Analytical Data
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基因名
BPGM
- Application
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别名
2,3-Bisphosphoglycerate Mutase; 2,3-bisphosphoglycerate mutase, erythrocyte; 2,3-bisphosphoglycerate synthase; BPG-dependent PGAM
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种属
Mouse
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表达系统
E. coli
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标签
N-His
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纯度
Greater than 95% as determined by SDS-PAGE.
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蛋白编号
P15327
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表达区间
Trp85~Val216
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分子量
19kDa
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内毒素
< 1.0 EU per μg protein as determined by the LAL method.
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性状
Freeze-dried powder
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缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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复溶方法
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- 个性化定制
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稳定性测试
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.
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保存条件 & 期限
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.
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运输条件
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
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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.
