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Recombinant Human EGFR protein

  • 中文名: 表皮生长因子受体(EGFR)重组蛋白
  • 别    名: EGFR;ERBB;ERBB1;HER1;Epidermal growth factor receptor
货号: PA1000-984DB
Price: ¥询价
数量:
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产品详情

纯度>95%SDS-PAGE.
种属Human
靶点EGFR
Uniprot NoP00533
内毒素< 0.01EU/μg
表达宿主E.coli
表达区间25-645aa
氨基酸序列LEEKKVCQGTSNKLTQLGTFEDHFLSLQRMFNNCEVVLGNLEITYVQRNY DLSFLKTIQEVAGYVLIALNTVERIPLENLQIIRGNMYYENSYALAVLSN YDANKTGLKELPMRNLQEILHGAVRFSNNPALCNVESIQWRDIVSSDFLS NMSMDFQNHLGSCQKCDPSCPNGSCWGAGEENCQKLTKIICAQQCSGRCR GKSPSDCCHNQCAAGCTGPRESDCLVCRKFRDEATCKDTCPPLMLYNPTT YQMDVNPEGKYSFGATCVKKCPRNYVVTDHGSCVRACGADSYEMEEDGVR KCKKCEGPCRKVCNGIGIGEFKDSLSINATNIKHFKNCTSISGDLHILPV AFRGDSFTHTPPLDPQELDILKTVKEITGFLLIQAWPENRTDLHAFENLE IIRGRTKQHGQFSLAVVSLNITSLGLRSLKEISDGDVIISGNKNLCYANT INWKKLFGTSGQKTKIISNRGENSCKATGQVCHALCSPEGCWGPEPRDCV SCRNVSRGRECVDKCNLLEGEPREFVENSECIQCHPECLPQAMNITCTGR GPDNCIQCAHYIDGPHCVKTCPAGVMGENNTLVWKYADAGHVCHLCHPNC TYGCTGPGLEGCPTNGPKIPS—Linker(gggsgggs)—10*His(hhhh hhhhhh)
预测分子量71 kDa
蛋白标签His tag N-Terminus
缓冲液PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
稳定性 & 储存条件Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt.
Reconstituted protein solution can be stored at 2-8°C for 2-7 days.
Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.
复溶Always centrifuge tubes before opening.Do not mix by vortex or pipetting.
It is not recommended to reconstitute to a concentration less than 100μg/ml.
Dissolve the lyophilized protein in distilled water.
Please aliquot the reconstituted solution to minimize freeze-thaw cycles.

参考文献

以下是3-4条关于EGFR重组蛋白的参考文献及摘要概括:

1. **文献名称**:*Human epidermal growth factor receptor cDNA sequence and aberrant expression of the amplified gene in A431 epidermoid carcinoma cells*

**作者**:Yarden Y, Schlessinger J

**摘要**:首次通过重组技术克隆了EGFR的cDNA,分析了其结构与功能,揭示了EGFR的酪氨酸激酶活性及其在肿瘤细胞中的异常表达机制。

2. **文献名称**:*Targeted therapy for cancer: The application of recombinant EGFR extracellular domain in kinase inhibitor screening*

**作者**:Huang L et al.

**摘要**:利用重组EGFR胞外域蛋白建立高通量筛选模型,鉴定小分子激酶抑制剂,为抗肿瘤药物开发提供实验基础。

3. **文献名称**:*Cetuximab (Erbitux) – a recombinant human/mouse chimeric EGFR monoclonal antibody for cancer therapy*

**作者**:Mendelsohn J, Baselga J

**摘要**:综述了基于重组EGFR蛋白开发的西妥昔单抗(抗EGFR单克隆抗体)的临床前及临床研究,阐明其通过阻断配体结合抑制肿瘤生长的机制。

4. **文献名称**:*Structural analysis of the EGFR ectodomain reveals mechanisms of ligand-induced activation*

**作者**:Zhang X et al.

**摘要**:通过重组表达EGFR胞外域蛋白并解析其晶体结构,揭示了EGF结合诱导受体二聚化及激活的分子构象变化。

(注:以上文献信息为简化概括,实际引用请核对原文。)

背景信息

Epidermal Growth Factor Receptor (EGFR) recombinant protein is a genetically engineered version of the transmembrane tyrosine kinase receptor that plays a central role in regulating cell proliferation, survival, and differentiation. EGFR, also known as HER1 or ErbB1. belongs to the ErbB receptor family and is activated by ligands such as epidermal growth factor (EGF) and transforming growth factor-alpha (TGF-α). Upon ligand binding, EGFR undergoes dimerization and autophosphorylation, initiating downstream signaling cascades like RAS/MAPK, PI3K/AKT, and JAK/STAT pathways. Dysregulation of EGFR, due to overexpression or mutations, is implicated in various cancers, making it a key therapeutic target.

Recombinant EGFR proteins are produced using expression systems (e.g., mammalian, insect, or bacterial cells) to ensure proper post-translational modifications and functional activity. These proteins typically include the extracellular ligand-binding domain or the intracellular kinase domain, enabling studies on receptor-ligand interactions, signaling mechanisms, and drug screening. Researchers use EGFR recombinant proteins to develop monoclonal antibodies (e.g., cetuximab) or small-molecule inhibitors (e.g., gefitinib, osimertinib) that block aberrant signaling in cancers. Additionally, they serve as critical tools in structural biology, helping to elucidate EGFR's conformational changes during activation and resistance mechanisms.

The development of EGFR recombinant proteins has advanced personalized cancer therapies, particularly for non-small cell lung cancer (NSCLC) with EGFR mutations. However, challenges like drug resistance and tumor heterogeneity drive ongoing research to optimize recombinant variants for improved therapeutic targeting and diagnostic applications.

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