Rabbit Anti-Rat Matrix Metalloproteinase 3 (MMP3) Polyclonal Antibody

Rat matrix metalloproteinase 3 (MMP-3, stromelysin-1) is a 477-residue secreted zinc-dependent endopeptidase comprising an N-terminal pro-domain (residues 1-99), a catalytic domain with the conserved HEXXHXXGXXH zinc-binding motif, and a C-terminal hemopexin-like module that confers substrate specificity. Upon activation, the pro-peptide is cleaved to generate the 45 kDa active enzyme, which degrades fibronectin, laminin, and collagens III-V. Constitutively expressed in synovial fibroblasts, uterus, and involuting mammary gland, MMP-3 localizes to extracellular matrix and pericellular sites. Antibodies raised against the catalytic or hemopexin domain detect latent, active, and fragmented forms with negligible cross-reactivity to other MMP family members, enabling selective immunoblot and immunohistochemical visualization in rat tissue homogenates and culture supernatants.