epitope mapping within an internal region of HBXIP of human origin
recommended for detection of HBX-interacting protein of mouse, rat and human origin by WB, IF and ELISA; also reactive with additional species, including equine, canine, bovine, porcine and avian
HBXIP Background Information HBXIP (hepatitis B virus X-interacting protein), also known as HBV X-interacting protein or HBX-interacting protein, was originally identified by its ability to form a complex with the C-terminus of hepatitis B virus X (HBX) protein. HBXIP negatively regulates the activity of HBX and alters the replicative life cycle of the virus. HBXIP is an evolutionarily conserved protein. It contains a leucine zipper motif and two consensus phosphorylation sites. HBXIP also forms complexes with survivin (an overexpressed protein in most human cancers) and is necessary for allowing survivin to bind and inhibit the activation of pro-caspase-9, suggesting that HBXIP acts as an anti-apoptotic cofactor of survivin. In addition, HBXIP is involved in bipolar spindle formation and regulates centrosome dynamics and cytokinesis in cells, possibly through an interaction with Dynein light chain. The overexpression of HBXIP promotes proliferation in a variety of cells lines.
