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Email: info@nsjbio.com
- Tel: 858.663.9055
- Email: info@nsjbio.com
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EGFR is a transmembrane receptor tyrosine kinase that dimerizes upon ligand binding (e.g., EGF, TGF-α), triggering autophosphorylation and activation of downstream pathways including RASâMAPK/ERK and PI3KâAKTâmTOR. Through these cascades, EGFR regulates proliferation, survival, differentiation, and migration across epithelial and stromal compartments. EGFR is also known as ErbB1/HER1 and forms homo- or heterodimers with other ErbB family members to fine-tune signaling outputs.
Dysregulated EGFR activityâvia gene amplification, overexpression, or activating mutationsâdrives oncogenic signaling in lung, colorectal, head and neck, and glioblastoma settings. EGFR status is routinely assessed to guide targeted therapies, and phospho-EGFR measurements inform pathway engagement and drug response. Beyond oncology, EGFR contributes to tissue repair, fibrosis, and inflammatory signaling, making it broadly relevant to both basic and translational research.
The EGF Receptor antibody enables specific detection of endogenous EGFR in applications such as western blot, immunohistochemistry, immunofluorescence, and flow cytometry, supporting both total and phospho-protein workflows when paired with appropriate reagents. Researchers use the EGF Receptor antibody to quantify expression levels, map subcellular localization at membranes and endosomes, and monitor pathway modulation under genetic or pharmacologic perturbations. With high specificity and consistent performance across diverse sample types, the EGF Receptor antibody is a reliable choice for studies of receptor signaling and therapeutic response.
Optimal dilution of the EGF Receptor antibody should be determined by the researcher.
Recombinant human protein (amino acids N36-N497) was used as the immunogen for the EGF Receptor antibody.
After reconstitution, the EGF Receptor antibody can be stored for up to one month at 4oC. For long-term, aliquot and store at -20oC. Avoid repeated freezing and thawing.
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