Key features and details
- Assay type: Enzyme activity
- Detection method: Colorimetric
- Platform: Microplate reader
- Sample type: Inhibitor compounds
Product nameMMP1 Inhibitor Screening Assay Kit (Colorimetric)
See all MMP1 kits
Sample typeInhibitor compounds
Assay typeEnzyme activity
Abcam MMP1 Inhibitor Screening Assay Kit (Colorimetric) (ab139443) is a complete assay system designed to screen MMP1 inhibitors using a thiopeptide as a chromogenic substrate (Ac-PLG-[2-mercapto-4-methyl-pentanoyl]-LG-OC2H5). The MMP cleavage site peptide bond is replaced by a thioester bond in the thiopeptide. Hydrolysis of this bond by an MMP produces a sulfhydryl group, which reacts with DTNB [5,5’-dithiobis(2-nitrobenzoic acid), Ellman’s reagent] to form 2-nitro-5-thiobenzoic acid, which can be detected by its absorbance at 412 nm (ε=13,600 M-1cm-1 at pH 6.0 and above). The assays are performed in a convenient 96-well microplate format.
This kit is useful to screen inhibitors of MMP1, a potential therapeutic target. The MMP inhibitor NNGH is also included as a prototypic control inhibitor.
Thiol inhibitors should not be used with this kit, as they may interfere with the colorimetric assay.
Storage instructionsPlease refer to protocols.
Components 1 x 96 tests 96-well Clear Microplate (1/2 Volume) 1 unit Colorimetric Assay Buffer 1 x 20ml MMP Inhibitor 1 x 50µl MMP Substrate 1 x 50µl MMP1 Enzyme (Human, Recombinant) 1 x 66µl
FunctionCleaves collagens of types I, II, and III at one site in the helical domain. Also cleaves collagens of types VII and X. In case of HIV infection, interacts and cleaves the secreted viral Tat protein, leading to a decrease in neuronal Tat's mediated neurotoxicity.
Sequence similaritiesBelongs to the peptidase M10A family.
Contains 4 hemopexin-like domains.
DomainThere are two distinct domains in this protein; the catalytic N-terminal, and the C-terminal which is involved in substrate specificity and in binding TIMP (tissue inhibitor of metalloproteinases).
The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.
modificationsUndergoes autolytic cleavage to two major forms (22 kDa and 27 kDa). A minor form (25 kDa) is the glycosylated form of the 22 kDa form. The 27 kDa form has no activity while the 22/25 kDa form can act as activator for collagenase.
Cellular localizationSecreted > extracellular space > extracellular matrix.
- Information by UniProt
- 27 kDa interstitial collagenase
ab139443 has been referenced in 1 publication.
- Gonulalan EM et al. A new perspective on evaluation of medicinal plant biological activities: The correlation between phytomics and matrix metalloproteinases activities of some medicinal plants. Saudi Pharm J 27:446-452 (2019). PubMed: 30976190