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Description
Epidermal Growth Factor (EGF) elicits a variety of cellular responses that are initiated by EGF Receptor (EGFR) binding and activation of intrinsic tyrosine kinase activity. EGFR, also known as ErbB1 or HER1, is a member of the ErbB class of receptor protein tyrosine kinases. It has an extracellular ligand-binding domain, a single transmembrane region, and a cytoplasmic region containing a protein tyrosine kinase domain and a c-terminal regulatory domain with many phosphorylation sites. Following ligand binding, EGFR forms homodimers and heterodimers with ErbB2. Specific C-terminal tyrosine residues are then autophosphorylated and, in turn, bind to adaptor proteins, kinases, or protein tyrosine phosphatases. In addition, c-Src-dependent phosphorylations at other sites, such as tyrosine 845 (Y845) in the kinase domain, regulate the receptor's kinase activity. Inappropriate expression or mutations of EGFR and/or deregulation of its signaling pathways are associated with many types of cancer, making EGFR a promising target for cancer therapies. The 12A3 monoclonal antibody recognizes the phosphorylated Y845 in the protein tyrosine kinase domain of human EGFR.
Intracellular Staining
Specifications
Specifications
| Antigen | EGF Receptor (pY845) |
| Applications | Flow Cytometry |
| Classification | Monoclonal |
| Clone | 12A3 |
| Conjugate | Alexa Fluor 647 |
| Formulation | Aqueous buffered solution containing BSA and ≤0.09% sodium azide. |
| Host Species | Mouse |
| Immunogen | Phosphorylated Human EGF Receptor Peptide |
| Purification Method | Affinity Purified |
| Quantity | 50 Tests |
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