PGD Human, Active
Escherichia Coli.
EC 1.1.1.44, 6PGD, PGDH, 6-phosphogluconate dehydrogenase decarboxylating, PGD.
Greater than 90.0% as determined by SDS-PAGE.
Description
PGD Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 503 amino acids (1-483) and having a molecular mass of 55.3 kDa.
PGD Human is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Product Specs
6PGD is the second dehydrogenase in the pentose phosphate pathway. Pentose is essential for the biosynthesis of nucleic acid. The pentose phosphate pathway is a major source of NADPH. 6PGD deficiency is usually asymptomatic, and this condition is inherited in an autosomal dominant manner. PGD deficiency increases erythrocyte pyruvate kinase activity levels and reduces glutathione synthetase, leading to hemolysis.
PGD Human Recombinant, produced in E. coli, is a single, non-glycosylated polypeptide chain containing 503 amino acids (1-483) and has a molecular weight of 55.3 kDa.
PGD Human is fused to a 20 amino acid His-Tag at the N-terminus and purified using proprietary chromatographic techniques.
The PGD solution (1mg/ml) is supplied with 10% Glycerol, 1mM DTT, 0.1M NaCl, and 20mM Tris-HCl buffer (pH 8.0).
Adding a carrier protein (0.1% HSA or BSA) is recommended for long-term storage.
Avoid repeated freeze-thaw cycles.
Greater than 90.0% as determined by SDS-PAGE.
Specific activity is greater than 10 units/mg. One unit is defined as the amount of enzyme that will oxidize 1.0 µmole of 6-phospho-D-gluconate to D-ribulose 5-phosphate per minute at pH 8.0 at 25°C in the presence of beta-NADP.
EC 1.1.1.44, 6PGD, PGDH, 6-phosphogluconate dehydrogenase decarboxylating, PGD.
Escherichia Coli.
MGSSHHHHHH SSGLVPRGSH MAQADIALIG LAVMGQNLIL NMNDHGFVVC AFNRTVSKVD DFLANEAKGT KVVGAQSLKE MVSKLKKPRR IILLVKAGQA VDDFIEKLVP LLDTGDIIID GGNSEYRDTT RRCRDLKAKG ILFVGSGVSG GEEGARYGPS LMPGGNKEAW PHIKTIFQGI AAKVGTGEPC CDWVGDEGAG HFVKMVHNGI EYGDMQLICE AYHLMKDVLG MAQDEMAQAF EDWNKTELDS FLIEITANIL KFQDTDGKHL LPKIRDSAGQ KGTGKWTAIS ALEYGVPVTL IGEAVFARCL SSLKDERIQA SKKLKGPQKF QFDGDKKSFL EDIRKALYAS KIISYAQGFM LLRQAATEFG WTLNYGGIAL MWRGGCIIRS VFLGKIKDAF DRNPELQNLL LDDFFKSAVE NCQDSWRRAV STGVQAGIPM PCFTTALSFY DGYRHEMLPA SLIQAQRDYF GAHTYELLAK PGQFIHTNWT GHGGTVSSSS YNA
Product Science Overview
Phosphogluconate Dehydrogenase is a protein-coding gene that produces a single, non-glycosylated polypeptide chain containing 503 amino acids. The enzyme catalyzes the oxidative decarboxylation of 6-phosphogluconate to ribulose-5-phosphate and carbon dioxide, with the concomitant reduction of NADP+ to NADPH . This reaction is the third step in the oxidative branch of the pentose phosphate pathway .
The enzyme is highly significant in various biological processes:
- Metabolic Regulation: It acts as a key checkpoint in the reprogramming of regulatory T cells’ metabolism and function. Blocking 6PGD in the oxidative PPP can lead to a substantial reduction in the suppressive function of regulatory T cells, shifting their phenotype towards more inflammatory types .
- Cancer Metabolism: 6PGD is commonly upregulated in many human cancers. It promotes tumor growth and radiation resistance by enhancing its activity through tyrosine phosphorylation. This modification increases its binding affinity to NADP+, thereby activating the PPP for NADPH and ribose-5-phosphate production .
Human recombinant Phosphogluconate Dehydrogenase is produced in Escherichia coli (E. coli). The recombinant enzyme is fused to a 20 amino acid His-Tag at the N-terminus and purified using proprietary chromatographic techniques. This recombinant form is used in various research applications to study its function and role in different biological processes .
Phosphogluconate Dehydrogenase is used extensively in research to understand its role in:
- Cellular Metabolism: Investigating how it regulates the balance between glycolysis and the pentose phosphate pathway.
- Immunotherapy: Exploring its potential as a metabolic checkpoint for immunotherapy applications, particularly in modulating the plasticity and function of regulatory T cells .
- Cancer Research: Studying its role in cancer metabolism, tumor growth, and resistance to therapies .
