Life Science

A potent, cell-permeable, and selective inhibitor of &gamma-secretase, blocking the cleavage of both APP and Notch CTFs with IC₅₀ values of ~0.3 nM induces neuronal differentiation, impairs ovarian folliculogenesis, and suppresses

A potent, cell-permeable, and selective inhibitor of &gamma-secretase, blocking the cleavage of both APP and Notch CTFs with IC₅₀ values of ~0.3 nM induces neuronal differentiation, impairs ovarian folliculogenesis, and suppresses

Blocks lysosomal acidification through selective inhibition of the V-type ATPase (EC50 = 2.1-2.

Blocks lysosomal acidification through selective inhibition of the V-type ATPase (EC50 = 2.1-2.

Blocks lysosomal acidification through selective inhibition of the V-type ATPase (EC50 = 2.1-2.

Selective inhibitor of vacuolar type H+-ATPases (IC₅₀ = 5 nM) blocks the acidification of vacuolar organelles as well as early to late endosomal transport interferes with bone resorption, maturation of CD8 T lymphocytes, and the

Selective inhibitor of vacuolar type H+-ATPases (IC₅₀ = 5 nM) blocks the acidification of vacuolar organelles as well as early to late endosomal transport interferes with bone resorption, maturation of CD8 T lymphocytes, and the

Concanavalin A (Con A) Agarose consists of Con A coupled to 4% agarose by the cyanogen bromide method. Con A is a tetrameric metalloprotein lectin isolated from Canavalia ensiformis (jack bean).

Concanavalin A (Con A) Agarose consists of Con A coupled to 4% agarose by the cyanogen bromide method. Con A is a tetrameric metalloprotein lectin isolated from Canavalia ensiformis (jack bean).

Concanavalin A (Con A) Agarose consists of Con A coupled to 4% agarose by the cyanogen bromide method. Con A is a tetrameric metalloprotein lectin isolated from Canavalia ensiformis (jack bean).

Concanavalin A (Con A) Agarose consists of Con A coupled to 4% agarose by the cyanogen bromide method. Con A is a tetrameric metalloprotein lectin isolated from Canavalia ensiformis (jack bean).

A plant lectin that selectively cross-links cell-surface glycoproteins and affects the initiation of cell agglutination, mitogenesis, and apoptosis widely used in affinity chromatography purifications of various glycoproteins and cellular