Tissue Inhibitor of Metalloprotease 2 (TIMP-2) is a member of the TIMP family, which consists of four protease inhibitors: TIMP-1, TIMP-2, TIMP-3, and TIMP-4. These inhibitors play a crucial role in regulating the activity of matrix metalloproteinases (MMPs), which are zinc-dependent endopeptidases involved in the degradation of the extracellular matrix (ECM) and various cell surface proteins .
TIMP-2 is a secreted protein that binds to MMPs, inhibiting their proteolytic activity. This binding prevents MMPs from accessing their catalytic domain, thereby regulating ECM turnover and maintaining tissue homeostasis . TIMP-2 is unique among the TIMP family members due to its ability to form a complex with MMP-14, which in turn activates pro-MMP-2, highlighting its dual role in both inhibition and activation of MMPs .
The regulation of MMP activity by TIMP-2 is essential for various physiological processes, including tissue repair, wound healing, angiogenesis, and morphogenesis . An imbalance between TIMPs and MMPs has been linked to several pathological conditions, such as rheumatoid arthritis, cardiovascular diseases, cancer metastasis, and endometriosis .
Recombinant TIMP-2 (Human, Sf9) is produced using the Sf9 insect cell expression system. This system is widely used for the production of recombinant proteins due to its ability to perform post-translational modifications similar to those in mammalian cells . The recombinant TIMP-2 produced in Sf9 cells retains its biological activity and is used in various research applications, including enzymatic assays and studies on ECM regulation .
Recombinant TIMP-2 is utilized as a positive control in enzymatic assays to study MMP activity and inhibition . It is also employed in research focused on understanding the mechanisms of ECM turnover and the role of TIMPs in various diseases . Additionally, recombinant TIMP-2 is used in studies investigating the therapeutic potential of TIMPs in treating conditions associated with excessive MMP activity .