PGD Human
Phosphogluconate Dehydrogenase Human Recombinant
Cat. No.
BT14117
Source
Escherichia Coli.
Synonyms
EC 1.1.1.44, 6PGD, PGDH, 6-phosphogluconate dehydrogenase decarboxylating, PGD.
Appearance
Sterile Filtered clear colorless solution.
Purity
Greater than 95% as determined by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Description
PGD Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 503 amino acids (1-483 a.a.) and having a molecular mass of 55.3 kDa.
The PGD is fused to a 20 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.
Product Specs
Introduction
6-phosphogluconate dehydrogenase (6PGD) is the second dehydrogenase in the pentose phosphate pathway. The pentose phosphate pathway is essential for nucleic acid biosynthesis and a major source of NADPH. 6PGD deficiency is typically asymptomatic and is inherited in an autosomal dominant manner. This deficiency can elevate erythrocyte pyruvate kinase activity and decrease glutathione synthetase, potentially leading to hemolysis.
Description
Recombinant human 6PGD, expressed in E. coli, is a non-glycosylated polypeptide chain containing 503 amino acids (with amino acids 1-483 present) and having a molecular mass of 55.3 kDa. The protein includes a 20 amino acid His-tag at the N-terminus and is purified using proprietary chromatographic techniques.
Physical Appearance
Clear, colorless, and sterile-filtered solution.
Formulation
The PGD solution is formulated in 20mM Tris-HCl (pH 8), 1mM DTT, 0.1M NaCl, and 10% glycerol.
Stability
For short-term storage (up to 2-4 weeks), store at 4°C. For extended storage, freeze at -20°C. Adding a carrier protein (0.1% HSA or BSA) is recommended for long-term storage. Minimize repeated freeze-thaw cycles.
Purity
Purity is greater than 95% as determined by SDS-PAGE.
Synonyms
EC 1.1.1.44, 6PGD, PGDH, 6-phosphogluconate dehydrogenase decarboxylating, PGD.
Source
Escherichia Coli.
Amino Acid Sequence
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
Structure and Function
PGD is a protein-coding gene, and the human recombinant form is typically produced in E. coli for research and therapeutic purposes . The enzyme’s activity is essential for cellular processes that require NADPH, such as fatty acid synthesis and the maintenance of reduced glutathione levels, which protect cells from oxidative damage .
Genetic and Biochemical Characteristics
Recombinant Production
Recombinant human PGD is produced using E. coli expression systems. The recombinant protein is often tagged with a His-tag for purification purposes and is supplied in a carrier-free form to avoid interference in experimental applications . The enzyme’s activity is measured by its ability to dehydrogenate 6-phosphogluconic acid, with a specific activity greater than 6000 pmol/min/μg .
Applications in Research
Clinical Relevance
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