PGP Human, Active
Glycerol-3-phosphate phosphatase, G3PP, Aspartate-based ubiquitous Mg(2+)-dependent phosphatase, AUM, Phosphoglycolate phosphatase, PGP.
Description
PGP Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 345 amino acids (1-321a.a) and having a molecular mass of 36.5kDa.
PGP is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Product Specs
Glycerol-3-phosphate phosphatase, G3PP, Aspartate-based ubiquitous Mg(2+)-dependent phosphatase, AUM, Phosphoglycolate phosphatase, PGP.
MGSSHHHHHH SSGLVPRGSH MGSHMAAAEA GGDDARCVRL SAERAQALLA DVDTLLFDCD GVLWRGETAV PGAPEALRAL RARGKRLGFI TNNSSKTRAA YAEKLRRLGF GGPAGPGASL EVFGTAYCTA LYLRQRLAGA PAPKAYVLGS PALAAELEAV GVASVGVGPE PLQGEGPGDW LHAPLEPDVR AVVVGFDPHF SYMKLTKALR YLQQPGCLLV GTNMDNRLPL ENGRFIAGTG CLVRAVEMAA QRQADIIGKP SRFIFDCVSQ EYGINPERTV MVGDRLDTDI LLGATCGLKT ILTLTGVSTL GDVKNNQESD CVSKKKMVPD FYVDSIADLL PALQG.
Product Science Overview
Phosphoglycolate phosphatase was first studied and purified in plants, where it is involved in the photorespiratory pathway. This pathway is essential for photosynthesis, as it helps in the regeneration of 3-phosphoglycerate from 2-phosphoglycolate, which is a byproduct of the carboxylation reaction catalyzed by ribulose-1,5-bisphosphate carboxylase-oxygenase (rubisco) .
In humans, phosphoglycolate phosphatase has been identified in various tissues, including red blood cells, lymphocytes, and cultured fibroblasts. It is most active in skeletal muscle and cardiac muscle . The enzyme’s activity is crucial for the regulation of 2,3-diphosphoglycerate (2,3-DPG), a compound that affects hemoglobin’s oxygen-binding affinity .
The structural characterization of phosphoglycolate phosphatase from Thermoplasma acidophilum revealed that the enzyme exists as a dimer. Each monomer consists of two distinct domains: a smaller cap domain and a larger core domain. The active site of the enzyme is a continuous tunnel lined with acidic residues, which is consistent with other acid phosphatases .
Human recombinant phosphoglycolate phosphatase is produced using Escherichia coli expression systems. The recombinant enzyme is a single, non-glycosylated polypeptide chain containing 345 amino acids and has a molecular mass of approximately 36.5 kDa . It is purified using proprietary chromatographic techniques to ensure high purity and activity .
The recombinant enzyme is formulated in a buffer solution containing Tris-HCl, NaCl, glycerol, and dithiothreitol (DTT) to maintain its stability and activity. It is typically stored at 4°C for short-term use or frozen at -20°C for long-term storage .
Phosphoglycolate phosphatase is used in various research applications, including studies on metabolic pathways, enzyme kinetics, and the regulation of 2,3-DPG in red blood cells. It is also used in the development of therapeutic strategies for diseases associated with phosphoglycolate metabolism, such as tardive dyskinesia and polycystic kidney disease .
