Egfr Antigen
Egfr Antigen - Related Videos
06:57
Development of an Antigen-driven Colitis Model to Study Presentation of Antigens by Antigen Presenting Cells to T Cells
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Cited by 9 •
2016
In this antigen-driven colitis model, OT-II CD4+ T cells expressing a red fluorescent protein were adoptively transferred into RAG-/- mice that express a green fluorescent protein in mononuclear phagocytes (MPs). The hosts were challenged with Escherichia coli (E.coli) expressing the ovalbumin protein (OVA) fused to a cyan fluorescent protein (CFP).
08:12
Identification of EGFR and RAS Inhibitors using Caenorhabditis elegans
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Cited by 4 •
2020
The genetically tractable nematode Caenorhabditis elegans can be used as a simple and inexpensive model for drug discovery. Described here is a protocol to identify anticancer therapeutics that inhibit the downstream signaling of RAS and EGFR proteins.
05:04
Viral Antigen Microarray Assay to Detect Antibody Isotypes in Serum Against Viral Antigen
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2025
In this video, we demonstrate the process for detecting antibody isotypes in multiple human serum samples using a microarray slide printed with antigenic subtypes of influenza virus strains.
09:38
Establishing Dual Resistance to EGFR-TKI and MET-TKI in Lung Adenocarcinoma Cells In Vitro with a 2-step Dose-escalation Procedure
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Cited by 4 •
2017
An in vitro method for establishing dual resistance to an EGFR-TKI and a MET-TKI in cancer cells is described. This method is useful for developing treatments for patients with EGFR-mutations, who exhibit disease progression despite EGFR-TKI treatment with MET-amplification. It can also be modified for inhibitors targeting other molecules.
02:41
B Cell Activation on an Antigen-Coated Coverslip
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2025
This video demonstrates B cell activation in vitro. The process involves antigen interaction with B cell receptors, leading to cytoskeleton remodeling, immune synapse formation, lysosome movement, antigen internalization, processing, and subsequent presentation on MHC molecules for B cell activation.
FAQs
Phosphorylation indicates that receptor engagement has progressed into intracellular signaling rather than merely reflecting receptor presence at the cell surface. EGFR-associated activation can be examined in relation to the RAS–RAF–MEK–ERK and PI3K–AKT pathways, which connect receptor status with proliferation, survival, differentiation, and tissue repair. This distinction helps separate expression measurements from functional signaling outcomes.
Antigenic regions provide molecular targets that antibodies can recognize on the epidermal growth factor receptor. Examining this recognition helps researchers assess whether an antibody-based reagent detects EGFR in relevant cells and supports interpretation of receptor-expression patterns. Such information can contribute to biomarker development and disease classification, especially when receptor status has biological or clinical significance.
Changes in EGFR expression may indicate that host cells are responding differently during inflammation or contact with a pathogen. Measuring receptor abundance alongside signaling changes can help distinguish altered receptor availability from altered downstream activity. In immunology and infection research, this comparison provides context for understanding how host-cell regulatory systems are affected during disease-related interactions.
An EGFR antigen measurement primarily addresses whether antigenic receptor regions are present and recognizable, whereas pathway analysis addresses signaling consequences associated with receptor activation. A sample may therefore provide information about receptor expression or antibody binding without directly establishing downstream activity. Using both types of readout gives a more complete view of receptor status and function.
EGFR-targeting antibodies can be used to examine receptor expression and antibody recognition in cells or tissue-related samples. Their results may help classify disease states, identify EGFR-associated patterns, and investigate signaling changes linked to inflammation, infection, or abnormal receptor activity. The value of the measurement depends on interpreting binding or expression findings in their biological context.
The receptor connects immune or pathogen-associated conditions with host-cell behaviors such as survival, proliferation, differentiation, and tissue repair. Investigators can study whether inflammation or pathogen interaction changes EGFR expression or associated signaling. These observations help place receptor biology within a host-response framework rather than treating antigen recognition as an isolated antibody-binding event.
EGFR antigen measurements can support biomarker development and disease classification by identifying receptor-related patterns in samples. When abnormal EGFR activity contributes to cancer, antibody-based recognition and related analyses also help investigate therapeutic strategies directed at the receptor. These applications link molecular detection with interpretation of disease biology and the evaluation of immune-based approaches.