A recombinant fragment of human TIMP2 protein was used as the immunogen for the TIMP2 antibody.
It recognizes a protein of 21kDa, identified as tissue inhibitor of metalloproteinases-2 (TIMP-2). It is closely related to TIMP-1 and shows the highest binding affinity to both the latent (pro) and active forms of 72kDa Type IV collagenase (also known as MMP-2 or gelatinase A). It also has affinity for the active form of 92kDa Type IV collagenase (also known as MMP-9 or gelatinase B). TIMP-2 inhibits the proteolytic invasiveness of tumor cells and normal placental trophoblast cells.
