Bisphosphoglycerate Mutase; BPGM; 2; 3-Bisphosphoglycerate Mutase Erythrocyte; 2; 3-Bisphosphoglycerate Synthase; 2; 3-Diphosphoglycerate Mutase; DPGM; BPG-Dependent PGAM; BPGM

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

E Coli

>95% as determined by reducing SDS-PAGE.

Supplied as a 0.2 mum filtered solution of 20mM Tris, 1mM DTT, pH 8.0.

Store at < -20 degree C, stable for 6 months after receipt. Please minimize freeze-thaw cycles.

Manufactured in an ISO 9001:2015 Certified Laboratory.

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.

Bisphosphoglycerate Mutase (BPGM) is a member of the Phosphoglycerate Mutase family and BPG-Dependent PGAM subfamily. BPGM is a multifunctional enzyme. BPGM catalyzes 2, 3-DPG synthesis via its synthetase activity, and 2, 3-DPG degradation via its phosphatase activity. It also has phosphoglycerate phosphomutase activity. BPGM plays a major role in regulating hemoglobin oxygen affinity by controlling the levels of 2, 3-bisphosphoglycerate (2, 3-BPG). Deficiency of BPGM increases the affinity of cells for oxygen and result in hemolytic anemia.

Molecular Mass: 31.0 kDa
Actual Protein Molecular Mass: 30 kDa

bisphosphoglycerate mutase

bisphosphoglycerate mutase

Bisphosphoglycerate mutase

BPGM; DPGM??[Similar Products]

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]

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 5.4.2.11) activity.

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