes its activity in the degradation of EGFR. SNX9 is shown to be involved in endocytosis and intracellular vesicle trafficking, both during interphase and at the end of mitosis. It is required for efficient progress through mitosis and cytokinesis and also for normal formation of the cleavage furrow at the end of mitosis. (Ref.: Schobel, S., et al. (2008). J. Biol. Chem.283(21); 14257-14268).