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Your Position: Home > Protein > MMP-7 > MM7-C53H3

Cynomolgus MMP-7 Protein, His Tag (active enzyme, HPLC verified)

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  • Synonym
    MMP7,Matrilysin,Matrin,MPSL1,PUMP1
  • Source
    Cynomolgus MMP-7 Protein, His Tag(MM7-C53H3) is expressed from CHO cells. It contains AA Leu 21 - Lys 270 (Accession # G7PNJ9).
    Predicted N-terminus: Leu 21
  • Molecular Characterization
    MMP-7 Structure

    This protein carries a polyhistidine tag at the C-terminus.

    The protein has a calculated MW of 29.9 kDa. The protein migrates as 30-32 kDa when calibrated against Star Ribbon Pre-stained Protein Marker under reducing (R) condition (SDS-PAGE) due to glycosylation.

  • Endotoxin
    Less than 1.0 EU per μg by the LAL method / rFC method.
  • Purity

    >90% as determined by SDS-PAGE.

    >90% as determined by SEC-HPLC.

  • Formulation

    Supplied as 0.2 μm filtered solution in 10 mM HEPES, 150 mM NaCl, pH7.5 with glycerol as protectant.

    Contact us for customized product form or formulation.

  • Shipping

    This product is supplied and shipped with dry ice, please inquire the shipping cost.

  • Storage

    Please avoid repeated freeze-thaw cycles.

    This product is stable after storage at:

    1. The product MUST be stored at -70°C or lower upon receipt;
    2. -70°C for 3 months under sterile conditions.
SDS-PAGE
MMP-7 SDS-PAGE

Cynomolgus MMP-7 Protein, His Tag on SDS-PAGE under reducing (R) condition. The gel was stained with Coomassie Blue. The purity of the protein is greater than 90% (With Star Ribbon Pre-stained Protein Marker).

SEC-HPLC
MMP-7 SEC-HPLC

The purity of Cynomolgus MMP-7 Protein, His Tag (Cat. No. MM7-C53H3) was greater than 90% as determined by SEC-HPLC.

Bioactivity

Measured by its ability to cleave the fluorogenic peptide substrate Mca-PLGL-Dpa-AR-NH2. The specific activity is >350 pmol/min/μg (QC tested).

  • Background
    MMP-7 (matrilysin), the smallest zinc-dependent endopeptidase in the MMP family, lacks a hemopexin domain but features a catalytic zinc-binding motif (HEXXHXXGXXH) critical for degrading extracellular matrix (ECM) components, including collagens III/IV/V, elastin, and proteoglycans. Activated via proteolytic cleavage (e.g., by MMP-3), it promotes tissue remodeling in wound healing while driving pathological processes such as tumor invasion (via E-cadherin degradation and Wnt/β-catenin activation) and fibrosis (via β-catenin-mediated renal damage). Overexpressed in epithelial cancers, MMP-7 correlates with metastasis but paradoxically shows protective genetic variants in some contexts. It also processes non-ECM substrates like TNF-α and Fas ligand, amplifying inflammation and oncogenesis. In fibrotic diseases, elevated serum MMP-7 predicts progression, serving as a diagnostic biomarker. Therapeutic strategies targeting MMP-7, including inhibitors and monoclonal antibodies, highlight its dual roles as both a driver of ECM disruption and a modulator of immune-tumor interactions.
  • Clinical and Translational Updates

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  • Number of Drugs in Clinical Trials:1 Details
  • Latest Research Phase:Phase 2 Clinical

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