Life Science

azido-FTY720 is a highly photoreactive analog of FTY720 that can be used to identify receptor binding sites for this ligand.

azido-FTY720 is a highly photoreactive analog of FTY720 that can be used to identify receptor binding sites for this ligand.

azido-FTY720 is a highly photoreactive analog of FTY720 that can be used to identify receptor binding sites for this ligand.

A macrolide antibiotic with high stability at acidic pH, long half-life, and favorable effectiveness against a range of organisms.

A macrolide antibiotic with high stability at acidic pH, long half-life, and favorable effectiveness against a range of organisms.

A macrolide antibiotic with high stability at acidic pH, long half-life, and favorable effectiveness against a range of organisms.

A macrolide antibiotic with high stability at acidic pH, long half-life, and favorable effectiveness against a range of organisms.

A semi-synthetic with broad spectrum antibacterial properties used as part of antibiotic cocktails known as PANTA (with polymyxin B, amphotericin B, nalidixic acid, and trimethoprim) and PANTAV (PANTA with vancomycin).

A semi-synthetic with broad spectrum antibacterial properties used as part of antibiotic cocktails known as PANTA (with polymyxin B, amphotericin B, nalidixic acid, and trimethoprim) and PANTAV (PANTA with vancomycin).

A semi-synthetic with broad spectrum antibacterial properties used as part of antibiotic cocktails known as PANTA (with polymyxin B, amphotericin B, nalidixic acid, and trimethoprim) and PANTAV (PANTA with vancomycin).

A small molecule that at 1-25 &microM improves ER protein-folding ability, stimulates the expression of multiple chaperone proteins, and induces phosphorylation of eIF2&alpha to reduce protein synthesis exerts antidiabetic activity in both ob/ob

A small molecule that at 1-25 &microM improves ER protein-folding ability, stimulates the expression of multiple chaperone proteins, and induces phosphorylation of eIF2&alpha to reduce protein synthesis exerts antidiabetic activity in both ob/ob