171601 Sigma-AldrichAmyloid Precursor Protein β-Secretase Inhibitor - Calbiochem
The Amyloid Precursor Protein β-Secretase Inhibitor controls the biological activity of Amyloid Precursor Protein β-Secretase. This small molecule/inhibitor is primarily used for Neuroscience applications.
More>> The Amyloid Precursor Protein β-Secretase Inhibitor controls the biological activity of Amyloid Precursor Protein β-Secretase. This small molecule/inhibitor is primarily used for Neuroscience applications. Less<<Synonyms: KTEETSEVN(stat)VAEF
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Overview
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Key Spec Table
| Empirical Formula |
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| C₇₃H₁₁₈N₁₆O₂₇ |
Pricing & Availability
| Catalogue Number | Availability | Packaging | Qty/Pack | Price | Quantity | |
|---|---|---|---|---|---|---|
| 171601-500UGCN |
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Plastic ampoule | 500 μg |
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| Description | |
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| Overview | A potent inhibitor of the amyloid precursor protein (APP) β-secretase (IC50 = 30 nM). |
| Catalogue Number | 171601 |
| Brand Family | Calbiochem® |
| Synonyms | KTEETSEVN(stat)VAEF |
| References | |
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| References | Sinha, S., et al. 1999. Nature 402, 537. |
| Product Information | |
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| ATP Competitive | N |
| Form | Lyophilized |
| Formulation | Supplied as a trifluoroacetate salt. |
| Hill Formula | C₇₃H₁₁₈N₁₆O₂₇ |
| Chemical formula | C₇₃H₁₁₈N₁₆O₂₇ |
| Hygroscopic | Hygroscopic |
| Reversible | N |
| Quality Level | MQ100 |
| Applications |
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| Biological Information | |
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| Primary Target | APP |
| Primary Target IC<sub>50</sub> | 30 nM against amyloid precursor protein (APP) β-secretase |
| Purity | ≥98% by HPLC |
| Physicochemical Information | |
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| Cell permeable | N |
| Peptide Sequence | H-Lys-Thr-Glu-Glu-Ile-Ser-Glu-Val-Asn-Stat-Val-Ala-Glu-Phe-OH [Stat = (3S,4S)-Statine] |
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| Specifications |
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| Global Trade Item Number | |
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| Catalogue Number | GTIN |
| 171601-500UGCN | 04055977207293 |
Documentation
Amyloid Precursor Protein β-Secretase Inhibitor - Calbiochem SDS
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Amyloid Precursor Protein β-Secretase Inhibitor - Calbiochem Certificates of Analysis
| Title | Lot Number |
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| 171601 |
References
| Reference overview |
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| Sinha, S., et al. 1999. Nature 402, 537. |



