Anti-Pleckstrin/PLEK Antibody Picoband® Fluoro647 Conjugated

Enables phosphatidylinositol-3,4-bisphosphate binding activity; protein homodimerization activity; and protein kinase C binding activity. Involved in several processes, including G protein-coupled receptor signaling pathway; actin cytoskeleton organization; and positive regulation of supramolecular fiber organization. Located in cytoplasm and ruffle membrane.

Ubiquitin carboxyl-terminal hydrolase 21; Deubiquitinating enzyme 21; Ubiquitin thioesterase 21; Ubiquitin-specific-processing protease 21; USP21; USP23; PP1490

Cofactors, Vitamins/Minerals, Metabolism, Mitochondrial, Mitochondrial Markers, Mitochondrial Metabolism, Pathways and Processes, Signal Transduction, Vitamins/Minerals

Deubiquitinates histone H2A, a specific tag for epigenetic transcriptional repression, thereby acting as a coactivator. Deubiquitination of histone H2A releaves the repression of di- and trimethylation of histone H3 at 'Lys-4', resulting in regulation of transcriptional initiation. Regulates gene expression via histone H2A deubiquitination. Also capable of removing NEDD8 from NEDD8 conjugates but has no effect on Sentrin-1 conjugates. Deubiquitinates BAZ2A/TIP5 leading to its stabilization.

1. Cmarik, J. L., Hegamyer, G., Gerrard, B., Dean, M., Colburn, N. H. cDNA cloning and mapping of mouse pleckstrin (Plek), a gene upregulated in transformation-resistant cells. Genomics 66: 204-212, 2000. 2. Tyers, M., Haslam, R. J., Rachubinski, R. A., Harley, C. B. Molecular analysis of pleckstrin: the major protein kinase C substrate of platelets. J. Cell. Biochem. 40: 133-145, 1989. 3. Tyers, M., Rachubinski, R. A., Stewart, M. I., Varrichio, A. M., Shorr, R. G. L., Haslam, R. J., Harley, C. B. Molecular cloning and expression of the major protein kinase C substrate of platelets. Nature 333: 470-473, 1988.