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ADAMTS13 and 15 are not regulated by the full length and N-terminal domain forms of TIMP-1, -2, -3 and -4

A disintegrin and metalloproteinase with thombospondin motifs (ADAMTS) 13 and 15 are secreted zinc proteinases involved in the turnover of von Willebrand factor and cancer suppression. In the present study, ADAMTS13 and 15 were subjected to inhibition studies with the full-length and N-terminal domain forms of tissue inhibitor of metalloproteinases (TIMPs)-1 to -4. TIMPs have no ability to inhibit the ADAMTS proteinases in the full-length or N-terminal domain form. While ADAMTS13 is also not sensitive to the hydroxamate inhibitors, batimastat and ilomastat, ADAMTS15 can be effectively inhibited by batimastat (Kiapp 299 nM). In conclusion, the present results indicate that TIMPs are not the regulators of these two ADAMTS proteinases.

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Cat.No. Product Name Information Publications Customer Product Validation
S7155 Batimastat (BB-94) Batimastat (BB-94) is a potent, broad spectrum matrix metalloprotease (MMP) inhibitor for MMP-1, MMP-2, MMP-9, MMP-7 and MMP-3 with IC50 of 3 nM, 4 nM, 4 nM, 6 nM and 20 nM, respectively. Also inhibits the activitity of other metalloproteases, such as ADAM17. (20) (4)

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MMP