A calpain and papain substrate
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Suc-Leu-Tyr-AMC

Item No. 10008120

Product Insert (PDF)Safety Data Sheet (SDS) (PDF)
Technical Information
Formal Name
N-(3-carboxy-1-oxopropyl)-L-leucyl-N-(4-methyl-2-oxo-2H-1-benzopyran-7-yl)-L-tyrosinamide
CAS Number
94367-20-1
Synonyms
  • Suc-LY-AMC
Molecular Formula
C29H33N3O8
Formula Weight
551.6
Purity
≥98%
Formulation (Request formulation change)
A crystalline solid
Solubility(Learn about Variance in Solubility)
DMF: 30 mg/mlDMSO: 30 mg/mlDMSO:PBS(pH7.2) (1:1): 0.5 mg/mlEthanol: 20 mg/ml
λmax
328 nm
SMILES
CC(C1=CC=C(C=C1O2)NC([C@H](CC3=CC=C(C=C3)O)NC([C@@H](NC(CCC(O)=O)=O)CC(C)C)=O)=O)=CC2=O
InChi Code
InChI=1S/C29H33N3O8/c1-16(2)12-22(31-25(34)10-11-26(35)36)29(39)32-23(14-18-4-7-20(33)8-5-18)28(38)30-19-6-9-21-17(3)13-27(37)40-24(21)15-19/h4-9,13,15-16,22-23,33H,10-12,14H2,1-3H3,(H,30,38)(H,31,34)(H,32,39)(H,35,36)/t22-,23-/m0/s1
InChi Key
RIYLNECMTVNMSO-GOTSBHOMSA-N
Shipping & Storage Information
Storage
-20°C
Shipping
Room temperature in continental US; may vary elsewhere
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    5 mg

    $41

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    10 mg

    $69

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    25 mg

    $119

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    50 mg

    $215

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    Product Description

    Suc-Leu-Tyr-AMC is a fluorescent substrate for calpain I and II and papain (another cysteine protease) that is used for measuring the chymotrypsin-like peptidase activity of the 20S proteasome (excitation max: 360 nm; emission max: 460 nm).1,2,3 Suc-Leu-Tyr-AMC can also be cleaved by the Ti protease from E. coli.4

    WARNING This product is not for human or veterinary use.

    References & Product Citations
    Product Description References

    1. Seol, J.H., Park, S.C., Ha, D.B., et al. Na+, K+-specific inhibition of protein and peptide hydrolyses by proteasomes from human hepatoma tissues. FEBS Lett. 247(2), 197-200 (1989).

    2. Sasaki, T., Kikuchi, T., Yumoto, N., et al. Comparative specificity and kinetic studies on porcine calpain I and calpain II with naturally occurring peptides and synthetic fluorogenic substrates. The Journal of Biological Chemisty 259(20), 12489-12494 (1984).

    3. Edelstein, C.L., Wieder, E.D., Yaqoob, M.M., et al. The role of cysteine proteases in hypoxia-induced rat renal proximal tubular injury. Proc. Natl. Acad. Sci. USA 92, 7662-7666 (1995).

    4. Woo, K.M., Chung, W.J., Ha, D.B., et al. Protease Ti from escherichia coli requires ATP hydrolysis for protein breakdown but not for hydrolysis of small peptides. The Journal of Biological Chemisty 264(4), 2088-2091 (1989).