Millipore Sigma Vibrant Logo
Attention: We have moved. EMD Millipore products are no longer available for purchase on emdmillipore.com.Learn More

565767 α-Secretase Substrate II, Fluorogenic - Calbiochem

An internally quenched fluorogenic peptide substrate containing the α-secretase cleavage site of β-Amyloid Precursor Protein (APP).

MSDS (material safety data sheet) or SDS, CoA and CoQ, dossiers, brochures and other available documents.

Synonyms: Ac-RE(EDANS)-VHHQKLVF-K(DABCYL)-R-OH

View Products on Sigmaaldrich.com
565767
Purchase on Sigma-Aldrich

Overview

Replacement Information

Products

Catalog NumberPackaging Qty/Pack
565767-1MG Plastic ampoule 1 mg
Description
OverviewAn 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 (Vmax/Km = 0.031 min-1). The cleavage is shown to occur at the Lys-Leu bond.
Catalogue Number565767
Brand Family Calbiochem®
SynonymsAc-RE(EDANS)-VHHQKLVF-K(DABCYL)-R-OH
References
ReferencesKomano, H., et al. 1999. J. Biol. Chem. 274, 24431.
Komano, H., et al. 1998. J. Biol. Chem. 273, 31648.
Product Information
ATP CompetitiveN
FormRed solid
FormulationSupplied as a trifluoroacetate salt.
Hill FormulaC₁₀₀H₁₄₄N₃₀O₂₀S
Chemical formulaC₁₀₀H₁₄₄N₃₀O₂₀S
Hygroscopic Hygroscopic
ReversibleN
Quality LevelMQ100
Applications
Biological Information
Primary TargetSubstrate containing the α-secretase cleavage site of β-Amyloid Precursor Protein (APP)
Purity≥95% by HPLC
Physicochemical Information
Cell permeableN
Emission max.
Excitation max.
Peptide SequenceAc-Arg-Glu(EDANS)-Val-His-His-Gln-Lys-Leu-Val-Phe-Lys(DABCYL)-Arg-OH
Dimensions
Materials Information
Toxicological Information
Safety Information according to GHS
Safety Information
Product Usage Statements
Storage and Shipping Information
Ship Code Ambient Temperature Only
Toxicity Standard Handling
Storage -20°C
Protect from Light Protect from light
Hygroscopic Hygroscopic
Do not freeze Ok to freeze
Special InstructionsFollowing reconstitution, aliquot and freeze (-20°C). Stock solutions are stable for up to 3 months at -20°C.
Packaging Information
Packaged under inert gas Packaged under inert gas
Transport Information
Supplemental Information
Specifications
Global Trade Item Number
Catalog Number GTIN
565767-1MG 04055977267754

Documentation

α-Secretase Substrate II, Fluorogenic - Calbiochem SDS

Title

Safety Data Sheet (SDS) 

α-Secretase Substrate II, Fluorogenic - Calbiochem Certificates of Analysis

TitleLot Number
565767

References

Reference overview
Komano, H., et al. 1999. J. Biol. Chem. 274, 24431.
Komano, H., et al. 1998. J. Biol. Chem. 273, 31648.
Data Sheet

Note that this data sheet is not lot-specific and is representative of the current specifications for this product. Please consult the vial label and the certificate of analysis for information on specific lots. Also note that shipping conditions may differ from storage conditions.

Revision10-September-2008 RFH
SynonymsAc-RE(EDANS)-VHHQKLVF-K(DABCYL)-R-OH
DescriptionAn 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 (Vmax/Km = 0.031 min-1). The cleavage has been shown to occur at the Lys-Leu bond. Excitation max: ~340 nm; emission max: ~490 nm.
FormRed solid
FormulationSupplied as a trifluoroacetate salt.
Intert gas (Yes/No) Packaged under inert gas
Chemical formulaC₁₀₀H₁₄₄N₃₀O₂₀S
Peptide SequenceAc-Arg-Glu(EDANS)-Val-His-His-Gln-Lys-Leu-Val-Phe-Lys(DABCYL)-Arg-OH
Purity≥95% by HPLC
SolubilityDMSO (5 mg/ml)
Storage Protect from light
-20°C
Hygroscopic
Do Not Freeze Ok to freeze
Special InstructionsFollowing reconstitution, aliquot and freeze (-20°C). Stock solutions are stable for up to 3 months at -20°C.
Toxicity Standard Handling
ReferencesKomano, H., et al. 1999. J. Biol. Chem. 274, 24431.
Komano, H., et al. 1998. J. Biol. Chem. 273, 31648.