PGP Human

Phosphoglycolate Phosphatase is a cytoplasmic enzyme that exists as a dimer with a molecular weight of approximately 72,000 Daltons . The human recombinant form of this enzyme is produced in Escherichia coli (E. coli) and is a single, non-glycosylated polypeptide chain containing 345 amino acids . It has a molecular mass of 36.5 kDa and is fused to a 24 amino acid His-tag at the N-terminus . This recombinant form is purified using proprietary chromatographic techniques to ensure high purity and activity.

Phosphoglycolate Phosphatase is found in various tissues, including red blood cells, lymphocytes, and cultured fibroblasts . It is most active in skeletal and cardiac muscles . The enzyme’s catalytic activity involves the hydrolysis of 2-phosphoglycolate to glycolate and phosphate, which is a critical step in the glycolate pathway . The enzyme shows optimal activity at a pH of 6.7 and has a Michaelis constant (Km) of 1 mM for phosphoglycolate .

The recombinant form of Phosphoglycolate Phosphatase is formulated in a buffer containing 20 mM Tris-HCl (pH 8.0), 0.15 M NaCl, 10% glycerol, and 1 mM DTT . It is recommended to store the enzyme at -20°C for long-term storage, and at 4°C if it will be used within 2-4 weeks . To maintain its stability, it is advisable to avoid multiple freeze-thaw cycles and to add a carrier protein such as 0.1% human serum albumin (HSA) or bovine serum albumin (BSA) for long-term storage .

Phosphoglycolate Phosphatase is used in various biochemical and physiological studies to understand its role in metabolic pathways. Its recombinant form is particularly useful for research purposes, as it allows for the study of the enzyme’s properties and functions in a controlled environment.