The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
≥ 105 pmole/min/µg.
Activation: This is a proform enzyme and requires activation prior to testing activity. Dilute the enzyme to 100 ng/ml in a solution containing 50 mM HEPES, pH 7.4, 10 mM CaCl2, 0.05% Brij-35, and 1 mM APMA (amino-phenyl mercuric acetate). Incubate at 37ºC for 2 hours. Assay conditions: Reaction mixture with 10 μM 390 MMP substrate 1. Incubate for 30 minutes at room temperature. Fluorescence intensity is measured at exc328/em393.
>90% by SDS-PAGE.
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Preparation and Storage
Stability and Storage
Shipped on Dry Ice. Store at -80°C. Avoid freeze / thaw cycle.
Cleaves 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.
Belongs to the peptidase M10A family. Contains 4 hemopexin-like domains.
There 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.
Undergoes 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.
Secreted > extracellular space > extracellular matrix.