Molecular Biology Reagents

16-Oxocafestol is a synthetic derivative of cafestol.

16-Oxocafestol is a synthetic derivative of cafestol.

17(R)-HDoHE is a primary mono-oxygenation product of docosahexaenoic acid, which is in human whole blood, human leukocytes, and murine brain. It serves as a precursor to 17(S)-resolvins and has intrinsic biological activity, such as the inhibition

17(R)-HDoHE is a primary mono-oxygenation product of docosahexaenoic acid, which is in human whole blood, human leukocytes, and murine brain. It serves as a precursor to 17(S)-resolvins and has intrinsic biological activity, such as the inhibition

17(S)-HpDoHE is a mono-oxygenation product of docosahexaenoic acid in human leukocytes, human whole blood, human glial cells, and murine brain . 17(S)-HpDoHE is generally reduced to 17(S)-HDoHE, a compound that serves as a precursor to

17(S)-HpDoHE is a mono-oxygenation product of docosahexaenoic acid in human leukocytes, human whole blood, human glial cells, and murine brain . 17(S)-HpDoHE is generally reduced to 17(S)-HDoHE, a compound that serves as a precursor to

17-(3-Hydroxypropyl-¹³C3)-6β,7β:15β,16β-dimethyleneandrostane-3β,5β,17β-triol.

17-(Acetyloxy)-6-(hydroxymethyl)-pregna-4,6-diene-3,20-dione.

A less toxic, potent, synthetic derivative of the ansamycin benzoquinone antibiotic Geldanamycin Streptomyces hygroscopicus (Cat. No.

This ansamycin antibiotic exhibits high affinity binding toHeat Shock Protein 90 (Hsp90) and alters its function binding to the ATP binding pocket. Inteneded for laboratory use only.

This ansamycin antibiotic exhibits high affinity binding to Heat Shock Protein 90 (Hsp90) and alters its function binding to the ATP binding pocket.

This ansamycin antibiotic exhibits high affinity binding to Heat Shock Protein 90 (Hsp90) and alters its function binding to the ATP binding pocket.