The Phospho-Smad2(S255) antibody is a specialized tool used to detect Smad2 protein phosphorylated at serine residue 255. a key post-translational modification in transforming growth factor-beta (TGF-β) signaling. Smad2. a receptor-regulated SMAD (R-SMAD), acts as a critical mediator of TGF-β superfamily pathways, which regulate diverse cellular processes, including proliferation, differentiation, apoptosis, and immune responses. Upon TGF-β receptor activation, Smad2 is phosphorylated at specific C-terminal serine residues (e.g., S465/S467) by type I receptors, enabling its association with Smad4 and translocation to the nucleus to modulate gene expression.
Phosphorylation at S255. located in the linker region of Smad2. is less characterized but may play a regulatory role in signaling dynamics. Unlike C-terminal phosphorylation, S255 modification is thought to involve non-canonical kinases (e.g., CDK, MAPK) and could influence Smad2 stability, subcellular localization, or interactions with co-regulators. This site-specific antibody allows researchers to investigate context-dependent Smad2 regulation, particularly in crosstalk between TGF-β and other signaling pathways. It is widely used in techniques like Western blotting, immunofluorescence, and immunohistochemistry to study TGF-β pathway activity in diseases such as cancer, fibrosis, and autoimmune disorders. Validation of its specificity is essential, as phosphorylation patterns may vary across cell types and experimental conditions.