Technical Data
PDK-1 (Pyruvate Dehydrogenase Kinase-1, PDHK1)
Pyruvate dehydrogenase kinase 1 (PDK1), a 48kD member of
the mitochondrial matrix protein kinase family, is related to the
histidine protein kinases found in prokaryotes. A mitochondrial multiple subunit enzyme, pyruvate dehydrogenase (PDH) catalyses the oxidative decarboxylation of pyruvic acid to generate acetyl-CoA, NADH, and CO2. This reaction is central to the homeostasis of carbohydrate fuels in mammals. Along with three other isoforms, PDK1 is responsible for phosphorylation and concomitant inactivation of PDH, the E1 component of the multi-enzyme pyruvate dehydrogenase complex. Phosphorylation of PDH by PDK1 occurs at three serine residues on the E1 alpha subunits: Ser264, Ser271, and Ser203. In vitro studies indicate that PDK1 is the only isoenzyme able to phosphorylate Ser203 of PDH, while PDK2 and PDK3 exhibit the strongest activity toward Ser264 and Ser271, respectively. Northern blot analysis reveals that PDK1 is predominantly expressed in heart tissue.

Suitable for use in Western Blot and Immunohistochemistry. Other applications not tested.

Recommended Dilutions:
Western Blot (ECL): 1:1000
Immunohistochemistry (Paraffin): 10ug/ml
Optimal dilutions to be determined by researcher.

Storage and Stability:
May be stored at 4C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20C. Aliquots are stable for 12 months after receipt. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
PabIgGAffinity Purified
50ug-20CBlue IceHumanRabbit
Synthetic peptide corresponding to a sequence from human PDK-1, conjugated to KLH (Q15118).
Purified by Protein A affinity chromatography.
Supplied as a liquid in PBS, 0.09% sodium azide, 50% glycerol.
Recognizes human PDK-1 at ~48kD. Species Crossreactivity: mouse, rat, canine, monkey, porcine and rabbit
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.
1. Gudi, R., et al. (1995) J Biol Chem. 270, 28989-28994. 2. Harris, R.A., et al. (1995) Adv Enzyme Regul. 35, 147-162. 3. Harris, R.A., et al. (2002) Adv Enzyme Regul. 42, 249-259. 4. Korotchkina, L.G. and Patel, M.S. (2001) J Biol Chem. 40, 37223-37229.