Anti-PBP/PEBP1 Antibody Picoband® Fluoro594 Conjugated

PEBP1 (Phosphatidylethanolamine-binding protein 1), also called PBP, RKIP, inhibits the phosphorylation and activation of MEK by RAF1. PEBP1 is identical to the phosphatidylethanolamine-binding protein (PBP) with a relative molecular mass of 23 kD. The PEBP1 gene is mapped on 12q24.23. PEBP1 coimmunoprecipitates with RAF1 and MEK from cell lysates and colocalizes with RAF1 when examined by confocal microscopy. PEBP1 overexpression interferes with the activation of MEK and ERK, induction of AP1-dependent reporter genes, and transformation elicited by an oncogenically activated RAF1 kinase. PEBP1 expression was rapidly upregulated during induction of chemotherapy-triggered apoptosis in human prostate and breast cancer cell lines, and maximal RKIP expression correlated perfectly with the onset of apoptosis by Chatterjee et al (2004) . RKIP depletion 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.

Phosphatidylethanolamine-binding protein 1; PEBP-1; HCNPpp; Neuropolypeptide h3; Prostatic-binding protein; Raf kinase inhibitor protein; RKIP; Hippocampal cholinergic neurostimulating peptide; HCNP; PEBP1; PBP; PEBP

A synthetic peptide corresponding to a sequence at the C-terminus of human PBP, which shares 87.5% and 80% amino acid (aa) sequence identity with mouse and rat PBP, respectively.

Epigenetics and Nuclear Signaling, Cancer, Cell Biology, Oncoproteins/Suppressors, Tumor Suppressors, Cell Cycle, Neuroscience, Cell Division, Kinases/Phosphatases, Spindle, Neurotransmitter, Neuropeptides

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 (By similarity) . 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.

1. Chatterjee, D., Bai, Y., Wang, Z., Beach, S., Mott, S., Roy, R., Braastad, C., Sun, Y., Mukhopadhyay, A., Aggarwal, B. B., Darnowski, J., Pantazis, P., Wyche, J., Fu, Z., Kitagwa, Y., Keller, E. T., Sedivy, J. M., Yeung, K. C. RKIP sensitizes prostate and breast cancer cells to drug-induced apoptosis. J. Biol. Chem. 279: 17515-17523, 2004. 2. Hengst, U., Albrecht, H., Hess, D., Monard, D. The phosphatidylethanolamine-binding protein is the prototype of a novel family of serine protease inhibitors. J. Biol. Chem. 276: 535-540, 2001. 3. Yeung, K., Seitz, T., Li, S., Janosch, P., McFerran, B., Kaiser, C., Fee, F., Katsanakis, K. D., Rose, D. W., Mischak, H., Sedivy, J. M., Kolch, W. Suppression of Raf-1 kinase activity and MAP kinase signalling by RKIP. Nature 401: 173-177, 1999.