EGFR
The epidermal growth factor receptor (EGFR; ErbB1) is a member of the epidermal growth factor RTK (receptor tyrosine kinases) family, which also includes HER2/neu (ErbB2), ErbB3 (HER3), and ErbB4 (HER4). The EGFR is present at the cell surface and composed of an extracellular ligand-binding ectodomain, a single chain transmembrane domain, and an intracellular tyrosine kinase domain. Multiple ligands bind to and activate the EGFR, including epidermal growth factor (EGF), transforming growth factor (TGF-α), amphiregulin, heparin-binding EGF, and betacellulin.
After ligand binding, the receptors form homo- or heterodimeric complexes activating the tyrosine kinase domain. The dimerization and autophosphorylation of EGFR result in a series of intracellular signaling events that involve activation of the Ras-Raf-MAP kinase, PI-3K/Akt, PKC, and Stat/Jak pathways. Activation of the EGFR is involved in regulating cellular proliferation, differentiation, and survival. Driven largely by its role in promoting cell proliferation and opposing apoptosis, the EGFR has been vilified as a proto-oncogene.
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EGFR Recombinant Proteins (46)
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Inhibitors & Agonists (352)
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Recombinant Protein Expression Service
- Codon Optimization
- Gene Synthesis
- Construction of Expression Vector
- Strain Screening
- Protein Expression
- Purification & QC
- Protein Delivery
- Fòrmula: Human
- Peso molecular: Sf9 insect cells
The EpCAM/TROP1 protein serves as an important homogeneous interacting molecule that promotes direct contact between intestinal epithelial cells (IEC) and intraepithelial lymphocytes (IEL) in the mucosal epithelium. This feature helps establish an immune barrier against mucosal infections. EpCAM/TROP1 Protein, Human (His-SUMO) is the recombinant human-derived EpCAM/TROP1 protein, expressed by E. coli , with N-6*His, N-SUMO labeled tag.
