The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
Use at an assay dependent concentration. PubMed: 28186971
1/500 - 1/1000. Detects a band of approximately 66 kDa (predicted molecular weight: 66 kDa).
Seems to specifically activate progelatinase A. May thus trigger invasion by tumor cells by activating progelatinase A on the tumor cell surface. May be involved in actin cytoskeleton reorganization by cleaving PTK7.
Expressed in stromal cells of colon, breast, and head and neck. Expressed in lung tumors.
Belongs to the peptidase M10A family. Contains 4 hemopexin-like domains.
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.
The precursor is cleaved by a furin endopeptidase.
Membrane. Melanosome. Identified by mass spectrometry in melanosome fractions from stage I to stage IV.
Jiang B et al. Ensnaring membrane type 1-matrix metalloproteinase (MT1-MMP) with tissue inhibitor of metalloproteinase (TIMP)-2 using the haemopexin domain of the protease as a carrier: a targeted approach in cancer inhibition. Oncotarget8:22685-22699 (2017).
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