In Abcam's MMP-1 Inhibitor Screening Kit, MMP-1 hydrolyzes a specific FRET substrate to release a quenched fluorescent group, which can be detected at Em/Ex = 490/520nm. In presence of potent MMP-1 inhibitors the hydrolyzation of substrate will be inhibited or stopped. The kit provides a rapid, simple, sensitive, and reliable test suitable as a high throughput screening assay of MMP-1 inhibitors. For comparison of the relative efficacy of test inhibitors, a control inhibitor, GM 6001 (IC50 = 0.4 nM for MMP-1) is included. Visit our FAQs page for tips and troubleshooting.
The Matrix metalloproteinase-1 (MMP-1, Interstitial collagenase, fibroblast collagenase) is a member of a multigene family of calcium-dependent, zinc-containing endoproteinases, the matrix metalloproteinases (MMPs). The MMPs are responsible for the degradation of the extracellular matrix (ECM) including collagens, elastins, gelatin, matrix glycoproteins and proteoglycan during normal development and disease processes. MMPs are regulated by hormones, growth factors and cytokines. MMP-1 belongs to the subclass, the collagenases, and along with MMP-8, and MMP-13 are the only members of the MMP family that are capable of degrading the types I, II and III interstitial collagens with high efficiency. These collagens are primarily found in bone, cartilage and skin.
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.
Post-translational 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.