Tyrosine Kinases

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

The protein tyrosine kinase superfamily includes roughly 60 receptor tyrosine kinases (RTKs) and about 30 intracellular tyrosine kinases. RTKs (such as EGF receptors, FGF receptors, FLT3, KIT, MET, PDGF receptors, and VEGF receptors) include an extracellular domain, a transmembrane domain, and a catalytic intracellular domain. Upon activation, RTKs dimerize and autophosphorylate their intracellular domains, initiating downstream signaling that often includes non-receptor tyrosine kinases. Non-receptor tyrosine kinases include a catalytic domain and a regulatory domain, which vary for each family. For example, the SRC-family kinase regulatory domain requires autophosphorylation for kinase domain activation, while most other intracellular tyrosine kinase families use different regulatory mechanisms. Tyrosine kinases and their downstream signaling pathways are involved in many basic biological processes, such as growth, proliferation, and differentiation. These processes are commonly dysregulated during oncogenesis, often due to frequent mutations of key tyrosine kinases or regulators. These oncogenic processes make the tyrosine kinase superfamily members attractive drug targets, and there are several chemotherapeutics targeting tyrosine kinases already on the market (e.g.,  imatinib mesylate). Studying tyrosine kinase expression and regulation in an experimental model system can yield new insights into their role in normal biological and pathophysiological processes.