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MMP inhibitor
BML-EI300-0001 1 mg 68.00 USD
BML-EI300-0005 5 mg 269.00 USD
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Potent broad-spectrum hydroxamate inhibitor of matrix metalloproteinases (MMPs). Ki values have been reported for the following human MMPs: MMP-1 (fibroblast collagenase): 0.4nM; MMP-2 (gelatinase A): 0.5nM; MMP-3 (stromelysin-1): 27nM; MMP-7 (matrilysin): 3.7nM; MMP-8 (neutrophil collagenase): 0.1nM; MMP-9 (gelatinase B): 0.2nM; MMP-12 (metalloelastase): 3.6nM; MMP-14 (MT1-MMP): 13.4nM; MMP-26 (endometase): 0.36nM. Also inhibits MMP-10, MMP-13, MMP-15, MMP-17, MMP-20, MMP-21, TACE, ADAM19, other ADAMs, anthrax lethal factor, neprilysin, leucine aminopeptidase, and DPPIII. Typical concentration range for use in tissue culture is 10-25µM. This inhibitor has also been used in vivo.

Product Specification

Alternative Name:Galardin, Ilomastat, N-[(2R)-2-(Hydroxamidocarbonylmethyl)-4-methylpentanoyl]-L-tryptophan methylamide
Formulation:Lyophilized solid.
Purity:≥98% (HPLC)
Appearance:White to off-white powder.
Solubility:Soluble in DMSO (at least 25mM) or 100% ethanol (10mg/ml)
Shipping:Shipped on Blue Ice
Long Term Storage:-20°C
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Product Literature References

Podosome assembly is controlled by the GTPase ARF1 and its nucleotide exchange factor ARNO: N.B. Rafiq, et al.; J. Cell Biol. 216, 181 (2017), Abstract;
Phenotype anchoring in zebrafish reveals a potential role for matrix metalloproteinases (MMPs) in tamoxifen's effects on skin epithelium: S.M. Bugel, et al.; Toxicol. Appl. Pharmacol. 18, 296 (2016), Application(s): Cell culture, Abstract;
Cross-talk between lysophosphatidic acid receptor 1 and tropomyosin receptor kinase a promotes lung epithelial cell migration: L. Nan, et al.; Biochim. Biophys. Acta 1863, 229 (2015), Application(s): Cell culture, Abstract;
Inside-out Regulation of Ectodomain Cleavage of Cluster-of-Differentiation-44 [CD44] and of Neuregulin-1 requires Substrate Dimerization: M. Hartmann, et al.; J. Biol. Chem. 290, 17041 (2015), Application(s): Cell Culture, Abstract; Full Text
Membrane Cholesterol Modulates LOX-1 Shedding in Endothelial Cells: M. Gioia, et al.; PLoS One 10, e0141270 (2015), Application(s): Hydroxamate inhibitor, Abstract; Full Text
PCSK6-mediated corin activation is essential for normal blood pressure: S. Chen, et al.; Nat. Med. 21, 1048 (2015), Application(s): Protease inhibitor, Abstract;
Fluorescent substrates for the proteinases ADAM17, ADAM10, ADAM8, and ADAM12 useful for high-throughput inhibitor screening: M. L. Moss et al.; Anal. Biochem. 366, 144 (2007), Abstract;
Activity-based probes for the proteomic profiling of metalloproteases: A. Saghatelian, et al.; Proc. Natl. Acad. Sci. USA 101, 10000 (2004), Abstract;
Evidence for disulfide involvement in the regulation of intramolecular autolytic processing by human adamalysin19/ADAM19: T. Kang et al.; Exp. Cell. Res. 298, 285 (2004), Abstract;
Tetrahydroisoquinoline based sulfonamide hydroxamates as potent matrix metalloproteinase inhibitors: D. Ma et al.; Bioorg. Med. Chem. Lett. 14, 47-50 (2004), Abstract;
The structural basis for substrate and inhibitor selectivity of the anthrax lethal factor: B. E. Turk et al.; Nat. Struct. Mol. Biol. 11, 60 (2004), Abstract;
Membrane-anchored CD40 is processed by the tumor necrosis factor-alpha-converting enzyme. Implications for CD40 signaling: C. Contin et al.; J. Biol. Chem. 278, 32801 (2003), Abstract;
The intermediate S1’ pocket of the endometase/matrilysin-2 active site revealed by enzyme inhibition kinetic studies, protein sequence analyses, and homology modeling: H. I. Park et al.; J. Biol. Chem. 278, 51646 (2003), Abstract;
The structure and regulation of the human and mouse matrix metalloproteinase-21 gene and protein: G. N. Marchenko et al.; Biochem. J. 372, 503 (2003), Abstract;
Matrix metalloproteinases contribute to brain damage in experimental pneumococcal meningitis: S. L. Leib; Infect. Immun. 68, 615 (2000), Abstract;
Catalytic activities and substrate specificity of the human membrane type 4 matrix metalloproteinase catalytic domain: Y. Wang et al.; J. Biol. Chem. 274, 33043 (1999), Abstract;
Inhibition of membrane-type 1 matrix metalloproteinase by hydroxamate inhibitors: an examination of the subsite pocket: M. Yamamoto et al.; J. Med. Chem. 41, 1209 (1998), Abstract;
Inhibition of matrix metalloproteinase activity inhibits smooth muscle cell migration but not neointimal thickening after arterial injury: M. P. Bendeck et al.; Circ. Res. 78, 38 (1996), Abstract;
Low molecular weight inhibitors in corneal ulceration: R. E. Galardy et al.; Ann. N. Y. Acad. Sci. 732, 315 (1994), Abstract;
Reversal of experimental autoimmune encephalomyelitis with a hydroxamate inhibitor of matrix metalloproteases: K. Gijbels et al.; J. Clin. Invest. 94, 2177 (1994), Abstract;

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