Phospho-PLD1 (Ser561) Antibody selectively recognizes PLD1 phosphorylated at Ser561 and does not cross-react with phosphorylated PLD2 isoforms . Key validation data include:
This antibody is validated for multiple experimental techniques, with optimized dilution ranges:
Phosphorylation of PLD1 at Ser561 is a key regulatory mechanism:
PKC-Mediated Regulation: Protein kinase C (PKC) phosphorylates PLD1 at Ser561, Thr147, and Ser2, modulating its enzymatic activity . Phosphorylation at Ser561 and Thr147 enhances PLD1’s role in signal transduction pathways .
Functional Impact: This modification influences PLD1’s interaction with downstream effectors, such as ADP-ribosylation factor (Arf) GTPases, to regulate vesicular trafficking and lipid metabolism .
Cellular Context: Phospho-PLD1 activity is upregulated during stress conditions, contributing to autophagy and tumorigenesis .
Key studies leveraging this antibody have revealed:
Kinetic Modulation: PKC increases PLD1’s substrate binding affinity (K<sub>m</sub>) and catalytic efficiency (k<sub>cat</sub>) through interactions at N- and C-terminal domains .
Downstream Signaling: Phospho-PLD1-generated phosphatidic acid (PtdOH) activates mTOR and Akt kinases, linking PLD1 to metabolic regulation .
Pathophysiological Roles: Elevated PLD1 phosphorylation is observed in cancer models, suggesting therapeutic targeting potential .