Anti-PCBP1 Antibody Picoband® Fluoro488 Conjugated

Poly (rC) -binding protein 1 is a protein that in humans is encoded by the PCBP1 gene. This intronless gene is thought to have been generated by retrotransposition of a fully processed PCBP-2 mRNA. This gene and PCBP-2 have paralogues (PCBP3 and PCBP4) which are thought to have arisen as a result of duplication events of entire genes. The protein encoded by this gene appears to be multifunctional. It along with PCBP-2 and hnRNPK corresponds to the major cellular poly (rC) -binding protein. It contains three K-homologous (KH) domains which may be involved in RNA binding. This encoded protein together with PCBP-2 also functions as translational coactivators of poliovirus RNA via a sequence-specific interaction with stem-loop IV of the IRES and promote poliovirus RNA replication by binding to its 5'-terminal cloverleaf structure. It has also been implicated in translational control of the 15-lipoxygenase mRNA, human Papillomavirus type 16 L2 mRNA, and hepatitis A virus RNA. The encoded protein is also suggested to play a part in formation of a sequence-specific alpha-globin mRNP complex which is associated with alpha-globin mRNA stability.

Atherosclerosis, Cadherins, Cancer, Cardiovascular, Cell Adhesion, Cell Adhesion Molecules, Cytoskeleton/ECM, Invasion/Microenvironment, Signal Transduction, Vascular Inflammation, Vasculature

Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. This cadherin may play an important role in endothelial cell biology through control of the cohesion and organization of the intercellular junctions. Acts in concert with KRIT1 to establish and maintain correct endothelial cell polarity and vascular lumen. These effects are mediated by recruitment and activation of the Par polarity complex and RAP1B. Required for activation of PRKCZ and for localization of phosphorylated PRKCZ, PARD3, TIAM1 and RAP1B to the cell junction.

1. Chkheidze, A. N., Liebhaber, S. A. A novel set of nuclear localization signals determine distributions of the alpha-CP RNA-binding proteins. Molec. Cell. Biol. 23: 8405-8415, 2003. 2. Hahm, K., Kim, G., Turck, C. W., Smale, S. T. Isolation of a murine gene encoding a nucleic acid-binding protein with homology to hnRNP K. Nucleic Acids Res. 21: 3894 only, 1993. 3. Kosturko, L. D., Maggipinto, M. J., Korza, G., Lee, J. W., Carson, J. H., Barbarese, E. Heterogeneous nuclear ribonucleoprotein (hnRNP) E1 binds to hnRNP A2 and inhibits translation of A2 response element mRNAs. Molec. Biol. Cell 17: 3521-3533, 2006