EPyruvate dehydrogenase (PDH) is a mitochondrial multienzyme complex that catalyzes the oxidative decarboxylation of pyruvate and is one of the major enzymes responsible for the regulation of homeostasis of carbohydrate fuels in mammals. The enzymatic activity is regulated by a phosphorylation/dephosphorylation cycle. Phosphorylation of PDH by a specific pyruvate dehydrogenase kinase (PDK) results in inactivation. Multiple alternatively spliced transcript variants have been found for this gene. [provided by RefSeq, Jun 2013].

Q15118;

PDHK1; mitochondrial; [Pyruvate dehydrogenase [lipoamide]] kinase isozyme 1; HGNC:8809; Mitochondrial pyruvate dehydrogenase kinase isoenzyme 1; PDK 1; PDK-1; Pyruvate dehydrogenase kinase isoform 1; Pyruvate dehydrogenase kinase, isoenzyme 1; PDK1_HUMAN;

PDK1 Antibody detects endogenous levels of total PDK1.

Human, Mouse, Rat, Chicken, Dog, Pig, Cow, Horse, Sheep, Rabbit

Rabbit

WB 1:1000-1:2000
IHC 1:50-1:200
IF 1:100-1:400
ICC 1:100-1:400
IP 1:50

 ~45 kD;

Store at -20 °C. Stable for 12 months from date of receipt.

 WB 1:1000-1:2000;   IF/IHC 1:50-1:200;  IP 1:50-1:200;

Western blot analysis of extracts from Lane1: 293T cell lysate, Lane2: Mouse heart and Lane3: Mouse kidney, using PDK1 antibody.