Full length protein
MSKYKLIMLR HGEGAWNKEN RFCSWVDQKL NSEGMEEARN CGKQLKALNF EFDLVFTSVL NRSIHTAWLI LEELGQEWVP VESSWRLNERHYGALIGLNR EQMALNHGEE QVRLWRRSYN VTPPPIEESH PYYQEIYNDR RYKVCDVPLD QLPRSESLKD VLERLLPYWN ERIAPEVLRG KTILISAHGN SSRALLKHLE GISDEDIINI TLPTGVPILL ELDENLRAVG PHQFLGDQEA IQAAIKKVED QGKVKQAKKL EHHHHHH
31 kDa including tags
1 to 259
His tag C-Terminus
BPGM Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 267 amino acids (1-259 a.a.) and having a molecular mass of 31 kDa.
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in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
ab116488 was purified by proprietary chromatographic techniques and filter sterilized.
although stable at 4°C for 30 days, should be stored desiccated below -20°C for periods greater than 30 days. Please avoid freeze-thaw cycles.
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Shipped at 4°C. Please see notes section.
Constituents: 0.32% Tris HCl, 0.02% DTT, 10% Glycerol
- 2,3-bisphosphoglycerate mutase
- 2,3-bisphosphoglycerate mutase, erythrocyte
Plays a major role in regulating hemoglobin oxygen affinity by controlling the levels of 2,3-bisphosphoglycerate (2,3-BPG). Also exhibits mutase (EC 126.96.36.199) and phosphatase (EC 188.8.131.52) activities.
Defects in BPGM are the cause of bisphosphoglycerate mutase deficiency (BPGMD) [MIM:222800]. A disease characterized by hemolytic anemia, splenomegaly, cholelithiasis and cholecystitis.
Belongs to the phosphoglycerate mutase family. BPG-dependent PGAM subfamily.
Glycation of Lys-159 in diabetic patients inactivates the enzyme.
Information by UniProt
Recombinant Human BPGM protein (ab116488)参考文献
has not yet been referenced specifically in any publications.
Please note: All products are "FOR RESEARCH USE ONLY AND ARE NOT INTENDED FOR DIAGNOSTIC OR THERAPEUTIC USE"