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2,3-diphosphoglycerate (2,3-DPG) is a small molecule found at high concentrations in red blood cells where it binds to and decreases the oxygen affinity of hemoglobin. Additionally we are shipping BPGM Proteins (20) and many more products for this protein.
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Human Polyclonal BPGM Primary Antibody for WB - ABIN656546
Lamesch, Li, Milstein, Fan, Hao, Szabo, Hu, Venkatesan, Bethel, Martin, Rogers, Lawlor, McLaren, Dricot, Borick, Cusick, Vandenhaute, Dunham, Hill, Vidal: hORFeome v3.1: a resource of human open reading frames representing over 10,000 human genes. in Genomics 2007
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Human Polyclonal BPGM Primary Antibody for EIA, WB - ABIN950665
Wang, Liu, Wei, Cheng, Lin, Gong: Seeing the process of histidine phosphorylation in human bisphosphoglycerate mutase. in The Journal of biological chemistry 2006
Show all 2 references for ABIN950665
Human Polyclonal BPGM Primary Antibody for ICC, IF - ABIN4285113
Bachmann, Burté, Pramana, Conte, Brown, Orimadegun, Ajetunmobi, Afolabi, Akinkunmi, Omokhodion, Akinbami, Shokunbi, Kampf, Pawitan, Uhlén, Sodeinde, Schwenk, Wahlgren, Fernandez-Reyes, Nilsson: Affinity proteomics reveals elevated muscle proteins in plasma of children with cerebral malaria. in PLoS pathogens 2014
1.94 A resolution X-ray structure of bisphosphoglycerate mutase is presented, focusing on the dynamic nature of key ligand-binding residues and their interaction with the inhibitor citrate
bisphosphoglycerate mutase crystallographic structure
analysis of histidine phosphorylation in human bisphosphoglycerate mutase
Placental expression of BPGM can influence maternal 2,3-bisphosphoglycerate (BPG) blood levels and supports a hypothesis under which BPG synthesized in the placenta may act on maternal haemoglobin to enhance delivery of oxygen to the developing fetus.
2,3-diphosphoglycerate (2,3-DPG) is a small molecule found at high concentrations in red blood cells where it binds to and decreases the oxygen affinity of hemoglobin. This gene encodes a multifunctional enzyme that catalyzes 2,3-DPG synthesis via its synthetase activity, and 2,3-DPG degradation via its phosphatase activity. The enzyme also has phosphoglycerate phosphomutase activity. Deficiency of this enzyme increases the affinity of cells for oxygen. Mutations in this gene result in hemolytic anemia. Multiple alternatively spliced variants, encoding the same protein, have been identified.
, 2,3-bisphosphoglycerate mutase, erythrocyte
, 2,3-bisphosphoglycerate synthase
, 2,3-diphosphoglycerate mutase
, BPG-dependent PGAM
, bisphosphoglycerate mutase
, erythrocyte 2,3-bisphosphoglycerate mutase