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SRP5250

Sigma-Aldrich

PDHK4, active, GST tagged human

PRECISIO® Kinase, recombinant, expressed in baculovirus infected Sf9 cells, ≥70% (SDS-PAGE), buffered aqueous glycerol solution

Synonym(s):

FLJ40832, PDK4

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About This Item

UNSPSC Code:
12352200
NACRES:
NA.32

biological source

human

recombinant

expressed in baculovirus infected Sf9 cells

product line

PRECISIO® Kinase

Assay

≥70% (SDS-PAGE)

form

buffered aqueous glycerol solution

specific activity

17-23 nmol/min·mg

mol wt

~71 kDa

NCBI accession no.

NM_002612

application(s)

cell analysis

shipped in

dry ice

storage temp.

−70°C

Gene Information

human ... PDK4(5166)

Biochem/physiol Actions

PDHK4 or Pyruvate Dehydrogenase Kinase 4 is a member of the PDHK family that phosphorylate and inactivate the Pyruvate Dehydrogenase (PDH). 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. PDHK4 upregulation in adipocytes participates in the hypolipidemic effect of thiazolidinediones through modulation of glyceroneogenesis. PDHK4 expression is strongly and selectively induced by Rosiglitazone in a direct and transcriptional manner.

Physical form

Supplied in 50mM Tris-HCl, pH 7.5, 150mM NaCl, 10mM glutathione, 0.1mM EDTA, 0.25mM DTT, 0.1mM PMSF, 25% glycerol.

Preparation Note

after opening, aliquot into smaller quantities and store at -70 °C. Avoid repeating handling and multiple freeze/thaw cycles

Legal Information

PRECISIO is a registered trademark of Merck KGaA, Darmstadt, Germany

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Regulatory Information

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Thomas Cadoudal et al.
Diabetes, 57(9), 2272-2279 (2008-06-04)
Pyruvate dehydrogenase complex (PDC) serves as the metabolic switch between glucose and fatty acid utilization. PDC activity is inhibited by PDC kinase (PDK). PDC shares the same substrate, i.e., pyruvate, as glyceroneogenesis, a pathway controlling fatty acid release from white
R Gudi et al.
The Journal of biological chemistry, 270(48), 28989-28994 (1995-12-01)
Recent evidence from this laboratory indicates that at least two isoenzymic forms of pyruvate dehydrogenase kinase (PDK1 and PDK2) may be involved in the regulation of enzymatic activity of mammalian pyruvate dehydrogenase complex by phosphorylation (Popov, K.M., Kedishvili, N.Y., Zhao

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