Analytical Data
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基因名
EGFR
- Application
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别名
Epidermal growth factor receptor; EGFR; ERBB; ERBB1; HER1
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种属
Mouse
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表达系统
HEK293
-
标签
C-His
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
Q9EP98
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表达区间
25-647aa
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分子量
100 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
Related Products
Identification
Protein Description
Epidermal Growth Factor Receptor (EGFR) is a transmembrane protein that plays a crucial role in cell growth, proliferation, and survival. Its dysregulation is commonly associated with various cancers, making it a pivotal target for therapeutic intervention. Research into recombinant EGFR proteins has gained momentum due to their potential applications in cancer biology and targeted therapies. The expression of EGFR is often upregulated in malignant tumors, where it mediates signaling pathways that promote tumorigenesis. As a result, scientists have focused on generating recombinant EGFR proteins to better understand its structure-function relationship and to develop novel inhibitors that can block its activity. Furthermore, recombinant EGFR proteins can serve as valuable tools for studying ligand-receptor interactions, developing diagnostic assays, and screening potential therapeutic compounds. The advent of advanced biotechnological techniques has made it easier to produce these proteins in sufficient quantities and with desired modifications, thus enabling detailed studies. As our understanding of EGFR continues to evolve, the ongoing research into its recombinant forms not only enhances our knowledge of cancer biology but also holds promise for improving treatment strategies and patient outcomes in EGFR-related malignancies.













