Phosphatase Inhibitor Cocktails
Protein phosphorylation is the most common and important form of reversible protein posttranslational modification (PTM), with up to 30% of all proteins being phosphorylated at any given time. Protein kinases (PKs) are the effectors of phosphorylation and catalyze the transfer of a γ-phosphate group from ATP to specific amino acids on proteins. Proteins are phosphorylated predominantly on Ser, Thr and Tyr residues, which account for 86, 12 and 2% respectively of the phosphoproteome, at least in mammals. In contrast, protein phosphatases (PPs) are the primary effectors of dephosphorylation, and are responsible for restoring the protein to its original dephosphorylated state. Phosphatases can be classified as non-specific phosphatases (e.g. acid or alkaline phosphatases), serine/threonine-specific, tyrosine-specific and dual-specific phosphatases (Ser/Thr & Tyr). A wide range of biological processes are controlled by phosphorylation and dephosphorylation of proteins. In order to understand the accurate phosphorylated status of a protein, it is important to preserve the phosphorylation state of the proteins during the extraction of phosphoproteins from tissue and cell sample lysates. BioVision introduces four different EZBlock™ Phosphatase Inhibitor Cocktails and two new Universal Protease and Phosphatase inhibitor cocktails, which would provide protection against both proteases and phosphatases during protein extraction and purification.
