The Cleaved-MMP3 (F100) Antibody is a rabbit polyclonal IgG targeting residues 81–130 of human MMP3. Key attributes include:
MMP3 (Stromelysin-1) undergoes proteolytic cleavage to become enzymatically active. The antibody specifically recognizes the F100 cleavage site, a critical region for its activation. Key roles of activated MMP3 include:
Degradation of extracellular matrix components (e.g., fibronectin, collagen III/IV) .
Regulation of immune responses and antiviral activity (e.g., against influenza A) .
In cancer, MMP3 promotes metastasis by reorganizing the extracellular matrix and activating pathways like Erk1/2 and NF-κB .
Colon Cancer: MMP3 knockdown combined with oncolytic VSV therapy reduced tumor growth and lung metastasis in mice .
Therapeutic Targeting: MMP3 inhibition (via siRNA or inhibitor NNGH) enhanced the efficacy of virotherapy in mouse models .
Specificity: The antibody selectively binds the cleaved MMP3 fragment, as shown in Western blots of apoptotic HCT116 cells .
Structural Basis: Antibody recognition depends on the DXXD motif at caspase-cleaved ends, enabling detection of diverse substrates with similar tertiary structures .