Bisphosphoglycerate mutase, EC 188.8.131.52, BPGM, 2,3-bisphosphoglycerate mutase erythrocyte, 2,3-bisphosphoglycerate synthase, BPG-dependent PGAM.
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 184.108.40.206 (mutase) and EC 220.127.116.11 (phosphatase), but with a reduced activity.
Anti-human BPGM mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human BPGM amino acids 1-259 purified from E. coli.
BPGM antibody was purified from mouse ascitic fluids by protein-A affinity chromatography.
1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.
Stability / Shelf Life
BPGM antibody has been tested by ELISA, Western blot analysis, Flow cytometry and ICC/IF to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results.