Analytical Data
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基因名
ESR2
- Application
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别名
Short name: ER-beta Alternative name(s): Nuclear receptor subfamily 3 group A member 2
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种属
Human
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表达系统
E. coli
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标签
N- His-SUMO
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
Q92731
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表达区间
2-323aa
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分子量
51.9 kDa
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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
ESR2, also known as estrogen receptor beta, is a crucial member of the nuclear hormone receptor superfamily that plays a significant role in mediating the biological effects of estrogens in various tissues. Its involvement in key physiological processes such as reproductive health, bone density regulation, cardiovascular function, and brain development necessitates a deeper understanding of its function and mechanisms. Research into ESR2 has gained traction due to its potential implications in diseases such as breast cancer, prostate cancer, and osteoporosis, where estrogen signaling is often disrupted. The development of recombinant ESR2 proteins facilitates elucidation of its structure-function relationships, allowing scientists to investigate ligand-binding properties, protein interactions, and downstream signaling pathways. Such studies are pivotal for identifying potential therapeutic targets and strategies, particularly in conditions associated with estrogen imbalance. Furthermore, the generation of high-purity recombinant ESR2 allows for advanced techniques such as crystallography and NMR spectroscopy to characterize conformational changes in response to ligands, providing insights into receptor activation and modulation. This research not only enhances our understanding of ESR2's biological significance but also paves the way for novel therapeutic interventions to address estrogen-related pathologies, ultimately contributing to improved health outcomes.
