C12-iE-DAP

C12-iE-DAP (compound 16) (Lauroyl-γ-D-glutamyl-meso-diaminopimelic acid) induces NF-κB/AP-1-dependent SEAP signaling in HEK-Blue cells expressing human NOD1, with an EC₅₀ of 0.027 nM^[5].
C12-iE-DAP (0.01-10 μg/mL; 18 h) acts synergistically with Curdlan or TDB to enhance NF-κB/AP-1-dependent SEAP expression in the human monocytic cell line THP1-XBlue-CD14, with activity levels exceeding the additive effect of stimulation by each agonist alone^[2].
C12-iE-DAP (1-100 μg/mL; 24 h) acts synergistically with Curdlan or TDB to enhance the production of the IL-8 cytokine in the human monocyte cell line THP-1, with the production level exceeding the additive effect of stimulation by individual agonists^[2].
C12-iE-DAP (10^-9-10^-8 M; 1 h) upregulates CD11b in granulocytes from fresh human whole blood in a dose-dependent manner, with a stronger induction effect at 10^-8 M than at 10^-9 M; whereas compound 27 exhibits stronger activity at both of the above concentrations^[5].

C12-iE-DAP (5 μg/mL; 6 h) induces IL6 and IL8 mRNA expression in primary human brain pericytes and increases IL-8 release in cell culture supernatants^[1].
C12-iE-DAP (1 μg/mL; 6 h)-induced IL8 expression in human brain pericytes depends on the NOD1/RIPK2/p38/NF-κB signaling pathway. NOD1 knockdown reduces IL8 induction by >62%, while inhibitors of RIPK2, p38 or NF-κB can significantly suppress this response^[1].
C12-iE-DAP (1 μg/mL) acts synergistically with LPS (5 ng/mL) for 6 h to enhance IL8 mRNA expression in primary human brain pericytes, and the induced level is higher than that of LPS (100 ng/mL) alone^[1].

C12-iE-DAP (2,000 ng/mL) increases the adhesion of HT29 cells to fibronectin, collagen I and collagen IV by approximately 2-fold, 2-fold and 1.5-fold, respectively, enhances the migration of HT29 cells by approximately 2-fold, and simultaneously increases the adhesion of MC38 cells to both collagen I and fibronectin by approximately 1.5-fold^[4].
C12-iE-DAP (up to 2,000 ng/mL; up to 80 min) increases p38 phosphorylation in colorectal cancer cells by up to approximately 7-fold in a dose- and time-dependent manner, but does not induce corresponding changes in IκBα degradation^[4].