Pyruvate dehydrogenase phosphatase (PDP) is a serine phosphatase that catalyzes the dephosphorylation and reactivation of the alpha subunit of the E1 component of the mitochondrial pyruvate dehydrogenase multienzyme complex. PDP is a heterodimer that consists of catalytic and regulatory subunits. PDPc (pyruvate dehydrogenase phosphatase, catalytic subunit 1), also known as Protein phosphatase 2C, is a 537 amino acid protein that is localized within the mitochondrial matrix. PDPc is stimulated by calcium binding and utilizes two magnesium ions as cofactors. PDPc efficiently dephosphorylates all three phosphorylation sites located on the alpha chain of the E1 component, which simultaneously activates pyruvate dehydrogenase to convert pyruvate to acetyl-CoA for utilization in the Krebs Cycle. Defects in the gene encoding PDPc are the cause of pyruvate dehydrogenase phosphatase deficiency, which results in lactic acidosis and neurological dysfunction.
The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE).
Form:
Rabbit IgG, 1mg/ml in PBS with 0.02% sodium azide, 50% glycerol, pH7.2
Application Dilute:
WB: 1:500~1:1000
Application Notes:
PDP1 polyclonal antibody detects endogenous levels of PDP1 protein.
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