A colorimetric collagenase substrate
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FALGPA (trifluoroacetate salt)

Item No. 37374

Product Insert (PDF)Safety Data Sheet (SDS) (PDF)
Technical Information
Formal Name
N-[3-(2-furanyl)-1-oxo-2-propen-1-yl]-L-leucylglycyl-L-prolyl-L-alanine, trifluoroacetate salt
Synonyms
  • 2-Furanacryloyl-L-leucylglycyl-L-prolyl-L-alanine
  • 2-Furanacryloyl-Leu-Gly-Pro-Ala-OH
Molecular Formula
C23H32N4O7 • XCF3COOH
Formula Weight
476.5
Purity
≥95%
Formulation (Request formulation change)
A solid
Peptide Sequence
Fa-LGPA-OH (Fa = furanacryloyl)
Solubility(Learn about Variance in Solubility)
DMF: 30 mg/mlDMSO: 30 mg/mlEthanol: 30 mg/mlPBS (pH 7.2): Slightly soluble
SMILES
O=C(C=CC1=CC=CO1)N[C@@H](CC(C)C)C(NCC(N2[C@H](C(N[C@@H](C)C(O)=O)=O)CCC2)=O)=O.OC(C(F)(F)F)=O
InChi Code
InChI=1S/C23H32N4O7.C2HF3O2/c1-14(2)12-17(26-19(28)9-8-16-6-5-11-34-16)21(30)24-13-20(29)27-10-4-7-18(27)22(31)25-15(3)23(32)33;3-2(4,5)1(6)7/h5-6,8-9,11,14-15,17-18H,4,7,10,12-13H2,1-3H3,(H,24,30)(H,25,31)(H,26,28)(H,32,33);(H,6,7)/t15-,17-,18-;/m0./s1
InChi Key
ATJHWLGMTQCBIY-OOAIBONUSA-N
Shipping & Storage Information
Storage
-20°C
Shipping
Room temperature in continental US; may vary elsewhere
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    1 mg

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    25 mg

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    Cayman Chemical
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    Product Description

    FALGPA is a colorimetric substrate for collagenase.1,2 It is selective for collagenase over trypsin, thermolysin, and elastase.1 Collagenase preferentially binds to and cleaves the Leu-Gly (LG) peptide sequence to release the furanacryloyl group, which can be quantified by colorimetric detection at 324 to 345 nm as a measure of collagenase activity. FALGPA has been used to identify inhibitors of C. histolyticum collagenase.3

    WARNING This product is not for human or veterinary use.

    References & Product Citations
    Product Description References

    1. Van Wart, H.E., and Steinbrink, D.R. A continuous spectrophotometric assay for Clostridium histolyticum collagenase. Anal. Biochem. 113(2), 356-365 (1981).

    2. Jackson, R.J., Dao, M.L., and Lim, D.V. Modified FALGPA assay for cell-associated collagenolytic activity. J. Microbiol. Methods 21(2), 209-215 (1995).

    3. Yiotakis, A., Hatgiyannacou, A., Dive, V., et al. New thiol inhibitors of Clostridium histolyticum collagenase. Importance of the P3' position. Eur. J. Biochem. 172(3), 761-766 (1988).