Phosphorylation of signal transduction molecule Smad3, can be an important information for understanding of various biological functions of transforming growth factor (TGF)-β. TGF-β type I receptor and mitogen activated protein kinase (MAPK) phosphorylate Smad3 at the C-terminal and at linker (middle) regions respectively. Mitogenic signaling induced by HGF, EGF and inflammatory cytokines is mediated by Smad3 phosphoisoforms that phosphorylate serines located in linker region. This monoclonal antibody against for Smad3L (S213) recognizes specifically the part containing phosphorylated serine 213 (ser213) located in linker region of Smad3 .
It can be used for western blotting, immunoprecipitation and immunohistochemistry. It is applicable for enzyme biochemical analysis of Smad3 signaling and makes it possible to visualize the intermolecular reaction of phosphorylated Smad3 signaling in human tissues and monitor them in real-time. Thus, analysis of Smad3 signaling with this antibody is expected to be widely applied in cancer and fibrosis research, and to contribute to understanding the wide variety of life phenomena mediated by phosphoisoforms of Smad3.

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