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Background:
Serine/threonine phosphorylation is a major reversible post-translational modification in eukaryotes. Kinases catalyze the attachment of phosphate groups to the hydroxyl groups of serine and threonine residues, while phosphatases remove them dynamically. This modification changes protein charge, conformation and molecular interactions, serving as a vital molecular switch. It governs diverse cellular processes including signal transduction, cell cycle, proliferation, differentiation, metabolism and immune response. Aberrant phosphorylation is closely linked to inflammation, cancer and other disorders.





