Anti-PBP

0.5mg/ml if reconstituted with 0.2ml sterile DI water. Phosphatidylethanolamine-binding protein inhibits the phosphorylation and activation of MEK by RAF1. PBP coimmunoprecipitates with RAF1 and MEK from cell lysates and colocalizes with RAF1 when examined by confocal microscopy. Overexpression interferes with the activation of MEK and ERK, induction of AP1-dependent reporter genes, and transformation elicited by an oncogenically activated RAF1 kinase. PBP expression was rapidly upregulated during induction of chemotherapy-triggered apoptosis in human prostate and breast cancer cell lines, and maximal expression correlated perfectly with the onset of apoptosis by Chatterjee et al(2004). Depletion of the protein decreased the mitotic index, the number of metaphase cells, traversal times from nuclear envelope breakdown to anaphase, and an override of mitotic checkpoints induced by spindle poisons. Protein function: Binds ATP, opioids and phosphatidylethanolamine. Has lower affinity for phosphatidylinositol and phosphatidylcholine. Serine protease inhibitor which inhibits thrombin, neuropsin and chymotrypsin but not trypsin, tissue type plasminogen activator and elastase. Inhibits the kinase activity of RAF1 by inhibiting its activation and by dissociating the RAF1/MEK complex and acting as a competitive inhibitor of MEK phosphorylation. [The UniProt Consortium]