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SRP5248

Sigma-Aldrich

PDHK2, active, GST tagged human

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

Synonym(s):

PDK2

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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

6.4-8.6 nmol/min·mg

mol wt

~70 kDa

NCBI accession no.

NM_002611

application(s)

cell analysis

shipped in

dry ice

storage temp.

−70°C

Gene Information

human ... PDK2(5164)

Biochem/physiol Actions

PDHK2 or Pyruvate Dehydrogenase Kinase 2 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. PDHK2 is a primary PPARbeta/delta target gene in humans which underlines the importance of PPAR in the control of metabolism. There are two candidate PPAR response elements in the PDHK2 gene.

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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Tatjana Degenhardt et al.
Journal of molecular biology, 372(2), 341-355 (2007-08-03)
The nuclear receptors peroxisome proliferator-activated receptors (PPARs) are known for their critical role in the metabolic syndrome. Here, we show that they are direct regulators of the family of pyruvate dehydrogenase kinase (PDK) genes, whose products act as metabolic homeostats
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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