IPA 

IPA is a specific Sec18/NSF inhibitor. IPA binds to phosphatidic acid competitively, induces conformational rigidification of Sec18/NSF, disrupts its essential flexibility, and blocks SNARE priming and vacuolar membrane fusion. IPA can be used to investigate the activity of Sec18 and SNARE priming kinetics^[1].

IPA binds to purified monomeric Saccharomyces cerevisiae Sec18, as well as isolated Sec18 D1, D2 domains and D1-D2 recombinants, with the D1 domain showing the highest binding affinity (IC₅₀=762 nM (Sec18), 220 nM (D1), 641 nM (D2))^[1].
IPA potently and specifically competes with phosphatidic acid for binding to monomeric Saccharomyces cerevisiae Sec18 and its isolated D1 and D2 domains, but exerts no significant inhibitory effect on the binding of phosphatidic acid to other phosphatidic acid-interacting proteins, or on the binding of Sec18 to PI liposomes^[1].
IPA (100 μM) potently inhibits the binding of monomeric Saccharomyces cerevisiae Sec18 to PA liposomes with different membrane curvatures, and exhibits slightly stronger inhibitory effects on liposomes with larger diameters^[1].

MedChemExpress (MCE) has not independently confirmed the accuracy of these methods. They are for reference only.

394.38

C₂₂H₁₈O₇

200348-48-7

O=C(O)C1C2C=CC(C1C3=C4C=CC(=O)C(O)=C4OC=5C(O)=C(O)C=CC53)C2C

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Please store the product under the recommended conditions in the Certificate of Analysis.

• [1]. Sparks RP, et al. A small-molecule competitive inhibitor of phosphatidic acid binding by the AAA+ protein NSF/Sec18 blocks the SNARE-priming stage of vacuole fusion. J Biol Chem. 2019;294(46):17168-17185.  [Content Brief]