VU0359595

VU0359595

CAT N°: 10955
Price:

From 60.00 51.00

Phospholipase D (PLD) is an enzyme that cleaves the head group from phospholipids, producing the second messenger phosphatidic acid. Two mammalian isoforms of PLD, PLD1, and PLD2, have been identified, with multiple splice variants of each. Although the two isoforms share structural and functional features, they are regulated differently and apparently subserve distinct roles. VU0359595 is an inhibitor of PLD1 (IC50 = 3.7 nM) that is >1,700-fold selective over PLD2 (IC50 = 6.4 ?M).{24567} Preliminary evidence suggests that VU0359595 does not interact with the catalytic site of PLD, but instead may bind and inhibit PLD through an allosteric site.{24567}

Territorial Availability: Available through Bertin Technologies only in France

  • Synonyms
    • (1R,2R)-N-[(1S)-2-[4-(5-bromo-2,3-dihydro-2-oxo-1H-benzimidazol-1-yl)-1-piperidinyl]-1-methylethyl]-2-phenyl-cyclopropanecarboxamide; (1S,2S)-N-[(1S)-2-[4-(5-bromo-2,3-dihydro-2-oxo-1H-benzimidazol-1-yl)-1-piperidinyl]-1-methylethyl]-2-phenyl-cyclopropanecarboxamide
  • Correlated keywords
    • 1246303-14-9 1257404-85-5 molecular library initiative agonists CID-53361951 CID53361951 CIDs 53361951 ML270 MLs 270 ML-270 PLD1 phophoslipases D inhibitors PLDs PLD-1 VUs 0359595 VU-0359595 inhibits inhibitions PLs phosphatidic acids isoforms binds binding binders allosteric sitesselective cell biology intracellular signaling transductions
  • Product Overview:
    Phospholipase D (PLD) is an enzyme that cleaves the head group from phospholipids, producing the second messenger phosphatidic acid. Two mammalian isoforms of PLD, PLD1, and PLD2, have been identified, with multiple splice variants of each. Although the two isoforms share structural and functional features, they are regulated differently and apparently subserve distinct roles. VU0359595 is an inhibitor of PLD1 (IC50 = 3.7 nM) that is >1,700-fold selective over PLD2 (IC50 = 6.4 ?M).{24567} Preliminary evidence suggests that VU0359595 does not interact with the catalytic site of PLD, but instead may bind and inhibit PLD through an allosteric site.{24567}

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