Active Recombinant Human EGFR protein, His&GST-tagged

• Cat.No.: EGFR-31H
• Product Overview: Active Recombinant Human EGFR protein(Met 668-Ala 1210)(NP_005219) was expressed in Insect Cells, fused with the N-terminal polyhistidine-tagged GST tag at the N-terminus.

Specification

• Species: Human
• Source: Insect Cells
• Tag: GST&His
• Protein Length: 668-1210 aa
• Form: Supplied as sterile 50mM Tris,150mM NaCl, 25%glycerol，0.02%Triton X-100,0.4mM β-Mercaptoethanol,pH 7.5.
• Bio-activity: The specific activity was determined to be 105 nmol/min/mg using Poly(Glu:Tyr) 4:1 as substrate.
• Molecular Mass: The recombinant human EGFR /GST chimera consists of 780 amino acids and has a calculated molecular mass of 89.1 kDa.
• Endotoxin: < 1.0 EU per μg of the protein as determined by the LAL method.
• Purity: > 85 % as determined by SDS-PAGE
• Storage: Store it under sterile conditions at -20°C to -80°C upon receiving. Recommend to aliquot the protein into smaller quantities for optimal storage. Avoid repeated freeze-thaw cycles.
• Concentration: 0.2-1.0 mg/mL.

Gene Information

• Gene Name: EGFR epidermal growth factor receptor [ Homo sapiens ]
• Official Symbol: EGFR
• Synonyms: EGFR; epidermal growth factor receptor; epidermal growth factor receptor (avian erythroblastic leukemia viral (v erb b) oncogene homolog), ERBB; ERBB1; erythroblastic leukemia viral (v erb b) oncogene homolog (avian); proto-oncogene c-ErbB-1; cell growth inhibiting protein 40; cell proliferation-inducing protein 61; receptor tyrosine-protein kinase erbB-1; avian erythroblastic leukemia viral (v-erb-b) oncogene homolog; ERBB; HER1; mENA; PIG61
• Gene ID: 1956
• mRNA Refseq: NM_005228
• Protein Refseq: NP_005219
• MIM: 131550
• UniProt ID: P00533

Case Study

Case 1: Hallaji M, et al. Sci Rep. 2025

This study explores Fc-fusion peptides (peptibodies) as targeted cancer therapy alternatives to monoclonal antibodies, focusing on EGFR-targeted FcIgG-GE11 developed via phage display. Expressed in E. coli, the peptibody demonstrated high EGFR-binding affinity, dose/time-dependent growth inhibition, and cell cycle arrest in EGFR-overexpressing tumors, mirroring Cetuximab’s anti-cancer effects. MTT assays and In-Cell ELISA confirmed comparable potency to Cetuximab in suppressing Tyr1173 phosphorylation, highlighting its potential for precision oncology and biopharmaceutical innovation.

Fig1. FcIgG-GE11 and Cetuximab did not bind to the negative EGFR cell line.

Fig2. Analysis of EGFR phosphorylation in cells treated with FcIgG-GE11 and Cetuximab.

Case 2: Dabiri M, et al. Protein Expr Purif. 2025

This study tackles EGFR/HER2 dimerization-driven therapeutic resistance in breast cancer by developing a human scFv antibody targeting EGFR’s dimerization interface. The recombinant scFv inhibited EGFR-HER2 interaction, reduced STAT3 phosphorylation, altered Bcl-2/Bax ratios, and suppressed proliferation in EGFR+/HER2+ cancer cells (MCF7, MDA-MB-468, SKOV3) while sparing normal cells. Computational modeling validated its binding specificity, highlighting its potential for precision oncology and targeted cancer therapy against antibody-resistant tumors.

Fig1. Dimerization inhibition by the produced scFv.

Fig2. Cell-ELISA results of the purified scFv against VERO EGFR/HER2 cells.

Application

1. Applications of Recombinant EGFR Protein in Cancer Research and Therapeutics Recombinant EGFR protein plays a pivotal role in advancing targeted cancer therapy and drug discovery. As a key biomarker in EGFR-driven tumors (e.g., breast, lung, and ovarian cancers), it enables high-throughput screening for monoclonal antibodies, small-molecule inhibitors, and peptide-based therapeutics. Its use in cell-based assays validates drug candidates’ ability to block EGFR dimerization, inhibit STAT3 phosphorylation, and modulate Bcl-2/Bax apoptotic pathways, addressing mechanisms behind therapy resistance. 2. Diagnostic and Therapeutic Innovations In diagnostics, recombinant EGFR supports biomarker quantification via ELISA and immunohistochemistry, aiding personalized treatment strategies for EGFR-overexpressing cancers. Therapeutically, it facilitates the design of bispecific antibodies and CAR-T cell therapies targeting EGFR/HER2 heterodimers. Its integration into 3D tumor models and organoid systems further refines preclinical testing, enhancing predictive accuracy for precision oncology. 3. Biopharmaceutical Development and Beyond The protein is critical for optimizing phage display libraries to isolate high-affinity binders and engineer scFv fragments with minimal off-target effects. Additionally, it underpins studies on EGFR signaling crosstalk with pathways like MAPK/ERK, informing combination therapies. As a tool for cancer vaccine development, recombinant EGFR aids in eliciting immune responses against tumor-specific epitopes, solidifying its role in next-generation biotherapeutics.

Fig1. Viruses modulate the EGFR signaling network. (Se Sil Noh, 2023)