A fluorogenic peptide substrate
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Bz-FVR-AMC (trifluoroacetate salt)

Item No. 24845

Product Insert (PDF)Safety Data Sheet (SDS) (PDF)
Technical Information
Formal Name
N-((S)-1-(((S)-1-(((S)-5-guanidino-1-((4-methyl-2-oxo-2H-chromen-7-yl)amino)-1-oxopentan-2-yl)amino)-3-methyl-1-oxobutan-2-yl)amino)-1-oxo-3-phenylpropan-2-yl)benzamide, trifluoroacetate salt
Synonyms
  • Benzoyl-Phe-Val-Arg-AMC
  • Thrombin Fluorogenic Substrate III
Molecular Formula
C37H43N7O6 • XCF3COOH
Formula Weight
681.8
Purity
≥95%
Formulation (Request formulation change)
A lyophilized powder
Solubility(Learn about Variance in Solubility)
Water: 1 mg/ml
SMILES
O=C(N[C@@H](CC1=CC=CC=C1)C(N[C@@H](C(C)C)C(N[C@@H](CCCNC(N)=N)C(NC2=CC=C(C(C)=CC(O3)=O)C3=C2)=O)=O)=O)C4=CC=CC=C4.FC(F)(C(O)=O)F
InChi Code
InChI=1S/C37H43N7O6.C2HF3O2/c1-22(2)32(44-35(48)29(20-24-11-6-4-7-12-24)43-33(46)25-13-8-5-9-14-25)36(49)42-28(15-10-18-40-37(38)39)34(47)41-26-16-17-27-23(3)19-31(45)50-30(27)21-26;3-2(4,5)1(6)7/h4-9,11-14,16-17,19,21-22,28-29,32H,10,15,18,20H2,1-3H3,(H,41,47)(H,42,49)(H,43,46)(H,44,48)(H4,38,39,40);(H,6,7)/t28-,29-,32-;/m0./s1
InChi Key
ADUYTEHLGOONRQ-AVTZECDJSA-N
Shipping & Storage Information
Storage
-20°C
Shipping
Room temperature in continental US; may vary elsewhere
Certificates of Analysis & Batch Specific Data

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    1 mg

    $103

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    Product Description

    Bz-FVR-AMC is a fluorogenic peptide substrate for bovine cathepsins S and H, Xenopus endopeptidase XSCEP1, and esterase E-II from B. gabonica venom, among others.1,2,3 Upon enzymatic cleavage, 7-amino-4-methylcoumarin (AMC) is released and its fluorescence can be used to quantify enzyme activity. AMC displays excitation/emission maxima of 340-360/440-460 nm, respectively.

    WARNING This product is not for human or veterinary use.

    References & Product Citations
    Product Description References

    1. Xin, X.-Q., Gunesekera, B., and Mason, R.W. The specificity and elastinolytic activities of bovine cathepsins S and H. Arch. Biochem. Biophys. 299(2), 334-339 (1992).

    2. Darby, N.J., Lackey, D.B., and Smyth, D.G. Purification of a cysteine endopeptidase which is secreted with bioactive peptides from the epidermal glands of Xenopus laevis. Eur. J. Biochem. 195(1), 65-70 (1991).

    3. Cloete, D., Viljoen, C.C., and Schabort, J.C. Deviation from Michaelis-Menten kinetics for esterase E-II from the venom of Bitis gabonica, using synthetic arginine amides as substrates. Toxicon 21(6), 857-869 (1983).