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| Product Name | Bisphosphoglycerate Mutase, Recombinant, Human |
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| Description | 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 |
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| Size | 100ug |
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| Concentration | n/a |
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| Applications | WB |
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| Other Names | Bisphosphoglycerate Mutase, Recombinant, Human (BPGM, 2,3-bisphosphoglycerate Mutase (Erythrocyte), 2,3-bisphosphoglycerate Synthase, BPG-dependent PGAM) |
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| Gene, Accession, CAS # | Accession: NP_001715 |
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| Catalog # | B2100-67H |
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| Order / More Info | Bisphosphoglycerate Mutase, Recombinant, Human from UNITED STATES BIOLOGICAL |
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| Product Specific References | n/a |
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