Recombinant human PGAM2 protein (Active) is a Human Full Length protein, in the 1 to 253 aa range, expressed in Escherichia coli, with >95% purity and suitable for SDS-PAGE, FuncS.
M G S S H H H H H H S S G L V P R G S H M A T H R L V M V R H G E S T W N Q E N R F C G W F D A E L S E K G T E E A K R G A K A I K D A K M E F D I C Y T S V L K R A I R T L W A I L D G T D Q M W L P V V R T W R L N E R H Y G G L T G L N K A E T A A K H G E E Q V K I W R R S F D I P P P P M D E K H P Y Y N S I S K E R R Y A G L K P G E L P T C E S L K D T I A R A L P F W N E E I V P Q I K A G K R V L I A A H G N S L R G I V K H L E G M S D Q A I M E L N L P T G I P I V Y E L N K E L K P T K P M Q F L G D E E T V R K A M E A V A A Q G K A K
Application | Reactivity | Dilution info | Notes |
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Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Application FuncS | Reactivity Reacts | Dilution info - | Notes - |
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Interconversion of 3- and 2-phosphoglycerate with 2,3-bisphosphoglycerate as the primer of the reaction. Can also catalyze the reaction of EC 5.4.2.4 (synthase), but with a reduced activity.
PGAMM, PGAM2, Phosphoglycerate mutase 2, BPG-dependent PGAM 2, Muscle-specific phosphoglycerate mutase, Phosphoglycerate mutase isozyme M, PGAM-M
Recombinant human PGAM2 protein (Active) is a Human Full Length protein, in the 1 to 253 aa range, expressed in Escherichia coli, with >95% purity and suitable for SDS-PAGE, FuncS.
pH: 8
Constituents: 20% Glycerol (glycerin, glycerine), 0.58% Sodium chloride, 0.32% Tris HCl, 0.02% (R*,R*)-1,4-Dimercaptobutan-2,3-diol
ab219276 was purified by using conventional chromatography.
Interconversion of 3- and 2-phosphoglycerate with 2,3-bisphosphoglycerate as the primer of the reaction. Can also catalyze the reaction of EC 5.4.2.4 (synthase), but with a reduced activity.
Belongs to the phosphoglycerate mutase family. BPG-dependent PGAM subfamily.
This product is an active protein and may elicit a biological response in vivo, handle with caution.
PGAM2 or phosphoglycerate mutase 2 is an enzyme and plays an important role in glycolysis. This enzyme catalyzes the conversion of 3-phosphoglycerate to 2-phosphoglycerate. PGAM2 is known for its molecular weight of approximately 29 kDa. It expresses in skeletal muscle tissue predominantly allowing it to help meet the energy demands during muscle contraction. The activity of PGAM2 is essential in tissues that require high energy supply.
The enzyme PGAM2 is important in energy metabolism within the cells. It participates in the glycolytic pathway which leads to ATP production necessary for cell survival and functioning. PGAM2 acts as part of the glycolytic enzyme complex. By enabling the conversion of intermediates PGAM2 facilitates the continuous flow of the glycolytic cascade necessary for efficient energy extraction from glucose.
PGAM2's function is central in glycolysis and gluconeogenesis. These pathways are essential for energy production and glucose homeostasis respectively. It collaborates with proteins such as enolase the enzyme responsible for converting 2-phosphoglycerate to phosphoenolpyruvate further down the glycolytic pathway. These interactions support the efficient production of ATP and gluconeogenic capabilities of the liver and kidney where energy conservation and storage are fundamental.
PGAM2 deficiency has connections to metabolic and muscular conditions. One of the diseases associated with PGAM2 is glycogen storage disease type X also known as muscle phosphoglycerate mutase deficiency. It affects muscle function by disrupting glycolysis. Additionally aberrations in PGAM2 activity can associate with metabolic dysfunctions often connected to proteins such as lactate dehydrogenase which gatekeeps the final steps of anaerobic glycolysis. Studying PGAM2 deeply and its links to these diseases provides insights for potential therapeutic targets.
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15% SDS-PAGE - Recombinant human PGAM2 protein (Active) (ab219276) at 3 μg.
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