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MMP inhibitor
BML-EI325-0001 1 mg 84.00 USD
BML-EI325-0005 5 mg 336.00 USD
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Competitive, mechanism-based inhibitor of matrix metalloproteinases 2 and 9 (MMP-2 and MMP-9). It possesses Ki values in the nanomolar range against the gelatinases (14nM for MMP-2; 600nM for MMP-9), but in the micromolar range against other metalloproteinases (206µM for MMP-1, 15µM for MMP-3, 96µM for MMP-7, and 4µM for ADAM17/TACE). This inhibitor has also been used in vitro, in vivo, and in tissue culture. In vivo, it is metabolized to an even more potent gelatinase inhibitor.

Product Details

Purity:≥98% (TLC)
Appearance:White solid.
Solubility:Soluble in DMSO (at least 30mM) or 100% ethanol.
Shipping:Blue Ice
Long Term Storage:-20°C
Regulatory Status:RUO - Research Use Only
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Product Literature References

ADAM17 Mediates Proteolytic Maturation of Voltage-Gated Calcium Channel Auxiliary α2δ Subunits, and Enables Calcium Current Enhancement: I. Kadurin, et al.; Function (Oxf.) 3, zqac013 (2022), Abstract;
Primitive macrophages control HSPC mobilization and definitive haematopoiesis: J. Travnickova, et al.; Nat. Commun. 6, 6227 (2015), Application(s): Cell Culture, Assay, Abstract;
Metabolism of a highly selective gelatinase inhibitor generates active metabolite: M. Lee et al.; Chem. Biol. Drug. Des. 70, 371 (2007), Abstract;
Inhibition of human prostate cancer growth, osteolysis and angiogenesis in a bone metastasis model by a novel mechanism-based selective gelatinase inhibitor: R. D. Bonfil et al.; Cancer Res. 118, 2721 (2006), Abstract;
Antimetastatic activity of a novel mechanism-based gelatinase inhibitor: A. Krüger, et al.; Cancer Res. 65, 3523 (2005), Abstract; Full Text
A Convenient Synthesis of a Selective Gelatinase Inhibitor as an Antimetastatic Agent: I.T. Lim, et al.; J. Org. Chem. 69, 3572 (2004), Abstract;
Pronounced diversity in electronic and chemical properties between the catalytic zinc sites of tumor necrosis factor-alpha-converting enzyme and matrix metalloproteinases despite their high structural similarity: A. Solomon et al.; J. Biol. Chem. 279, 31646 (2004), Abstract;
Complex pattern of membrane type 1 matrix metalloproteinase shedding. Regulation by autocatalytic cells surface inactivation of active enzyme: M. Toth et al.; J. Biol. Chem. 277, 26340 (2002), Abstract;
X-ray absorption studies of human matrix metalloproteinase-2 (MMP-2) bound to a highly selective mechanism-based inhibitor. comparison with the latent and active forms of the enzyme: O. Kleifeld et al.; J. Biol. Chem. 276, 17125 (2001), Abstract;
Potent and Selective Mechanism-Based Inhibition of Gelatinases: S. Brown et al.; J. Am. Chem. Soc. 122, 6799 (2000), Abstract;

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