|Detection of Human Pyruvate Dehydrogenase Phosphatase/PDP1 by Western Blot. Western blot shows lysates of SW13 human adrenal cortex adenocarcinoma cell line and IMR‑32 human neuroblastoma cell line. PVDF membrane was probed with 1 µg/mL of Sheep Anti-Human Pyruvate Dehydrogenase Phosphatase/PDP1 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF7260) followed by HRP-conjugated Anti-Sheep IgG Secondary Antibody (Catalog # HAF016). A specific band was detected for Pyruvate Dehydrogenase Phosphatase/PDP1 at approximately 53 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.|
PPM2C (Protein phosphatase mitochondrial 2C; also PDP1) is a 52-54 kDa member of the PP2C family of enzymes. It is expressed in skeletal muscle and adipocytes, and represents one of two subunits that comprise PDP (pyruvate dehydrogenase phosphatase). PPMC2 is found within the mitochondrial matrix space where, as part of PDP, it dephosphorylates the E1 component of the pyruvate dehydrogenase complex, resulting in its activation, and the downstream generation of acetyl-CoA and NADH from pyruvate. Human PPM2C is 537 amino acids (aa) in length. It contains a mitochondrion targeting sequence (aa 1-71), followed by a mature region that possesses a catalytic domain between aa 109-440. There are three potential isoform variants. Two contain alternative start sites 25 and 59 aa upstream of the standard start site, respectively. A third shows a 12 aa substitution for aa 105-116. Over aa 72-537, human PPM2C shares 99% aa identity with mouse PPM2C.
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