The steady state phosphorylation of any given substrate is governed by the opposing activities of kinases and phosphatases. Protein phosphorylation systems are composed of at least three components: (a) phosphoproteins (b) kinases and (c) phosphatases, that dephosphorylate the phosphoproteins, thereby restoring the particular protein phosphorylation system to its basal stage.
Kinases and Phosphatases Signaling
Protein kinases function in tandem with specific phosphatases, enzymes that remove the phosphate group from phosphorylated serine, threonine, and tyrosine residues by hydrolysis. Based on cellular localization, phosphatases can be classified as transmembrane, receptor-linked or non-transmembrane/cytoplasmic and are essential components of the regulation of cellular signaling.
Anti-Phosphotyrosine, 4G10® Platinum
Clone 4G10® was the first and is the best single monoclonal antibody for the detection tyrosine phosphorylation. 4G10® is well known for its sensitivity and its ability to detect multiple tyrosine phosphorylations on numerous substrates. It has been validated by thousands of scientific and medical researchers in virtually every application and tyrosine target over the past 2 decades. Learn More
Tyrosine phosphorylation often mediates receptor signaling events at the membrane by initiating protein-protein interactions in response to growth factors, hormones and cytokines.
Advance your signaling research with Millipore’s tools to detect tyrosine phosphorylation, based on the first and best monoclonal antibody for the detection of tyrosine phosphorylation, Clone 4G10®. It is the most highly cited (in 75 % of related scientific journal articles over the last three years) and validated phosphotyrosine antibody available. It has been validated by thousands of researchers in virtually every application and tyrosine target over the past 18 years.
Anti-Phosphoserine, clone 4A4 (mouse monoclonal IgG1
Phosphoserine is the major mechanism for the regulation of diverse cellular processes including cell division, protein synthesis, transcriptional regulation and neurotransmission. Routinely evaluated by Western Blot analysis on lysate from Calyculin A/Okadaic-treated human A431 carcinoma cells. Learn More
Approximately 400 of the 518 kinases in the human genome are serine/threonine specific protein kinases and approximately 40 serine/threonine specific protein phosphatases are encoded by the human genome. Given the involvement of these kinases in all aspects of cell signaling, it is not surprising to find that serine/threonine kinases are instrumental in many critical disorders including many cancers, diabetes, and Alzheimer’s disease. As a result, many drug discovery programs are specifically targeting serine/threonine kinases.