A fluorogenic substrate for MMP-1, MMP-2, MMP-7, and MMP-9
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Dnp-PLGLWA-DArg-NH2 (trifluoroacetate salt)

Item No. 24841

Product Insert (PDF)Safety Data Sheet (SDS) (PDF)
Technical Information
Formal Name
1-(2,4-dinitrophenyl)-L-prolyl-L-leucylglycyl-L-leucyl-L-tryptophyl-L-alanyl-D-argininamide, trifluoroacetate salt
Molecular Formula
C45H64N14O11 • XCF3COOH
Formula Weight
977.1
Purity
≥95%
Formulation (Request formulation change)
A lyophilized powder
Solubility(Learn about Variance in Solubility)
Formic Acid: 1 mg/ml
SMILES
O=C(CNC([C@H](CC(C)C)NC([C@H]1N(C2=CC=C([N+]([O-])=O)C=C2[N+]([O-])=O)CCC1)=O)=O)N[C@@H](CC(C)C)C(N[C@@H](CC3=CNC4=C3C=CC=C4)C(N[C@@H](C)C(N[C@@H](C(N)=O)CCCNC(N)=N)=O)=O)=O.FC(F)(C(O)=O)F
InChi Code
InChI=1S/C45H64N14O11.C2HF3O2/c1-24(2)18-32(56-44(66)36-13-9-17-57(36)35-15-14-28(58(67)68)21-37(35)59(69)70)41(63)51-23-38(60)53-33(19-25(3)4)43(65)55-34(20-27-22-50-30-11-7-6-10-29(27)30)42(64)52-26(5)40(62)54-31(39(46)61)12-8-16-49-45(47)48;3-2(4,5)1(6)7/h6-7,10-11,14-15,21-22,24-26,31-34,36,50H,8-9,12-13,16-20,23H2,1-5H3,(H2,46,61)(H,51,63)(H,52,64)(H,53,60)(H,54,62)(H,55,65)(H,56,66)(H4,47,48,49);(H,6,7)/t26-,31+,32-,33-,34-,36-;/m0./s1
InChi Key
GMYYKUSXNGFHND-RWQUALJJSA-N
Shipping & Storage Information
Storage
-20°C
Shipping
Room temperature in continental US; may vary elsewhere
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    1 mg

    $112

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    Product Description

    Dnp-PLGLWA-DArg-NH2 is a fluorogenic substrate for matrix metalloproteinase-1 (MMP-1), MMP-2, MMP-7, and MMP-9.1,2 The activity of MMP-1, MMP-2, MMP-7, and MMP-9 can be quantified by measuring tryptophan fluorescence that is unquenched upon peptide hydrolysis that removes the N-terminal dinitrophenol (Dnp) group.

    WARNING This product is not for human or veterinary use.

    References & Product Citations
    Product Description References

    1. Stack, M.S., and Gray, R.D. Comparison of vertebrate collagenase and gelatinase using a new fluorogenic substrate peptide. The Journal of Biological Chemisty 264(8), 4277-4281 (1989).

    2. Crabbe, T., Willenbrock, F., Eaton, D., et al. Biochemical characterization of matrilysin. Activation conforms to the stepwise mechanisms proposed for other matrix metalloproteinases. Biochemistry 31(36), 8500-8507 (1992).