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TIMP-1 // Tissue Inhibitor of Metalloproteinase 1

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The MMPs family comprises at least 24 different MMPs with high sequence similarity in their catalytic domains. MMPs are synthetized as pro-enzymes which are inactive until removal of their pro-domain (Löffek et al., 2011; Nagase and Woessner, 1999). Tissue Inhibitor of Metalloproteinase family comprises 4 members. They are two-domain proteins with a N-Terminal domain of approximately 125 residues and a C terminal domain of about 65 residues (Brew et al., 2000). TIMPs complexes with MMPs and interact with the catalytic domain of MMPs, that results in inhibition of the MMP activity (Gomis-R et al., 1997). Mature TIMP-1 protein is a 28kDa protein which inhibit all MMPs (but is a poor inhibitor of Membrane Type (MT1-MMP, MT3-MMP, MT5-MMP and MMP19). It also bind proMMP-9 and inhibit ADAM10 (Murphy, 2011).

Bioclinica Lab employs a manual sandwich immunoassay for TIMP-1 measurement in serum.

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