|Detection of Human PLD1 by Western Blot. Western blot shows lysates of HeLa human cervical epithelial carcinoma cell line, HepG2 human hepatocellular carcinoma cell line, THP‑1 human acute monocytic leukemia cell line, and U937 human histiocytic lymphoma cell line. PVDF membrane was probed with 1 µg/mL of Human PLD1 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF5615) followed by HRP-conjugated Anti-Goat IgG Secondary Antibody (Catalog # HAF109). A specific band was detected for PLD1 at approximately 120 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.|
PLD1 (Phospholipase D1a) is a 110‑120 kDa member of the phospholipase D family of enzymes. It is expressed in endothelial cells and select tissues. Following activation and association with Type I alpha PIPkinase, PLD1 hydrolyzes the phosphodiester bond of membrane phosphatidylcholine, generating phosphatidic acid. Human PLD1 is 1074 amino acids in length). It contains one PX/phox homology domain (aa 84‑206), a pleckstrin homology domain (aa 219‑328), and two phosphodiesterase enzyme regions (aa 459‑486 and 891‑918). There are three splice variants. One shows a 10 aa substitution for aa 962‑1074 (PLD1d), a second shows an 84 aa substitution for aa 514‑1074 (PLD1c), and a third shows an Asn substitution for aa 585‑623 (PLD1b). Caspase cleavage of PLD1a at Gln545‑Ser546 generates a 62 kDa N-terminal, and a 61 kDa C-terminal fragment. Over aa 1‑140, human PLD1a shares 91% aa identity with mouse PLD1a.
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