Tissue Inhibitor of Metalloprotease 2 is a recombinant enzyme.
MMPs are secreted by diverse connective tissue and pro-inflammatory cells. Typically, these enzymes exhibit minimal expression under normal physiological circumstances. MMPs assume a pivotal role in various cellular processes, including cell proliferation, migration, differentiation, angiogenesis, apoptosis, and immunity. They share a common domain structure, consisting of three key components. First is the pro-peptide, which requires removal to activate the enzyme. Next, there is the catalytic domain, featuring a cysteine switch, where a cysteine residue interacts with zinc, and the haemopexin-like C-terminal domain is linked to the catalytic domain via a flexible hinge region. TIMP-2 (Tissue Inhibitor of Metalloproteinases 2) is indeed a natural inhibitor of the matrix metalloproteinases (MMPs). It forms complexes with certain enzymes within the metalloproteinase family, leading to their irreversible inactivation. TIMP-2 is known to act on a wide range of MMPs, including MMP-1, MMP-2, MMP-3, MMP-7, MMP-8, MMP-9, MMP-10, MMP-13, MMP-14, MMP-15, MMP-16, and MMP-19. Interestingly, TIMP-2 shares a significant degree of amino acid sequence homology, about 40%, with TIMP-1, especially in their N-terminal domains. This structural similarity underscores their related functions as inhibitors of metalloproteinases, despite some differences in their specific roles and affinities for certain MMPs.
Proteins and Peptides
Human
E. coli
Metalloproteinase Inhibitor 2 (TIMP2)
E. coli
Lyophilized
SDS-PAGE
5 µg
20 µg
1 mg
Recombinant
> 95% (SDS-PAGE and RP-HPLC)
TIMP2
No
Shipped within 5-10 working days.
This product is for research use only. <p></p> Not for human consumption, cosmetic, therapeutic or diagnostic use.
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