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. This product is recommended for use in applications that do not require a catalytically active form of the protein. Applications: Suitable for use in Western Blot. Other applications not tested. Recommended Dilution: Optimal dilutions to be determined by the researcher. Storage and Stability: May be stored at 4C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20C. Aliquots are stable for at least 6 months. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
