H-TIMP-2 is the second described of the four known mammalian TIMPs. The TIMPs are so named because they are slow, tight binding endogenous inhibitors of the Matrix Metalloproteinases (MMPs). TIMP-2 is constitutively produced by most cell types in culture, along with MMP-2 (Gelatinase-A). Although TIMP-2 is an efficient inhibitor of MMP-2, it is also required at low concentrations for the activation of MMP-2. It is thought that the MMP-2 is activated by a membrane-bound MMP; and that the TIMP-2 is required to bring the MMP-2 to the cell surface. The four TIMPs have different inhibition constants for the different MMPs studied. TIMP-2 has a greater efficiency against MMP-2, and TIMP-1 works better against MMP-9, MMP-1 and MMP-3. In addition to inhibiting the MMPs, TIMPs have been shown to have activity against the ADAMs family of proteinases. TIMP-3 is an efficient "sheddase" inhibitor, inhibiting ADAM-17 (TACE) at the low nanomolar levels seen with MMP inhibition. The other ADAMs proteinases have not yet been assayed for TIMP inhibition, but TIMP-2 seems to be much less active on ADAM-17 than is TIMP-3. H-TIMP-2 can be used as a positive control in enzymatic assays, ELISA assays, Western blots and substrate gel analysis (reverse zymograms). The TIMP-2 is unglycosylated, about 22 kD in size on reduced Western blots.

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