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Manufactured by BioVendor

6-phosphogluconate dehydrogenase, decarboxylating Human E. coli

  • Regulatory status:RUO
  • Type:Recombinant protein
  • Source:E. coli
  • Other names:6PGDH, PGD, PGDH
  • Species:Human
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Cat. No. Size Price

RD172410100 0.1 mg
PubMed Product Details
Technical Data


Recombinant protein


Total 492 AA. MW: 54.2 kDa (calculated). UniProtKB P52209 (Ala2-Ala483). N-terminal His-tag (10 extra AA). Protein identity confirmed by LC-MS/MS.

Amino Acid Sequence



E. coli


Purity as determined by densitometric image analysis: > 95%


14 % SDS-PAGE separation of Human PGDH (E.coli):
1. M.W. marker – 14, 21, 31, 45, 66, 97 kDa
2. reduced and boiled sample, 2.5 μg/lane
3. non-reduced and non-boiled sample, 2.5 μg/lane


< 1.0 EU/ug


Filtered (0.4 μm) and lyophilized in phosphate buffered saline + 5 % (w/v) trehalose.


Add 200 µl of deionized water to prepare a working stock solution of approximately 0.5 mg/ml and let the lyophilized pellet dissolve completely. Filter sterilize your culture media/working solutions containing this non-sterile product before using in cell culture.


Western blotting, ELISA


At ambient temperature. Upon receipt, store the product at the temperature recommended below.


Store the lyophilized protein at –80 °C. Lyophilized protein remains stable until the expiry date when stored at –80 °C. Aliquot reconstituted protein to avoid repeated freezing/thawing cycles and store at –80 °C for long term storage. Reconstituted protein can be stored at 4 °C for a week.

Quality Control Test

BCA to determine quantity of the protein.

SDS PAGE to determine purity of the protein.

LAL to determine quantity of endotoxin.


This product is intended for research use only.


Research topic

Cardiovascular disease, Oncology


6-Phosphogluconate dehydrogenase (6PGDH) is a homodimeric protein with the molecular weight of each subunit being 51 kDa. Its sequence is highly conserved among species. The enzyme belongs to the class of pyridine nucleotide linked oxidative decarboxylases. This class of enzymes generally utilizes one of the pyridine nucleotides NAD+ or NADP+ as a cofactor to catalyze oxidative decarboxylation of a β-hydroxy acid, yielding a ketone and CO2 . 6-Phosphogluconate dehydrogenase catalyzes reversible oxidative decarboxylation of 6 phosphogluconate to ribulose 5-phosphate and CO2 in the presence of NADP+ and the generation of its reduced form NADPH. This reaction is the third step of the pentose phosphate pathways (PPP), which is an alternative to glycolysis. The pentose phosphate pathway is primarily an anabolic pathway that utilizes glucose-6-phosphate to generate five carbon sugars and a NADPH. The PPP is an important source of NADPH for reductive biosynthesis reactions within cells such as fatty acid or steroid biosynthesis and also, a source of ribose-5-phosphate required for the synthesis of the nucleotides and nucleic acids. The first three reactions of the PPP are referred to as the oxidative and yield NADPH. The non-oxidative reactions of PPP are primarily designed to generate ribose-5-phosphate or to convert excess five-carbon sugars into intermediates of the glycolytic pathway. Although the PPP operates in all cells, high levels of PPP enzymes are found in cells of liver, adipose tissue, adrenal cortex, testis and lactating mammary gland, and the highest levels were detected in neutrophils and macrophages. Pentose phosphate pathways are considered important in tumor proliferation processes because of their role in supplying tumor cells with NADPH and carbons for intracellular anabolic processes. Flux measurements showed that PPP can be elevated by almost 8-fold in breast cancer cells compared to normal mammary epithelial cells. Recent study indicates that knockdown of 6-phosphogluconate dehydrogenase inhibits growth of lung cancer cells by senescence induction. This inhibition is not due to a defect in the oxidative PPP per se. Presumably, some of the glucose metabolites accumulated in 6PGD knockdown may be growth inhibitory and, therefore, 6PGDH inhibition may provide a novel strategy to treat glycolytic tumors such as lung cancer. Mutations within the gene encoding for this enzyme result in 6-phosphogluconate dehydrogenase deficiency, a rare autosomal hereditary disease affecting the red blood cells.

Summary References (6)

References to 6-Phosphogluconate dehydrogenase, decarboxylating

  • Boros LG, Lee PW, Brandes JL, Cascante M, Muscarella P, Schirmer WJ, Melvin WS, Ellison EC. Nonoxidative pentose phosphate pathways and their direct role in ribose synthesis in tumors: is cancer a disease of cellular glucose metabolism?. Med Hypotheses. 1998 Jan;50 (1):55-9
  • Hanau S, Montin K, Cervellati C, Magnani M, Dallocchio F. 6-Phosphogluconate dehydrogenase mechanism: evidence for allosteric modulation by substrate. J Biol Chem. 2010 Jul 9;285 (28):21366-71
  • Kindzelskii AL, Ueki T, Michibata H, Chaiworapongsa T, Romero R, Petty HR. 6-phosphogluconate dehydrogenase and glucose-6-phosphate dehydrogenase form a supramolecular complex in human neutrophils that undergoes retrograde trafficking during pregnancy. J Immunol. 2004 May 15;172 (10):6373-81
  • Meadows AL, Kong B, Berdichevsky M, Roy S, Rosiva R, Blanch HW, Clark DS. Metabolic and morphological differences between rapidly proliferating cancerous and normal breast epithelial cells. Biotechnol Prog. 2008 Mar-Apr;24 (2):334-41
  • Ozcicek F, Aktas M, Turkmen K, Coban TA, Cankaya M. The investigation of plasma glucose-6-phosphate dehydrogenase, 6-phoshogluconate dehydrogenase, glutathione reductase in premenauposal patients with iron deficiency anemia. Pak J Med Sci. 2014 Jul;30 (4):809-913
  • Sukhatme VP, Chan B. Glycolytic cancer cells lacking 6-phosphogluconate dehydrogenase metabolize glucose to induce senescence. FEBS Lett. 2012 Jul 30;586 (16):2389-95
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