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MAK183

Sigma-Aldrich

PDH Activity Assay Kit

Sufficient for 100 Colorimetric tests

Synonym(s):

Pyruvate Dehydrogenase Activity Assay Kit

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About This Item

UNSPSC Code:
12161503
NACRES:
NA.84

usage

sufficient for 100 colorimetric tests

detection method

colorimetric

relevant disease(s)

neurological disorders; cancer

storage temp.

−20°C

General description

Pyruvate dehydrogenase (PDH) is a mitochondrial enzyme that catalyzes the conversion of pyruvate to acetyl-CoA and CO2, and also links the tricarboxylic acid (TCA) and glycolysis pathways. The enzyme is inhibited by phosphorylation and activated by dephosphorylation. Mutations in PDH have been linked to pyruvate dehydrogenase deficiency (causing lactic acidosis and neurologic dysfunctions) and Leigh syndrome. PDH has also been implicated in oncogene-induced senescence. PDH measurements can provide insights into metabolic functions and oncogenesis.

Application

PDH Activity Assay Kit has been used to determine the activity of pyruvate dehydrogenase.

Suitability

Suitable for the detection of PDH activity in a variety of biological samples such as cell and tissue culture supernatants and purified mitochondria.

Principle

Pyruvate dehydrogenase activity is determined using a coupled enzyme reaction, which results in a colorimetric (450 nm) product proportional to the enzymatic activity present. One unit of pyruvate dehydrogenase is the amount of enzyme that will generate 1.0 mmole of NADH per minute at 37 °C.

Kit Components Only

Product No.
Description

  • PDH Assay Buffer

  • PDH Substrate

  • PDH Developer

  • NADH Standard

  • PDH Positive Control

Pictograms

CorrosionExclamation mark

Signal Word

Danger

Hazard Statements

Hazard Classifications

Eye Dam. 1 - Skin Corr. 1B - Skin Sens. 1

Storage Class Code

8A - Combustible, corrosive hazardous materials

WGK

WGK 3


Certificates of Analysis (COA)

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The Citric Acid Cycle Oxidizes Two-Carbon Units
Berg J M, et al.
Biochemistry (2002)
Minfeng Ying et al.
The Journal of biological chemistry, 294(24), 9615-9630 (2019-05-02)
Whether growing cancer cells prefer lactate as a fuel over glucose or vice versa is an important but controversial issue. Labeling of tricarboxylic acid (TCA) cycle intermediates with glucose or lactate isotope tracers is often used to report the relative
Ryan M Bradley et al.
Biochimica et biophysica acta. Molecular and cell biology of lipids, 1863(7), 700-711 (2018-04-09)
Lysophosphatidic acid acyltransferase (LPAAT) δ/acylglycerophosphate acyltransferase 4 is a mitochondrial enzyme and one of five homologues that catalyze the acyl-CoA-dependent synthesis of phosphatidic acid (PA) from lysophosphatidic acid. We studied skeletal muscle LPAATδ and found highest levels in soleus, a
Pyruvate as a pivot point for oncogene-induced senescence.
Olenchock B A and Matthew G V H
Cell, 153(7), 1429-1430 (2013)
The spectrum of pyruvate dehydrogenase complex deficiency: clinical, biochemical and genetic features in 371 patients.
Patel K P, et al.
Molecular Genetics and Metabolism, 106(3), 385-394 (2012)

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