P2743
Pyruvate Dehydrogenase Phosphatase from bovine kidney
buffered aqueous glycerol solution, ~850 units/mg protein
Product Name
Pyruvate Dehydrogenase Phosphatase from bovine kidney, buffered aqueous glycerol solution, ~850 units/mg protein
form
buffered aqueous glycerol solution
specific activity
~850 units/mg protein
UniProt accession no.
shipped in
dry ice
storage temp.
−70°C
Quality Level
Gene Information
cow ... PPM2C(280891)
Biochem/physiol Actions
Insulin-activated Mg2+-dependent and Ca2+-stimulated mitochondrial protein phosphatase specific for the pyruvate dehydrogenase complex.
Pyruvate dehydrogenase phosphatase catalytic subunit 1 (PDP1) catalyzes a Mg2+,-Ca2+ mediated dephosphorylation and activation of E1. PDP1 plays a crucial role in the regulation of pyruvate dehydrogenase complex (PDC) activity.
General description
Pyruvate dehydrogenase phosphatase (PDP) (EC 3.1.3.43) contains two genetically and biochemically different isoforms, PDP1 and PDP2. PDP1 is widely distributed and is composed of two subunits PDP1c, a catalytic subunit and PDP1r, a flavoprotein with a bound FAD.
Other Notes
One unit will releases 1 nmol of inorganic phosphate from 32P-labeled pyruvate dehydrogenase complex per min at 30 °C, pH 7.0.
Physical form
Solution in 50 μl of 50 mM Tris-HCl, pH 7.0, containing 14 mM β-mercaptoethanol, 1 mM benzamidine, 0.1 mM PMSF, 1 mM EDTA, and 50% glycerol.
signalword
Warning
hcodes
Hazard Classifications
Skin Sens. 1
Storage Class
10 - Combustible liquids
wgk
WGK 2
flash_point_f
Not applicable
flash_point_c
Not applicable
Regulatory Information
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Find documentation for the products that you have recently purchased in the Document Library.
Down?regulation of Pyruvate Dehydrogenase Phosphatase in Obese Subjects is a Defect that Signals Insulin Resistance
Piccinini M, et al.
Obesity Research, 13, 678-686 (2005)
Purification of Bovine Kidney and Heart Pyruvate Dehydrogenaseb Phosphatase on Sepharose Derivatized with the Pyruvate Dehydrogenase Complex
Pratt ML, et al.
European Journal of Biochemistry, 125, 349-355 (1982)
Structural Requirements within the Lipoyl Domain for the Ca2+-dependent Binding and Activation of Pyruvate Dehydrogenase Phosphatase Isoform 1 or Its Catalytic Subunit
Turkan A, et al.
The Journal of Biological Chemistry, 277, 14976-14985 (2002)
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