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219399 Cathepsin D Substrate I - Calbiochem

219399
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Panoramica

Replacement Information

Products

Numero di catalogoConfezionamento Qtà/conf
219399-10MG Fiala di plastica 10 mg
Description
OverviewUseful as a substrate for the determination of cathepsin D activity. Suitable for either colorimetric or fluorometric assay. Cathepsin D hydrolyzes the Phe-Phe bond. Requires dipeptidyl aminopeptidase II to free 4-methoxy-β-naphthylamine (4MeOβNA).
Catalogue Number219399
Brand Family Calbiochem®
SynonymsBz-RGFFP-4-MeOβNA, HCl
References
ReferencesTakahashi, T., and Tang, J. 1981. Methods Enzymol. 80, 565.
Smith, R.E., and Van Frank, R.M. 1975. in Lysosomes in Biology and Pathology 4 (Dingle, J.T., and Dean, R.T., eds.) p. 193, American Elsevier, Holland.
Product Information
ATP CompetitiveN
FormWhite lyophilized solid
Hill FormulaC₄₉H₅₅N₉O₇ · HCl
Chemical formulaC₄₉H₅₅N₉O₇ · HCl
ReversibleN
Quality LevelMQ100
Applications
Biological Information
Primary TargetSubstrate for the determination of cathepsin D activity
Purity≥95% by HPLC
Physicochemical Information
Cell permeableN
Emission max.
Excitation max.
Peptide SequenceBz-Arg-Gly-Phe-Phe-Pro-4MeOβNA, HCl
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
Protect from Moisture Protect from moisture
Do not freeze Ok to freeze
Special InstructionsFollowing reconstitution, aliquot and freeze (-20°C). Stock solutions are stable for up to 4 months at -20°C.
Packaging Information
Transport Information
Supplemental Information
Specifications

Documentation

Cathepsin D Substrate I - Calbiochem MSDS

Titolo

Scheda di sicurezza (MSDS) 

Cathepsin D Substrate I - Calbiochem Certificati d'Analisi

TitoloNumero di lotto
219399

Riferimenti bibliografici

Panoramica delle referenze
Takahashi, T., and Tang, J. 1981. Methods Enzymol. 80, 565.
Smith, R.E., and Van Frank, R.M. 1975. in Lysosomes in Biology and Pathology 4 (Dingle, J.T., and Dean, R.T., eds.) p. 193, American Elsevier, Holland.

Brochure

Titolo
Cathepsins and Related Products Technical Bulletin
Scheda tecnica

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.

Revision05-June-2008 RFH
SynonymsBz-RGFFP-4-MeOβNA, HCl
DescriptionA useful substrate for colorimetric or fluorometric assay of cathepsin D activity. Cathepsin D hydrolyzes the Phe-Phe bond. Dipeptidyl aminopeptidase II is required to free the 4-methoxy-β-naphthylamine (4MβNA). Excitation max: ~345 nm; emission max: ~425 nm.
FormWhite lyophilized solid
Recommended reaction conditions
1. Incubate the substrate, Bz-Arg-Gly-Phe-Phe-Pro-4MβNA (final concentration 350 µM) with cathepsin D in 500 µl of reaction buffer (20 mM glycine-HCl, pH 3.0) at 37°C to allow digestion of the substrate to Bz-Arg-Gly-Phe-OH and Phe-Pro-4MβNA. 2. Stop the reaction by adding 50 µl of 1% KOH and then add 850 µL of reaction buffer 2 (100 mM Tris-HCl, pH 7.8). 3. Add 1 mU dipeptidylpeptidase IV in 100 µl of reaction buffer 2 and incubate for >1 h at 37°C to completely hydrolyze the Phe-Pro-4MβNA to Phe-Pro-OH and 4MβNA. 4. Monitor the release of 4MβNA at 345 nm (excitation) and 425 nm (emission).
Chemical formulaC₄₉H₅₅N₉O₇ · HCl
Peptide SequenceBz-Arg-Gly-Phe-Phe-Pro-4MeOβNA, HCl
Purity≥95% by HPLC
SolubilityDMSO (5 mg/ml)
Storage -20°C
Protect from moisture
Protect from light
Do Not Freeze Ok to freeze
Special InstructionsFollowing reconstitution, aliquot and freeze (-20°C). Stock solutions are stable for up to 4 months at -20°C.
Toxicity Standard Handling
ReferencesTakahashi, T., and Tang, J. 1981. Methods Enzymol. 80, 565.
Smith, R.E., and Van Frank, R.M. 1975. in Lysosomes in Biology and Pathology 4 (Dingle, J.T., and Dean, R.T., eds.) p. 193, American Elsevier, Holland.