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MAP kinase-activated protein kinase 2 (MAPKAPK2) is an enzyme that in humans is encoded by the MAPKAPK2 gene. MAPKAP kinase-2 (MK2) is originally identified by its phosphorylation of glycogen synthase at serine-7 and the corresponding serine in a peptide (GS peptide-1) modelled after the N-terminus of glycogen synthase.

MAPKAP kinase-2 is a novel protein kinase activated by mitogen-activated protein kinase. This MAP kinase activated protein kinase, termed MAPKAP kinase-2, is distinguished from S6 kinase-II (MAPKAP kinase-1) by its response to inhibitors, lack of phosphorylation of S6 peptides and amino acid sequence.

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MK2-IN-1 is a potent, selecitve, non-ATP competitive MAPKAPK2(MK2) inhibitor with IC50 of 0.11 uM; shows excellent kinase selectivity against a broad panel of 150 protein kinases at 10 μM with only on exception of CK1γ3 >50 % inhibition; inhibits pro-inflammatory cytokine secretion from the human THP1 acute monocytic leukemia cell line, causing dose-dependent inhibition of LPS-stimulated TNFα and IL6 secretion; also dose dependently inhibits IL1β-stimulated MMP13 secretion from the SW1353 chondrosarcoma cell line and human primary chondrocyte cultures.

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