A fluorogenic substrate for MMP-7
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Dnp-RPLALWRS (trifluoroacetate salt)

Item No. 24699

Product Insert (PDF)Safety Data Sheet (SDS) (PDF)
Technical Information
Formal Name
N2-(2,4-dinitrophenyl)-L-arginyl-L-prolyl-L-leucyl-L-alanyl-L-leucyl-L-tryptophyl-L-arginyl-L-serine, 2,2,2-trifluoroacetate
Synonyms
  • Dnp-Arg-Pro-Leu-Ala-Leu-Trp-Arg-Ser-OH
  • Matrix Metalloproteinase-7 Fluorogenic Substrate
  • MMP-7 Fluorogenic Substrate
Molecular Formula
C52H77N17O14 • XCF3COOH
Formula Weight
1164.3
Purity
≥95%
Formulation (Request formulation change)
A lyophilized powder
Solubility(Learn about Variance in Solubility)
Formic Acid: 1 mg/ml
SMILES
CC(C)C[C@H](NC([C@H](C)NC([C@H](CC(C)C)NC([C@H]1N(C([C@H](CCCNC(N)=N)NC2=CC=C([N+]([O-])=O)C=C2[N+]([O-])=O)=O)CCC1)=O)=O)=O)C(N[C@H](C(N[C@@H](CCCNC(N)=N)C(N[C@@H](CO)C(O)=O)=O)=O)CC3=CNC4=C3C=CC=C4)=O.FC(F)(C(O)=O)F
InChi Code
InChI=1S/C52H77N17O14.C2HF3O2/c1-27(2)21-37(65-48(76)41-15-10-20-67(41)49(77)36(14-9-19-58-52(55)56)61-34-17-16-31(68(80)81)24-42(34)69(82)83)45(73)60-29(5)43(71)63-38(22-28(3)4)46(74)64-39(23-30-25-59-33-12-7-6-11-32(30)33)47(75)62-35(13-8-18-57-51(53)54)44(72)66-40(26-70)50(78)79;3-2(4,5)1(6)7/h6-7,11-12,16-17,24-25,27-29,35-41,59,61,70H,8-10,13-15,18-23,26H2,1-5H3,(H,60,73)(H,62,75)(H,63,71)(H,64,74)(H,65,76)(H,66,72)(H,78,79)(H4,53,54,57)(H4,55,56,58);(H,6,7)/t29-,35-,36-,37-,38-,39-,40-,41-;/m0./s1
InChi Key
AMNGVBSVDFWDQG-BZDQHTQVSA-N
Shipping & Storage Information
Storage
-20°C
Shipping
Room temperature in continental US; may vary elsewhere
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    500 µg

    $103

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    1 mg

    $183

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    Product Description

    Dnp-RPLALWRS is a fluorogenic substrate for matrix metalloproteinase-7 (MMP-7).1 The activity of MMP-7 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. Welch, A.R., Holman, C.N., Browner, M.F., et al. Purification of human matrilysin produced in Escherichia coli and characterization using a new optimized fluorogenic peptide substrate. Arch. Biochem. Biophys. 324(1), 59-64 (1995).