Analytical Data
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基因名
ERb
- Application
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别名
ERb;HER2;MLN19;NEU;Receptor tyrosine-Protein kinase erbB-2
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种属
Human
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表达系统
E. coli
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标签
His tag N-Terminus
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
P04626
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表达区间
720-976aa
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氨基酸序列
LRKVKVLGSGAFGTVYKGIWIPDGENVKIPVAIKVLRENTSPKANKEILDEAYVMAGVGSPYVSRLLGICLTSTVQLVTQLMPYGCLLDHVRENRGRLGSQDLLNWCMQIAKGMSYLEDVRLVHRDLAARNVLVKSPNHVKITDFGLARLLDIDETEYHADGGKVPIKWMALESILRRRFTHQSDVWSYGVTVWELMTFGAKPYDGIPAREIPDLLEKGERLPQPPICTIDVYMIMVKCWMIDSECRPRFRELVSEF
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分子量
36.6 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
The study of ERb (Estrogen Receptor beta) recombinant proteins has gained significant attention in recent years due to their potential role in various biological processes and therapeutic applications. Estrogen receptors are critical mediators of estrogenic signaling, which influences reproductive and non-reproductive tissues. While ER alpha has been extensively studied, the less understood ERb exhibits distinct tissue distributions and functional roles. Research indicates that ERb is involved in regulating pathways related to cell proliferation, differentiation, and apoptosis, which are vital in conditions such as cancer, osteoporosis, and cardiovascular diseases. The development of recombinant proteins allows for the detailed investigation of ERb's structure-function relationships, binding affinities, and interactions with co-regulators. These studies not only provide insights into ERb's physiological roles but also open avenues for the design of selective modulators that can target specific signaling pathways. By using recombinant protein technology, researchers can produce ERb in manageable quantities, facilitating high-throughput screening for potential therapeutic compounds. Furthermore, understanding how ERb functions at the molecular level can lead to the development of novel strategies for treatment, especially in hormone-related disorders and cancers. Thus, the exploration of ERb recombinant proteins stands as a promising frontier in biomedical research, with implications for improving therapeutic options and patient outcomes.












