Human Tissue Inhibitor of Metalloprotease 2 (TIMP2) Enzyme is a recombinant enzyme produced in HEK cells. This gene is a member of the TIMP gene family. The proteins encoded by this gene family are natural inhibitors of the matrix metalloproteinases, a group of peptidases involved in degradation of the extracellular matrix. In addition to an inhibitory role against metalloproteinases, the encoded protein has a unique role among TIMP family members in its ability to directly suppress the proliferation of endothelial cells. As a result, the encoded protein may be critical to the maintenance of tissue homeostasis by suppressing the proliferation of quiescent tissues in response to angiogenic factors, and by inhibiting protease activity in tissues undergoing remodelling of the extracellular matrix. [provided by RefSeq, Jul 2008].
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
HEK293 cells
Tissue Inhibitor of Metalloprotease 2 (TIMP2)
HEK293 cells
Lyophilized
SDS-PAGE
2 µg
10 µg
1 mg
Recombinant
> 95% (SDS-PAGE)
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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