Phosphorylation events are commonly probed by phosphorylation-specific antibodies. With years of in-depth research in phosphorylation binding domains and application of High-Affi™ technology, Creative Biolabs can produce high-affinity antibodies that recognize this most widely studied post-translational modification, phosphorylation.
Phosphorylation is a ubiquitous and essential post-translational modification (PTM) by covalent addition of a phosphate (PO43−) group to a protein or other organic molecule. Protein phosphorylation is mediated by kinases and phosphatases. This reversible phosphorylation and dephosphorylation action affects an estimated one-third of all proteins and involves many critical events in cellular response, such as cellular localization, protein degradation, protein conformational change, signal transduction, enzymatic activity regulation, and protein-protein interaction. Abnormal phosphorylation can cause a range of diseases, such as neurodegenerative diseases, cancer, diabetes, cardiovascular diseases, and autoimmune diseases. On a given protein, phosphorylation usually occurs on many distinct sites and respective amino acids catalyzed by kinds of kinases. In eukaryotic proteins, it occurs on serine, threonine, tyrosine or histidine residues. While in prokaryotic proteins, it occurs on serine, threonine, tyrosine, histidine, arginine or lysine residues. Serine is the most common phosphorylation site, followed by threonine. Particularly, tyrosine phosphorylation is relatively rare but is a key step at the origin of protein phosphorylation signaling pathways in most parts of the eukaryotes.
Fig. 1 Strategy for generating phospho-specific antibodies.
Creative Biolabs offers phospho-pan/phospho-site specific antibodies against phosphorylated amino acids listed below:
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