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CA-074 Me

Cathepsin inhibitor
 
BML-PI126-0001 1 mg 107.00 USD
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Potent and selective irreversible cell permeable cathepsin B inhibitor. Methyl ester (Me) is hydrolyzed by intracellular esterases releasing the active inhibitor. Prevents death of CA1 neurons after ischemia following IV delivery after the ischemic insult. In isolated rat osteoclasts it inhibited bone resorption with a maximal effect at 50 µM. This product is only suitable for in vivo and whole cell experiments. The free acid form must be used for in vitro experiments. Can be used to discriminate between cathepsin B and L/S forms.

Product Specification

Alternative Name:N-(L-3-trans-Propylcarbonyl-oxirane-2-carbonyl)-L-isoleucyl-L-proline methyl ester
 
Sequence:N-(L-3-trans-Propylcarbonyl-oxirane-2-carbonyl)-L-isoleucyl-L-proline methyl ester
 
Formula:C19H31N3O6
 
MW:397.5
 
Purity:≥99% (TLC)
 
Appearance:White solid.
 
Solubility:Soluble in DMSO.
 
Shipping:Shipped on Blue Ice
 
Long Term Storage:-20°C
 
BML-PI126 structure
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BML-PI126 structure

Product Literature References

Neutrophil and Alveolar Macrophage-Mediated Innate Immune Control of Legionella pneumophila Lung Infection via TNF and ROS: P. Ziltener, et al.; PLoS One 12, e1005591 (2016), Application(s): Cell culture, Abstract; Full Text
ATG16L1 deficiency in macrophages drives clearance of uropathogenic E. coli in an IL-1β-dependent manner: J.W. Symington, et al.; Mucosal Immunol. 8, 1388 (2015), Application(s): Cell Culture, ELISA, Abstract;
Synthesis of marmycin A and investigation into its cellular activity: T. Cañeque, et al.; Nat. Chem. 7, 744 (2015), Application(s): Cell Culture, Abstract;
An intracellular form of cathepsin B contributes to invasiveness in cancer: A, M. Szpaderska et al.; Cancer Res. 61, 3493 (2001), Abstract;
Fluorometric microassays for the determination of cathepsin L and cathepsin S activities in tissue extracts: B. Werle et al.; Biol. Chem. 380, 1109 (1999), Abstract;
Postictal blockade of ischemic hippocampal neuronal death in primates using selective cathepsin inhibitors: K. Tsuchiya et al.; Exp. Neurol. 155, 187 (1999), Abstract;
Inhibition of bone resorption by selective inactivators of cysteine proteinases: P. A. Hill et al.; J. Cell. Biochem. 56, 118 (1994), Abstract;

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