MW 429.5 Da, Purity >98%. Potent, selective PLD2 inhibitor (IC50 values are 90 and 500 nM for HEK293 and human cells respectively).
Choline phosphatase 1, Choline phosphatase 2, EC 3.1.4.4, PLD1C, PLD1_HUMAN, PLD2_HUMAN, Phosphatidylcholine-hydrolyzing phospholipase D1, Phosphatidylcholine-hydrolyzing phospholipase D2, Phospholipase D1, Phospholipase D2, Pldc, hPLD 2, hPLD1, mPLD2, rPLD2
MW 429.5 Da, Purity >98%. Potent, selective PLD2 inhibitor (IC50 values are 90 and 500 nM for HEK293 and human cells respectively).
Soluble in ethanol to 50 mM.
Soluble in DMSO to 50 mM.
Potent, selective PLD2 inhibitor (IC50 values are 90 and 500 nM for HEK293 and human cells respectively).
Phospholipase D1 (PLD1) and Phospholipase D2 (PLD2) are enzymes that hydrolyze phosphatidylcholine to produce phosphatidic acid and choline. PLD1 and PLD2 are isoforms with significant roles in cellular functions. PLD1 has a molecular mass of approximately 120 kDa and is widely expressed in various tissues including the brain liver and heart. Alternate names for PLD1 include PLD1A and hPLD1. PLD2 similar in structure shares overlapping functions with PLD1. Both isoforms are localized in cellular membranes where they perform their enzymatic activity.
PLD enzymes participate in signal transduction and membrane trafficking. PLD1 and PLD2 play roles in vesicle transport cytoskeletal organization and cellular proliferation. They are not typically part of large multiprotein complexes however they associate with other proteins like protein kinase C and small GTPases during signal transduction. By influencing intracellular pathways PLD1 and PLD2 contribute to diverse physiological processes.
PLD1 and PLD2 are key players in the phosphatidylinositol signaling system and the mTOR pathway. Within the phosphatidylinositol signaling system PLD1 and PLD2 work with proteins like phosphatidylinositol 3-kinase (PI3K) helping regulate cell survival and growth. In the mTOR pathway which connects nutrient availability to cellular growth these enzymes interact with mTOR complexes affecting protein synthesis and autophagy.
PLD1 and PLD2 have implications in cancer and neurological disorders. In cancer upregulation of PLD enzymes associates with tumorigenesis and metastasis potentially through interactions with proteins like Ras and Rho GTPases. In neurological disorders aberrant PLD activity links to Alzheimer's disease where PLD enzymes may interact with amyloid precursor protein influencing amyloid-beta production. Understanding PLD1 and PLD2 functions offers insights into therapeutic strategies for these conditions.
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2D chemical structure image of ab145226, BML 280, PLD2 inhibitor
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