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
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 4 degrees C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20 degrees C. 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.
Quick Search
Products 
