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BPGM Antibody (C-term) Blocking peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
| Primary Accession | P07738 |
|---|---|
| Clone Names | 100318193 |
| Gene ID | 669 |
|---|---|
| Other Names | Bisphosphoglycerate mutase, BPGM, 3-bisphosphoglycerate mutase, erythrocyte, 3-bisphosphoglycerate synthase, 3-diphosphoglycerate mutase, DPGM, BPG-dependent PGAM, BPGM |
| Format | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
| Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C. |
| Precautions | This product is for research use only. Not for use in diagnostic or therapeutic procedures. |
| Name | BPGM |
|---|---|
| Function | Plays a major role in regulating hemoglobin oxygen affinity by controlling the levels of its allosteric effector 2,3- bisphosphoglycerate (2,3-BPG). Also exhibits mutase (EC 5.4.2.11) activity. |
| Tissue Location | Expressed in red blood cells. Expressed in non- erythroid cells of the placenta; present in the syncytiotrophoblast layer of the placental villi at the feto-maternal interface (at protein level). |
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Provided below are standard protocols that you may find useful for product applications.
Background
2,3-diphosphoglycerate (2,3-DPG) is a small molecule foundat high concentrations in red blood cells where it binds to anddecreases the oxygen affinity of hemoglobin. This gene encodes amultifunctional enzyme that catalyzes 2,3-DPG synthesis via itssynthetase activity, and 2,3-DPG degradation via its phosphataseactivity. The enzyme also has phosphoglycerate phosphomutaseactivity. Deficiency of this enzyme increases the affinity of cellsfor oxygen. Mutations in this gene result in hemolytic anemia.Multiple alternatively spliced variants, encoding the same protein,have been identified.
References
Lamesch, P., et al. Genomics 89(3):307-315(2007)Wang, Y., et al. J. Biol. Chem. 281(51):39642-39648(2006)Wang, Y., et al. J. Biol. Chem. 279(37):39132-39138(2004)Fujita, T., et al. J. Biochem. 124(6):1237-1244(1998)Fujita, T., et al. J. Biochem. 124(6):1237-1244(1998)
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