Abcam, ab279384, Anti-PGAM4 + PGAM1 antibody [OTI2A12]

Size: 50µL
Mouse Monoclonal Phosphoglycerate Mutase antibody. Suitable for WB, IHC-P and reacts with Recombinant full length protein - Human, Human samples. Cited in 3 publications. Immunogen corresponding to Recombinant Full Length Protein corresponding to Human PGAM4.
Key facts
Host species:Mouse,
Clonality:Monoclonal,
Clone number:OTI2A12,
Isotype:IgG1,
Carrier free:No,
Reacts with:Human,
Applications:IHC-P, WBSee reactivity dataSee the reactivity data table below for information on validated species and application combinations.,
Immunogen:Recombinant Full Length Protein corresponding to Human PGAM4.Q8N0Y7

Properties and Storage Information:
Form-Liquid, Purification technique-Affinity purification Protein A/G, Storage buffer-pH: 7.3Preservative: 0.02% Sodium azideConstituents: 50% Glycerol (glycerin, glycerine), 1% BSA, Shipped at conditions-Blue Ice, Appropriate short-term storage duration-1-2 weeks, Appropriate short-term storage conditions-+4°C, Appropriate long-term storage conditions--20°C, Aliquoting information-Upon delivery aliquot, Storage information-Avoid freeze / thaw cycle

Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
Phosphoglycerate mutase 1 (PGAM1) and phosphoglycerate mutase 4 (PGAM4) are enzymes involved in glycolysis acting as isomerases that catalyze the conversion of 3-phosphoglycerate to 2-phosphoglycerate. PGAM1 and PGAM4 are known for their alternate names such as BPG-dependent PGAM and PGAM-B. PGAM1 has a molecular weight of approximately 29 kDa. PGAMs express highly in tissues that demand significant energy such as muscle and brain. They have key roles in maintaining cellular energy homeostasis.
Biological function summary
PGAM1 and PGAM4 contribute significantly to energy metabolism by facilitating important steps in glycolysis. These enzymes exist as part of a larger complex in the cytoplasm cooperating with other glycolytic enzymes. PGAMs play a role in modulating levels of glycolytic intermediates therefore influencing processes like growth and development. PGAMs' dynamic regulation impacts cancer cell metabolism making them targets for cancer therapy studies.
Pathways
PGAM1 and PGAM4 play roles in both the glycolytic and gluconeogenesis pathways. In glycolysis they interact closely with enzymes like phosphofructokinase and enolase to ensure the smooth conversion of glucose to pyruvate. PGAMs' activity is directly related to their interaction with key regulatory proteins such as the glycolytic enzyme pyruvate kinase. This positions PGAMs as important checkpoints in metabolic pathways that control energy production and consumption.
PGAM1 and PGAM4 have been linked to conditions such as cancer and metabolic disorders. Studies report increased PGAM1 activity in various cancers and its elevated levels have associations with other oncogenic proteins like c-Myc. In metabolic disorders such as insulin resistance and diabetes PGAMs can influence the dysregulation of energy metabolism by interacting with proteins involved in insulin signaling. This makes them potential markers for disease progression and therapeutic targets.