Metalloproteinases
Recombinant Active Metalloproteinases
HEK293-expressed MMPs, ADAMs, and ADAMTS enzymes — active and sequence-verified — for gelatinase assays, inhibitor screening, and ECM substrate cleavage studies, backed by 32 years of proteinase biology.
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Triple Point Biologics' Metalloproteinases recombinant catalog covers more than 40 individual proteins, including MMP-1 through MMP-28, the membrane-type MMPs (MT-MMPs), ADAM10, ADAM17, and multiple ADAMTS family members. Metalloproteinases are zinc-dependent endopeptidases that share a conserved catalytic domain containing the HEXXH zinc-binding motif. They are expressed across virtually all tissue types and act on a broad range of substrates — extracellular matrix (ECM) components such as collagens, fibronectin, and laminin, as well as cell-surface receptors, growth factors, and cytokines. The ADAMTS subfamily includes ADAMTS13, the primary von Willebrand factor-cleaving protease, whose activity has been extensively characterized in published studies of thrombotic thrombocytopenic purpura. Collectively, MMPs, ADAMs, and ADAMTS proteins have been investigated in models of tumor invasion and metastasis, ECM remodeling, ectodomain shedding, and acute and chronic inflammation.
All recombinant metalloproteinases in this collection are expressed in HEK293 cells to support mammalian post-translational processing, including glycosylation patterns relevant to native activity. Each catalog entry is paired with a matched rabbit polyclonal antibody raised in-house against the same recombinant protein, produced using antibody development protocols Triple Point Biologics has refined since 1994. The antibodies are validated for Western blot and IHC; cross-reactivity with closely related family members is annotated as predicted or experimentally validated on individual product pages. This recombinant–antibody pairing from a single production source reduces lot-to-lot variability when both reagents are used in the same experimental system.
Common applications for these recombinant proteins include fluorogenic and colorimetric protease activity assays (see the protease activity assay guide), zymography, substrate-specificity profiling, and use as positive controls in ELISA or immunoblot workflows (see using recombinant proteins as positive controls). Inhibitor screening studies frequently use the active, catalytic-domain constructs, while pro-domain and full-length variants are available where autoactivation or TIMP-interaction experiments require intact prodomain sequences.