Cathepsin D Substrate I-Calbiochem

C₄₉H₅₅N₉O₇ · xHCl

882.02 (free base basis)

Useful 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).
A 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.

Primary Target
Substrate for the determination of cathepsin D activity
Product does not compete with ATP.
Reversible: no
Cell permeable: no

Toxicity: Standard Handling (A)

Bz-Arg-Gly-Phe-Phe-Pro-4MeOβNA, HCl

Takahashi, T., and Tang, J. 1981. Methods Enzymol.80, 565.
Smith, R.E., and Van Frank, R.M. 1975. in Lysosomes in Biology and Pathology4 (Dingle, J.T., and Dean, R.T., eds.) p. 193, American Elsevier, Holland.

CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany

100

≥95% (HPLC)

lyophilized solid

Calbiochem^®

OK to freeze
desiccated
protect from light

white

DMSO: 5 mg/mL

λ_ex ~345 nm
λ_em ~425 nm

ambient

−20℃

10 mg in Plastic ampoule

11 - Combustible Solids

WGK 1