Protein Phosphatases

By reversing the phosphorylation of key regulatory proteins mediated by protein kinases, phosphatases serve as an important complement to kinases and attenuate activated signal transduction pathways. Important classes of phosphatases include both receptor and nonreceptor protein tyrosine phosphatases (PTPs), dual specificity phosphatases (DUSPs), cell cycle regulatory phosphatases, the 4 major serine/threonine protein phosphatase gene families (PP1, PP2A, PP2B, and PP2C), and other increasingly important gene families (PP4, PP5, PP6, and PP7). PTPs regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. DUSPs can dephosphorylate serine and threonine as well as tyrosine residues, primarily targeting MAP kinases. PP1 family members regulate of a variety of cellular processes, such as cell division, glycogen metabolism, muscle contractility, protein synthesis, and HIV-1 viral transcription. PP2A family members negatively regulate cell growth and division. Calcineurin (PP2B), the calmodulin-dependent protein phosphatase, acts as a calcium ion-dependent regulator of phosphorylation and plays a role in a wide range of biological activities. PP2C family members counteract cell stress response pathways. Alterations in phosphatase activity, including changes in gene expression, have been implicated in central nervous system and metabolic disorders, infectious diseases, and cancer.

QIAGEN provides a broad range of assay technologies for protein phosphatase research that enables analysis of gene expression and regulation, epigenetic modification, genotyping, and signal transduction pathway activation. Solutions optimized for protein phosphatase studies include PCR array, miRNA, siRNA, mutation analysis, pathway reporter, chromatin IP, DNA methylation, and protein expression products.