Recombinant Human TIMP-3 (Metalloproteinase inhibitor 3) Fragment (aa 24-211) is a high-purity protein that encompasses the complete N-terminal domain, providing researchers with an essential tool for studying extracellular matrix regulation, angiogenesis inhibition, and metalloproteinase activity. This 188-amino acid fragment retains key functional properties of the full-length protein, making it ideal for investigating TIMP-3's role in tissue remodeling and cancer biology.

TIMP-3 (Tissue inhibitor of metalloproteinases 3) is a secreted extracellular matrix protein that mediates critical processes including matrix regulation, inflammation, and angiogenesis through reversible inhibition of zinc protease enzymes. It functions as a potent regulator of extracellular matrix remodeling by inhibiting multiple matrix metalloproteinases (MMP-1, MMP-2, MMP-3, MMP-7, MMP-9, MMP-13, MMP-14, and MMP-15) and modulates the processing of amyloid precursor protein and apolipoprotein E receptor by inhibiting alpha-se