PGAM1 Protein, Human (His, Strep)

PGAM1 protein plays a pivotal role in glycolysis by catalyzing the vital interconversion of 2-phosphoglycerate and 3-phosphoglycerate. Additionally, it is instrumental in the conversion of (2R)-2,3-bisphosphoglycerate to (2R)-3-phospho-glyceroyl phosphate, further contributing to the intricate metabolic processes associated with glycolytic pathways. PGAM1 Protein, Human (His, Strep) is the recombinant human-derived PGAM1 protein, expressed by E. coli , with N-Strep, N-6*His labeled tag. The total length of PGAM1 Protein, Human (His, Strep) is 254 a.a., .

PGAM1, or phosphoglycerate mutase 1, plays a pivotal role in glycolysis by catalyzing the reversible interconversion of 2-phosphoglycerate and 3-phosphoglycerate. This enzymatic activity is a crucial step in the glycolytic pathway, facilitating the conversion of glucose-derived substrates into energy and metabolic intermediates. Additionally, PGAM1 is involved in the interconversion of (2R)-2,3-bisphosphoglycerate and (2R)-3-phospho-glyceroyl phosphate. The regulation of these reactions is vital for maintaining the glycolytic flux and ensuring the proper flow of metabolites through the glycolytic pathway. PGAM1's enzymatic functions contribute to the overall efficiency of energy production and metabolic homeostasis within cells.

Human

E. coli

N-Strep;N-6*His

P18669 (M1-K254)

5223

Greater than 90% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.