The MMP-2/MMP-9 Inhibitor I, also referenced under CAS 193807-58-8, controls the biological activity of MMP-2/MMP-9. This small molecule/inhibitor is primarily used for Protease Inhibitors applications.
Sinônimo(s):
MMP-2/MMP-9 Inhibitor I, (2R)-2-[(4-Biphenylylsulfonyl)amino]-3-phenylpropionic Acid
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A potent inhibitor of MMP-2 (IC50 = 310 nM) and MMP-9 (IC50 = 240 nM). Orally active in animal models of tumor growth and metastasis.
A potent inhibitor of MMP-2 (gelatinase A; IC50 = 310 nM) and MMP-9 (gelatinase B; IC50 = 240 nM).
Ações bioquímicas/fisiológicas
Cell permeable: no
Primary Target MMP-2, MMP-9
Product does not compete with ATP.
Reversible: no
Target IC50: 310 nM and 240 nM against MMP-2 and MMP-9
Embalagem
Packaged under inert gas
Advertência
Toxicity: Standard Handling (A)
Reconstituição
Following reconstitution, aliquot and freeze (-20°C). Stock solutions are stable for up to 6 months at -20°C.
Outras notas
Tamura, Y., et al. 1998. J. Med. Chem.41, 640.
Informações legais
CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany
Código de classe de armazenamento
11 - Combustible Solids
Classe de risco de água (WGK)
WGK 1
Ponto de fulgor (°F)
Not applicable
Ponto de fulgor (°C)
Not applicable
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The endothelial glycocalyx is a key component of the glomerular filtration barrier. We have shown that matrix metalloproteinase (MMP)-mediated syndecan 4 shedding is a mechanism of glomerular endothelial glycocalyx damage in vitro, resulting in increased albumin permeability. Here we sought to
Journal of medicinal chemistry, 41(4), 640-649 (1998-03-04)
Various N-sulfonylamino acid derivatives were synthesized and evaluated for their in vitro and in vivo activities to inhibit type IV collagenase (MMP-9 and MMP-2). When the amino acid residue and the sulfonamide moiety were modified, their inhibitory activities were greatly
Chronic inflammatory lung diseases are characterized by disease-specific extracellular matrix accumulation resulting from an imbalance of matrix metalloproteinases (MMPs) and their inhibitors. Zinc is essential for the function of MMPs, and zinc deficiency has been associated with enhanced tissue remodeling.
Select different protease inhibitor types based on your needs to prevent protein degradation during isolation and characterization and safeguard proteins in sample prep.
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