α-Secretase Substrate II, Fluorogenic

An internally quenched fluorogenic peptide substrate containing the α-secretase cleavage site of β-Amyloid Precursor Protein (APP). Shown to be a substrate for yapsin 2, a glycosyl-phosphatidylinositol-linked yeast aspartyl protease (V_max/K_m = 0.031 min^-1). The cleavage is shown to occur at the Lys-Leu bond.

An internally quenched fluorogenic peptide substrate that contains the α-secretase cleavage site of β-amyloid precursor protein (APP). Shown to be an effective substrate for yapsin-2, a glycosyl-phosphatidylinositol-linked aspartyl protease found in yeast (V_max/K_m = 0.031 min^-1). The cleavage has been shown to occur at the Lys-Leu bond. Excitation max: ~340 nm; emission max: ~490 nm.

Cell permeable: no

Primary Target
Substrate containing the α-secretase cleavage site of β-Amyloid Precursor Protein (APP)

Product does not compete with ATP.

Reversible: no

Packaged under inert gas

Toxicity: Standard Handling (A)

Ac-Arg-Glu(EDANS)-Val-His-His-Gln-Lys-Leu-Val-Phe-Lys(DABCYL)-Arg-OH

Komano, H., et al. 1999. J. Biol. Chem. 274, 24431.
Komano, H., et al. 1998. J. Biol. Chem. 273, 31648.

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