A partial length recombinant FNBP1 protein (amino acids 40-260) was used as the immunogen for this antibody.
Alternative Names:
FBP17,iKIAA0554
FNBP1 (formin binding protein 1) also known as FBP17,is an F-BAR domain protein that belongs to the formin-binding-protein family. It has a powerful self-polymerizing ability that promotes actin nucleation on membranes. F-BAR domain of FBP17 is capable of self-polymerizing into filaments, which adhere to the flat bilayer sheets and form a spiral protein coat around the tubulated membrane that they then induce. The gene for FNB1 maps to chromosome 9q34 and consists of a C-terminal Src homology 3 domain and an N-terminal region that is homologous to the cell division cycle protein, cdc15, a regulator of the actin cytoskeleton. The assembly of FBP17 is dependent on WASP, and its dissociation by WASP inhibition strongly induces a self-organization of PSTPIP2, another F-BAR protein, at podosomes. Podosomes/invadopodia are highly dynamic adhesive actin-based structures with enrichment of matrix metalloproteases (MMPs) activity formed at the ventral surface of the cell body, which are seen in macrophages, osteoclasts, dendritic cells and some cancer cells.
