Mouse PDHK4 (His & GST Tag) recombinant protein

Mouse PDHK4 (His & GST Tag) recombinant protein

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Kinase that plays a key role in regulation of glucose and fatty acid metabolism and homeostasis via phosphorylation of the pyruvate dehydrogenase subunits PDHA1 and PDHA2. This inhibits pyruvate dehydrogenase activity, and thereby regulates metabolite flux through the tricarboxylic acid cycle, down-regulates aerobic respiration and inhibits the formation of acetyl-coenzyme A from pyruvate. Inhibition of pyruvate dehydrogenase decreases glucose utilization and increases fat metabolism in response to prolonged fasting and starvation. Plays an important role in maintaining normal blood glucose levels under starvation, and is involved in the insulin signaling cascade. Via its regulation of pyruvate dehydrogenase activity, plays an important role in maintaining normal blood pH and in preventing the accumulation of ketone bodies under starvation. In the fed state, mediates cellular responses to glucose levels and to a high-fat diet. Regulates both fatty acid oxidation and de novo fatty acid biosynthesis. Plays a role in the generation of reactive oxygen species. Protects detached epithelial cells against anoikis. Plays a role in cell proliferation via its role in regulating carbohydrate and fatty acid metabolism.

[Pyruvate dehydrogenase (acetyl-transferring)] kinase isozyme 4, mitochondrial

LIPOAMIDE; MITOCHONDRIAL; PYRUVATE DEHYDROGENASE KINASE; KINASE ISOZYME 4; AV005916; PYRUVATE DEHYDROGENASE KINASE 4; ISOENZYME 4; PDK4; ISOENZYME 4; MITOCHONDRIAL; ISOZYME 4; PYRUVATE DEHYDROGENASE; [PYRUVATE DEHYDROGENASE [LIPOAMIDE]] KINASE ISOZYME 4

O70571

Pdk4

Baculovirus-Insect Cells

A DNA sequence encoding the mouse PDK4 (O70571) (Met1-Val412) was expressed with the N-terminal polyhistidine-tagged GST tag at the N-terminus.

Mouse

The recombinant mouse PDK4/GST chimera consists of 649 amino acids and has a calculated molecular mass of 74.4 kDa. The recombinant protein migrates as an approximately 65 kDa band in SDS-PAGE under reducing conditions.

> 85 % as determined by SDS-PAGE

Kinase activity untested