BPGM Protein, Human (His)

BPGM Protein, Human (His) expresses in E. coliwith a His tag. Bisphosphoglycerate mutase is an erythrocyte-specific enzyme catalyzing a series of intermolecular phosphoryl group transfer reactions. Its main function is to synthesize 2,3-bisphosphoglycerate, the allosteric effector of hemoglobin^[1].

Bisphosphoglycerate mutase (BPGM) is an erythrocyte-specifictri-functional enzyme, catalyzing a series of intermolecular phosphoryl group transfer reactions. The main activity of BPGM is synthase, converting 1,3-bisphosphoglycerate(1,3-BPG) to 2,3-bisphosphoglycerate (2,3-BPG). The second activity is mutase, catalyzingthe inter-conversion between 2-phosphoglycerate (2-PGA) and 3-phosphoglycerate (3-PGA). The third activity is phosphatase, hydrolyzing the 2,3-BPG to 3-PGA or 2-PGA and a phosphate. BPGM is found in erythrocytes and placental cells, and itregulates the level of 2,3-BPG^[2].

The enzyme activity of this recombinant protein is testing in progress, we cannot offer a guarantee yet.

Human

E. coli

C-6*His

P07738 (S2-K259)

669  [NCBI]

Extracellular Domain

SKYKLIMLRHGEGAWNKENRFCSWVDQKLNSEGMEEARNCGKQLKALNFEFDLVFTSVLNRSIHTAWLILEELGQEWVPVESSWRLNERHYGALIGLNREQMALNHGEEQVRLWRRSYNVTPPPIEESHPYYQEIYNDRRYKVCDVPLDQLPRSESLKDVLERLLPYWNERIAPEVLRGKTILISAHGNSSRALLKHLEGISDEDIINITLPTGVPILLELDENLRAVGPHQFLGDQEAIQAAIKKVEDQGKVKQAKK

Approximately 30 kDa, based on SDS-PAGE under reducing conditions.

≥ 95%, as determined by reducing SDS-PAGE.

Solution.

Supplied as a 0.22 μm filter solution of 20 mM Tris, 1 mM DTT, pH 8.0.
Note: For SPR assay, please replace the buffer. Primary amine components (e.g., Tris, imidazole) can affect protein-coupled chips.

<1 EU/μg, determined by LAL method.

Stored at -80°C for 1 year from date of receipt. It is stable at -20°C for 3 months after opening. It is recommended to freeze aliquots at -80°C for extended storage. Avoid repeated freeze-thaw cycles.

Shipping with dry ice.

• [1]. Wang Y, et al. Seeing the process of histidine phosphorylation in human bisphosphoglycerate mutase. J Biol Chem. 2006;281(51):39642-39648.  [Content Brief]

  [2]. Chu WT, et al. Insights into the phosphatase and the synthase activities of human bisphosphoglycerate mutase: a quantum mechanics/molecular mechanics simulation. Phys Chem Chem Phys. 2014;16(9):3946-3954.  [Content Brief]