| CAS | 141223-71-4 |
| Sequence | Z-Val-Lys-Met-AMC |
| Sequence Single | Z-VKM-AMC |
| Molecular Formula | C34H45N5O7S |
| Molecular Weight | 667.83 |
| Technology | Synthetic |
| Storage | -20°C, avoid light, cool and dry place |
| Application | Alzheimer’s Disease |
| Description | Z-Val-Lys-Met-AMC is a substrate for Amyloid A4-generating enzymes and cathepsin B containing motif VKM corresponding to APP (669-671). Hook et al. used Z-Val-Lys-Met-AMC to detect β-secretase activity in isolated chromaffin vesicles. |
| References | 1. Amino acids and peptides. XXX. Synthesis of eglin c (41-49) and eglin c (60-63) and examination of their inhibitory activity towards human leukocyte elastase, cathepsin G, porcine pancreatic elastase and alpha-chymotrypsin. S.Tsuboi et al., Chem. Pharm. Bull., 39, 184 (1991) 2. Presence of angiotensin-converting enzyme in follicular fluids of porcine ovaries and its possible involvement in the intrafollicular breakdown of bradykinin. H.Matsui and T.Takahashi, Mol. Reprod. Dev., 62, 99 (2002) 3. Distribution of Alzheimer’s disease amyloid A4-generating enzymes in rat brain tissue. S.Ishiura et al., Neurosci. Lett., 115, 329 (1990) 4. Cysteine Cathepsins in the secretory vesicle produce active peptides: Cathepsin L generates peptide neurotransmitters and cathepsin B produces beta-amyloid of Alzheimer’s disease. V.Hook et al., Biochim. Biophys. Acta, 1824, 89 (2012) 5. Inhibition of cathepsin B reduces beta-amyloid production in regulated secretory vesicles of neuronal chromaffin cells: evidence for cathepsin B as a candidate beta-secretase of Alzheimer’s disease. V.Hook et al., Biol. Chem., 386, 931 (2005) 6. Beta-amyloid peptide in regulated secretory vesicles of chromaffin cells: evidence for multiple cysteine proteolytic activities in distinct pathways for beta-secretase activity in chromaffin vesicles. V.Y.H.Hook et al., J. Neurochem., 81, 237 (2002) 7. Inhibitors of cathepsin B improve memory and reduce beta-amyloid in transgenic Alzheimer disease mice expressing the wild-type, but not the Swedish mutant, beta-secretase site of the amyloid precursor protein. V.Y.H.Hook et al., J. Biol. Chem., 293, 7745 (2008) |