2,3-Bisphosphoglycerate Mutase, Recombinant Protein

BPGM Human; 2,3-Bisphosphoglycerate Mutase Human Recombinant; Bisphosphoglycerate mutase; EC 5.4.2.4; BPGM; 2; 3-bisphosphoglycerate mutase erythrocyte; 2; 3-bisphosphoglycerate synthase; BPG-dependent PGAM

For Research Use Only. Not for use in diagnostic procedures.

E Coli

Greater than 95% as determined by SDS-PAGE.

The BPGM solution contains 20mM Tris-HCl pH-8, 1mM DTT, and 10% glycerol.
Sterile Filtered clear colorless solution.

Small volumes of BPGM recombinant protein vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.

Description: BPGM Human Recombinant produced in E Coli is a single, non-glycosylated, polypeptide chain containing 267 amino acids (1-259 a.a.) and having a molecular mass of 31 kDa. The BPGM is fused to an 8 amino acid His Tag at C-Terminus and purified by proprietary chromatographic techniques.

Introduction: BPGM is found at high concentrations in red blood cells where it binds to and decreases the oxygen affinity of hemoglobin. PGM deficiency increases the oxygen affinity of cells. BPGM is a multifunctional enzyme that catalyzes 2,3-DPG synthesis through its synthetase activity, and 2,3-DPG degradation using its phosphatase activity. BPGM has phosphoglycerate phosphomutase activity. Mutations in BPGM cause hemolytic anemia. BPGM catalyzes the reaction of EC 5.4.2.1 (mutase) and EC 3.1.3.13 (phosphatase), but with a reduced activity.

ENZYMES; Enzymes; Mutase

30,005 Da

2,3-bisphosphoglycerate mutase

bisphosphoglycerate mutase; 2,3-bisphosphoglycerate mutase, erythrocyte; 2,3-bisphosphoglycerate synthase; 2,3-diphosphoglycerate mutase; BPG-dependent PGAM; erythrocyte 2,3-bisphosphoglycerate mutase

Bisphosphoglycerate mutase

BPGM; DPGM  [Similar Products]

PMGE_HUMAN

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. [provided by RefSeq, Sep 2009]

BPGM: Plays a major role in regulating hemoglobin oxygen affinity by controlling the levels of its allosteric effector 2,3- bisphosphoglycerate (2,3-BPG). Also exhibits mutase (EC 5.4.2.1) and phosphatase (EC 3.1.3.13) activities. Defects in BPGM are the cause of bisphosphoglycerate mutase deficiency (BPGMD). A disease characterized by hemolytic anemia, splenomegaly, cholelithiasis and cholecystitis. Belongs to the phosphoglycerate mutase family. BPG- dependent PGAM subfamily.

Protein type: EC 5.4.2.11; Phosphatase (non-protein); EC 5.4.2.4; Carbohydrate Metabolism - glycolysis and gluconeogenesis; EC 3.1.3.13; Isomerase

Chromosomal Location of Human Ortholog: 7q33

Molecular Function: phosphoglycerate mutase activity; bisphosphoglycerate mutase activity; bisphosphoglycerate phosphatase activity

Biological Process: erythrocyte development; glycolysis; dephosphorylation; carbohydrate metabolic process; respiratory gaseous exchange

Disease: Bisphosphoglycerate Mutase Deficiency

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