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

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

E Coli

>95%

Storage: Avoid repeated freeze/thaw cycles. Store at 2-8 degree C for one month. Aliquot and store at -80 degree C for 12 months.
Stability Test: The thermal stability is described by the loss rate of the target protein. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37 degree C for 48h, and no obvious degradation and precipitation were observed. The loss of this protein is less than 5% within the expiration date under appropriate storage condition.

Manufactured in an ISO 9001:2008 and ISO 13485:2003 Certified Laboratory.

Manufactured in a lab with traceable raw materials. Bulk orders can typically be prepared to the customera??s specifications, please inquire.

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.

SDS-PAGE, Western Blot (WB), ELISA (EIA), Immunoprecipitation (IP)

19.1kDa

bisphosphoglycerate mutase

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

Chromosomal Location of Human Ortholog: 7q33

Cellular Component: cytosol

Molecular Function: 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity; bisphosphoglycerate mutase activity; bisphosphoglycerate phosphatase activity

Biological Process: carbohydrate metabolic process; dephosphorylation; gluconeogenesis; glycolysis; regulation of pentose-phosphate shunt; respiratory gaseous exchange

Disease: Bisphosphoglycerate Mutase Deficiency

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