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Inhibitor of TNF-α processing
BML-PI135-0001 1 mg 289.00 USD
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Inhibitor of TACE, other ADAMs, ACE secretase and other metalloproteinases. Blocks release of TNFα, TGF-α, DCC, APP, L-selectin, ACE, IL6R, NOTCH, and erbB2/HER2. Has been used in culture (typical concentration 5-100µM).

Product Specification

Alternative Name:IC3, N-(R)-(2-(Hydroxyaminocarbonyl)methyl)-4-methylpentanoyl-L-t-butyl-glycine-L-alanine 2-aminoethyl amide
N-(R)-(2-(Hydroxyaminocarbonyl)methyl)-4-methylpentanoyl-L-t-butyl-glycine-L-alanine 2-aminoethyl amide
Purity:≥99% (HPLC)
Appearance:Lyophilized solid.
Solubility:Soluble in water (at least 20mM) or 100% ethanol (at least 5mg/ml)
Shipping:Shipped on Blue Ice
Long Term Storage:-20°C
BML-PI135 structure
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BML-PI135 structure

Product Literature References

Angiotensin II induced proteolytic cleavage of myocardial ACE2 is mediated by TACE/ADAM-17: a positive feedback mechanism in the RAS: V.B. Patel, et al.; J. Mol. Cell. Cardiol. 66, 167 (2014), Abstract;
Elevated serum CXCL16 is an independent predictor of poor survival in ovarian cancer and may reflect pro-metastatic ADAM protease activity: M.J. Gooden, et al.; Br. J. Cancer 110, 1535 (2014), Abstract;
IL-7 and IL-15 instruct the generation of human memory stem T cells from naive precursors: N. Cieri, et al.; Blood 121, 573 (2013), Abstract; Full Text
Neutrophil apoptosis is associated with loss of signal regulatory protein alpha (SIRPα) from the cell surface: A. Stenberg, et al.; J. Leukoc. Biol. 93, 403 (2013), Abstract;
TWEAK transactivation of the epidermal growth factor receptor mediates renal inflammation: S. Rayego-Mateos, et al.; J. Pathol. 231, 480 (2013), Abstract;
Paracrine regulation of growth factor signaling by shed leucine-rich repeats and immunoglobulin-like domains 1: W. Yi, et al.; Exp. Cell. Res. 317, 504 (2011), Abstract;
Epidermal growth factor and perlecan fragments produced by apoptotic endothelial cells co-ordinately activate ERK1/2-dependent antiapoptotic pathways in mesenchymal stem cells: M. Soulez, et al.; Stem Cells 28, 810 (2010), Abstract; Full Text
TGFβ induces proHB-EGF shedding and EGFR transactivation through ADAM activation in gastric cancer cells: M. Ebi, et al.; Biochem. Biophys. Res. Commun. 402, 449 (2010), 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;
Transmembrane collagen XVII, an epithelial adhesion protein, is shed from the cell surface by ADAMs: C.W. Franzke, et al.; EMBO J. 21, 5026 (2002), Abstract;
A novel proteolytic cleavage involved in Notch signaling: the role of the disintegrin-metalloprotease TACE: C. Brou, et al.; Mol. Cell 5, 207 (2000), Abstract;
Function of an axonal chemoattractant modulated by metalloprotease activity: M. J. Galko, et al.; Science 289, 1365 (2000), Abstract;
Cleavage of the HER2 ectodomain is a pervanadate-activable process that is inhibited by the tissue inhibitor of metalloproteases-1 in breast cancer : J. Codony-Servat, et al.; Cancer Res. 59, 1196 (1999), Abstract;
Unaltered cleavage and secretion of angiotensin-converting enzyme in tumor necrosis factor-alpha-converting enzyme-deficient mice: R. Sadhukhan, et al.; J. Biol. Chem. 274, 10511 (1999), Abstract;
Crystal structure of the catalytic domain of human tumor necrosis factor-alpha-converting enzyme: K. Maskos, et al.; PNAS 95, 3408 (1998), Abstract;
Evidence that tumor necrosis factor alpha converting enzyme is involved in regulated alpha-secretase cleavage of the Alzheimer amyloid protein precursor: J. D. Buxaum, et al.; J. Biol. Chem. 273, 27765 (1998), Abstract;
TNFalpha processing enzyme inhibitors prevent aspirin-induced TNFalpha release and protect against gastric mucosal injury in rats: S. Fioruci, et al.; Aliment. Pharmacol. Ther. 12, 1139 (1998), Abstract;
A metalloproteinase disintegrin that releases tumour-necrosis factor-alpha from cells: R. A. Black, et al.; Nature 385, 729 (1997), Abstract;
Angiotensin-converting enzyme secretase is inhibited by zinc metalloprotease inhibitors and requires its substrate to be inserted in a lipid bilayer: S. Parvathy, et al.; Biochem. J. 327, 37 (1997), Abstract;
Diverse cell surface protein ectodomains are shed by a system sensitive to metalloprotease inhibitors: J. Arribas, et al.; J. Biol. Chem. 271, 11376 (1996), Abstract;

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