The protein encoded by this gene is a tumor suppressor and member of the serine/threonine kinase family. In response to cellular stress and proinflammatory cytokines, this kinase is activated through its phosphorylation by MAP kinases including MAPK1/ERK, MAPK14/p38-alpha, and MAPK11/p38-beta. The encoded protein is found in the nucleus but translocates to the cytoplasm upon phosphorylation and activation. This kinase phosphorylates heat shock protein HSP27 at its physiologically relevant sites. Two alternately spliced transcript variants of this gene encoding distinct isoforms have been reported.

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Western blotting analysis using MAPKAPK5 antibody . MAPKAPK5 expression in wild-type (WT) and MAPKAPK5 shRNA knockdown (KD) HeLa cells with 30 μg of total cell lysates. Hsp90 α serves as a loading control. The blot was incubated with MAPKAPK5 antibody and HRP-conjugated goat anti-mouse secondary antibody respectively. Image was developed using FeQ™ ECL Substrate Kit .

Western blotting analysis using MAPKAPK5 antibody . Total cell lysates (30 μg) from various cell lines were loaded and separated by SDS-PAGE. The blot was incubated with MAPKAPK5 antibody and HRP-conjugated goat anti-mouse secondary antibody respectively. Image was developed using FeQ™ ECL Substrate Kit .

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