Anti-PDP1/PDP Antibody Picoband® (Dylight488 Conjugate)

Pyruvate dehydrogenase (E1) is one of the three components (E1, E2, and E3) of the large pyruvate dehydrogenase complex. Pyruvate dehydrogenase kinases catalyze phosphorylation of serine residues of E1 to inactivate the E1 component and inhibit the complex. Pyruvate dehydrogenase phosphatases catalyze the dephosphorylation and activation of the E1 component to reverse the effects of pyruvate dehydrogenase kinases. Pyruvate dehydrogenase phosphatase is a heterodimer consisting of catalytic and regulatory subunits. Two catalytic subunits have been reported; one is predominantly expressed in skeletal muscle and another one is is much more abundant in the liver. The catalytic subunit, encoded by this gene, is the former, and belongs to the protein phosphatase 2C (PP2C) superfamily. Along with the pyruvate dehydrogenase complex and pyruvate dehydrogenase kinases, this enzyme is located in the mitochondrial matrix. Mutation in this gene causes pyruvate dehydrogenase phosphatase deficiency. Multiple alternatively spliced transcript variants encoding different isoforms have been identified.

Expressed in heart, placenta, skeletal muscle kidney, pancreas, spleen, prostate, testis, ovary, ileum and colon. Expressed in lung endothelial and smooth muscle cells (at protein level).

Catalyzes the first step in the biosynthesis of coenzyme A from vitamin B5, where cysteine is conjugated to 4'-phosphopantothenate to form 4-phosphopantothenoylcysteine.

At -20℃ for one year from date of receipt. After reconstitution, at 4℃ for one month. It can also be aliquotted and stored frozen at -20℃ for six months. Avoid repeated freezing and thawing.

Western blot, 0.25-0.5 μg/ml, Human, Mouse, Rat<br> Immunocytochemistry/Immunofluorescence, 5 μg/ml, Human<br> Flow Cytometry (Fixed), 1-3 μg/1x10⁶ cells, Human<br> ELISA, 0.1-0.5 μg/ml, -<br>