Phosphorylation is a ubiquitous cellular regulatory mechanism that mediates signal transduction pathways, which carry signals from the cell surface to the nucleus or cytoplasm, by altering the activity, subcellular localization, association or binding properties of a protein or lipid. Phosphorylation is a reversible, covalent modification of a molecule whereby a phosphate group is added or removed from the molecule. The altered activity of the molecule that is seen as a result of these modifications is essential for regulating critical cellular functions such as cell cycle, metabolism, differentiation, proliferation and apoptosis.
Families of specialized molecules catalyze the addition (kinases) and removal (phosphatases) of phosphate groups from proteins. Protein kinases, acting specifically on serine/threonine or tyrosine residues, can act as on/off switches for protein functions. Aberrant regulation and/or dysfunction of kinases has been shown to be connected to many diseases, including cancer and other proliferative diseases, inflammatory diseases, metabolic disorders and neurodegenerative diseases. As such, kinases are very desirable drug targets with tyrosine kinases representing the most prominent and druggable group. The translation of research to the clinic has yielded therapeutic candidates such as tyrosine kinase inhibitors (TKI), many of which have been investigated for treatment of various cancer and inflammation. We understand in translational research it is essential to ensure your target is the right target. We offer a broad range of kinase inhibitors, phosphatase inhibitors, and other bioactive small molecules for target identification and validation in kinase phosphatase biology research; a selection of these research tools is shown below.