Purity ~ 95% (SDS-PAGE). Purified by using conventional chromatography techniques. Bisphosphoglycerate mutase (BPGM) is an enzyme unique to erythrocytes and placental cells. This protein plays a major role in regulating hemoglobin oxygen affinity as a consequence of controlling 2,3-BPG concentration. It is responsible for the catalytic synthesis of 2,3-Bisphosphoglycerate (2,3-BPG) from 1,3-BPG. BPGM also has a mutase and a phosphatase function, but these are much less active. Recombinant human BPGM, fused to His-tag at C-terminus, was expressed in E. coli. Source: Recombinant corresponding to aa1-259 of human BPGM 6x His tagged expressed in E. coli. AA Sequence: MSKYKLIMLR HGEGAWNKEN RFCSWVDQKL NSEGMEEARN CGKQLKALNF EFDLVFTSVL NRSIHTAWLI LEELGQEWVP VESSWRLNER HYGALIGLNR EQMALNHGEE QVRLWRRSYN VTPPPIEESH PYYQEIYNDR RYKVCDVPLD QLPRSESLKD VLERLLPYWN ERIAPEVLRG KTILISAHGN SSRALLKHLE GISDEDIINI TLPTGVPILL ELDENLRAVG PHQFLGDQEA IQAAIKKVED QGKVKQAKKL EHHHHHH Enzyme Activity: Not determined. T