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Phosphoglyceric acid mutase (EC 188.8.131.52) is widely distributed in mammalian tissues where it catalyzes the reversible reaction of 3-phosphoglycerate (3-PGA) to 2-phosphoglycerate (2-PGA) in the glycolytic pathway (summary by Chen et al., 1974 [PubMed 4811757]).[supplied by OMIM, Nov 2010].. Additionally we are shipping PGAM1 Antibodies (65) and PGAM1 Kits (23) and many more products for this protein.
Showing 10 out of 21 products:
Mouse (Murine) PGAM1 Protein expressed in Escherichia coli (E. coli) - ABIN1098606
Ballif, Carey, Sunyaev, Gygi: Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain. in Journal of proteome research 2008
Show all 2 references for ABIN1098606
Human PGAM1 Protein expressed in Escherichia coli (E. coli) - ABIN667196
Junien, Despoisse, Turleau, de Grouchy, Bucher, Fundele: Assignment of phosphoglycerate mutase (PGAMA) to human chromosome 10. Regional mapping of GOT1 and PGAMA to subbands 10q26.1 (or q25.3). in Annales de génétique 1982
Show all 2 references for ABIN667196
Human PGAM1 Protein expressed in Wheat germ - ABIN1314779
Kimura, Sakurai, Koumura, Yamada, Hayashi, Tanaka, Hozumi, Tanaka, Takemura, Seishima, Inuzuka: High prevalence of autoantibodies against phosphoglycerate mutase 1 in patients with autoimmune central nervous system diseases. in Journal of neuroimmunology 2010
PGAM1 correlates with spermatogenic dysfunction and affects the function of cell proliferation, apoptosis and migration.
9630033F20Rik (show C12orf5 Proteins) may play an important role in muscle wasting and that it has a distinguished characterization of gene network.[9630033F20Rik (show C12orf5 Proteins)]
histidine-phosphorylated PGAM1 correlated with expression of PKM2 in tumor tissues; decreased pyruvate kinase activity in PKM2-expressing cells allows PEP-dep (show PREP Proteins)endent histidine phosphorylation of PGAM1 and may provide an alternate glycolytic pathway
PGAM1 may be associated with the grade of glioma and be involved in the biological behavior of glioma cells. PGAM1 might be a novel therapeutic target in glioma.
Our finding showed that PGAM1 might serve as a promising therapeutic target for UBC (show RPS27A Proteins).
PGAM1 is highly expressed in clear cell renal cell carcinoma (show MOK Proteins) and correlated with clinicalpathological features, which may contribute to tumor formation and progression.
PGAM is acetylated at lysines 100/106/113/138 in its central region, and a member of the Sirtuin (show SIRT1 Proteins) family (class III deacetylase), SIRT2 (show SIRT2 Proteins), is responsible for its deacetylation.
Tyrosine26 phosphorylation represents an additional acute mechanism underlying phosphoglycerate mutase 1 upregulation.
Phosphoglycerate mutase 1 (PGAM1) contributes to biosynthesis regulation by controlling intracellular levels of its substrate, 3-phosphoglycerate (3-PG), and product, 2-phosphoglycerate (2-PG).
PGAM1 deacetylation and activity are directly controlled by Sirt1 (show SIRT1 Proteins).
histidine-phosphorylated PGAM1 correlated with expression of PKM2 in cancer cell lines; decreased pyruvate kinase activity in PKM2-expressing cells allows PEP (show PAEP Proteins)-dependent histidine phosphorylation of PGAM1 and may provide an alternate glycolytic pathway
Our studies suggested that PGAM1 plays an important role in hepatocarcinogenesis
Phosphoglyceric acid mutase (EC 184.108.40.206) is widely distributed in mammalian tissues where it catalyzes the reversible reaction of 3-phosphoglycerate (3-PGA) to 2-phosphoglycerate (2-PGA) in the glycolytic pathway (summary by Chen et al., 1974
phosphoglycerate mutase 1 (brain)
, phosphoglycerate mutase 1
, uncharacterized protein LOC706211
, BPG-dependent PGAM 1
, phosphoglycerate mutase isozyme B
, phosphoglycerate mutase A, nonmuscle form