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444241

Sigma-Aldrich

MMP-2/MMP-9 Inhibitor I

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.

Sinónimos:

MMP-2/MMP-9 Inhibitor I, (2R)-2-[(4-Biphenylylsulfonyl)amino]-3-phenylpropionic Acid

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About This Item

Fórmula empírica (notación de Hill):
C21H19NO4S
Número de CAS:
193807-58-8
Peso molecular:
381.44
UNSPSC Code:
12352200
NACRES:
NA.77

Quality Level

100

assay

≥95% (HPLC)

form

solid

manufacturer/tradename

Calbiochem®

storage condition

OK to freeze

color

white

solubility

DMSO: 200 mg/mL

shipped in

ambient

storage temp.

−20°C

General description

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).

Biochem/physiol Actions

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

Packaging

Packaged under inert gas

Warning

Toxicity: Standard Handling (A)

Reconstitution

Following reconstitution, aliquot and freeze (-20°C). Stock solutions are stable for up to 6 months at -20°C.

Other Notes

Tamura, Y., et al. 1998. J. Med. Chem.41, 640.

Legal Information

CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany

Storage Class

11 - Combustible Solids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

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Y Tamura et al.
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
Raina D Ramnath et al.
Kidney international, 97(5), 951-965 (2020-02-11)
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
Michael Roth et al.
Biomedicines, 12(6) (2024-06-27)
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.

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