Analytical Data
-
Gene name
BPGM
- Application
-
Alternative Names
2,3-Bisphosphoglycerate Mutase; 2,3-bisphosphoglycerate mutase, erythrocyte; 2,3-bisphosphoglycerate synthase; BPG-dependent PGAM
-
Species
Mouse
-
Source
E. coli
-
Tag
N-His
-
Purity
Greater than 95% as determined by SDS-PAGE.
-
Uniprot
P15327
-
Expression Region
Trp85~Val216
-
Molecular Weight
19kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
-
Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
-
Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
BPGM (bisphosphoglycerate mutase) is a crucial enzyme involved in the regulation of 2,3-bisphosphoglycerate (2,3-BPG) levels within red blood cells. This metabolite plays a significant role in modulating hemoglobin's affinity for oxygen, thereby influencing oxygen delivery to tissues. The research surrounding BPGM recombinant proteins has gained prominence due to its implications in various physiological conditions and disorders. Alterations in 2,3-BPG levels can lead to pathological states such as anemia, hypoxia, and certain chronic diseases, making BPGM a potential target for therapeutic intervention. Additionally, recombinant BPGM proteins can serve as valuable tools in studying enzyme kinetics, protein stability, and structural biology, offering insights into the enzyme's functional mechanisms. Genetic engineering techniques have enabled the production of BPGM in heterologous systems, facilitating large-scale purification and functional characterization. Understanding the structure-function relationship of BPGM is essential for developing strategies to modulate its activity, providing promising avenues for clinical applications in improving oxygenation in tissues, especially in conditions characterized by impaired oxygen transport.
