PGAM1 Human, Active

PGAM1 is a member of the phosphoglycerate mutase family and is expressed in various tissues, including the brain and muscles . The human recombinant form of PGAM1 is typically expressed in Escherichia coli and purified to high levels of purity, often exceeding 90% . This recombinant protein is biologically active and can elicit a biological response in vivo, making it suitable for various biochemical and functional studies .

The primary function of PGAM1 is to facilitate the interconversion of 3-PGA and 2-PGA, a critical step in glycolysis . This reaction is essential for the proper functioning of the glycolytic pathway, which is vital for energy production in cells. PGAM1 also plays a role in gluconeogenesis, the process of generating glucose from non-carbohydrate substrates .

PGAM1 has been implicated in various diseases, including cancer. It is known to be upregulated in several types of tumors, such as pancreatic, lung, liver, renal clear cell carcinoma, and gliomas . The upregulation of PGAM1 in these cancers is often associated with poor prognosis, making it a potential target for therapeutic intervention .

The recombinant human PGAM1 protein is characterized by its high specific activity, with one unit of the enzyme converting 1.0 micromole of 3-phosphoglycerate to 2-phosphoglycerate per minute at pH 7.6 and 37°C . The enzyme is also known to be acetylated at specific lysine residues under high glucose conditions, which increases its catalytic activity .

Recombinant human PGAM1 is widely used in research to study its role in metabolism and disease. It is suitable for various applications, including SDS-PAGE and functional assays . Researchers use this protein to understand its biochemical properties, regulatory mechanisms, and potential as a therapeutic target.