Life Science

An inhibitor of FAS-II, blocking fatty acid synthesis in S. aureus and E.

An inhibitor of FAS-II, blocking fatty acid synthesis in S. aureus and E.

A natural demethoxy derivative of curcumin activates macrophage phagocytosis and, with 1&alpha,25-dihydroxyvitamin D3, stimulates amyloid-&beta clearance by macrophages (optimal stimulation at 100 nM BDMC) suppresses proliferation in cancer

A natural demethoxy derivative of curcumin activates macrophage phagocytosis and, with 1&alpha,25-dihydroxyvitamin D3, stimulates amyloid-&beta clearance by macrophages (optimal stimulation at 100 nM BDMC) suppresses proliferation in cancer

A natural demethoxy derivative of curcumin activates macrophage phagocytosis and, with 1&alpha,25-dihydroxyvitamin D3, stimulates amyloid-&beta clearance by macrophages (optimal stimulation at 100 nM BDMC) suppresses proliferation in cancer

A natural demethoxy derivative of curcumin activates macrophage phagocytosis and, with 1&alpha,25-dihydroxyvitamin D3, stimulates amyloid-&beta clearance by macrophages (optimal stimulation at 100 nM BDMC) suppresses proliferation in cancer

A highly selective, cell-permeable, and reversible PKC inhibitor (Ki = 14 nM) acts as a competitive inhibitor for the ATP binding site of PKC and shows high selectivity for PKC&alpha-, &beta1-, &beta2-, &gamma-, &delta-, and

A highly selective, cell-permeable, and reversible PKC inhibitor (Ki = 14 nM) acts as a competitive inhibitor for the ATP binding site of PKC and shows high selectivity for PKC&alpha-, &beta1-, &beta2-, &gamma-, &delta-, and

A highly selective, cell-permeable, and reversible PKC inhibitor (Ki = 14 nM) acts as a competitive inhibitor for the ATP binding site of PKC and shows high selectivity for PKC&alpha-, &beta1-, &beta2-, &gamma-, &delta-, and

A highly selective, cell-permeable, and reversible PKC inhibitor (Ki = 14 nM) acts as a competitive inhibitor for the ATP binding site of PKC and shows high selectivity for PKC&alpha-, &beta1-, &beta2-, &gamma-, &delta-, and

A general inhibitor of all PKC subtypes with structural similarity to the nonspecific PKC inhibitor staurosporine inhibits PDK1 (IC50 = 14 &muM) and PKA (IC50 = 2.94 &muM).

A general inhibitor of all PKC subtypes with structural similarity to the nonspecific PKC inhibitor staurosporine inhibits PDK1 (IC50 = 14 &muM) and PKA (IC50 = 2.94 &muM).