The epidermal growth factor receptor (EGFR; Proto-oncogene c-ErbB-1) is a ubiquitously receptor tyrosine kinase that is activated by a variety of ligands including EGF, EPGN, TGFA, and EREG. Ligand-bound EGFR undergoes dimerization and autophosphorylation exposing cytoplasmic domains which allow interaction with adaptor proteins and induction of several signaling pathways including PI3-AKT; PLCγ-PKC; Notch1; and Ras-Raf. EGFR therefore contributes to a diverse range of cellular processes inlcuding cell proliferation. Several studies have reported that EGFR signaling plays an important role in the development of various tumors. EGFR is regulated by PTPRJ and PTPRK phosphatases, and by the endocytic machinery including EPS15 that mediates internalization and degradation of the receptor.

This antibody recognizes the extracellular domain of EGFR.

Partially purified human EGFR from A431 cells

Anti-EGFR Antibody, clone 528 (Azide-free) detects level of EGFR & has been published & validated for use in Immunoprecipitation, Neutralizing.

Neutralizing Assay Analysis: A representative lot was used by an independent laboratory in A431 cells. (Kawamoto, T., et al. (1984). Journal of Biological Chemistry. 259(12):7761-7766.)

Evaluated by Immunoprecipitation in A431 cell lysate.

Immunoprecipitation Analysis: 10 µg of this antibody immunoprecipitated EGFR from A431 cell lysate.

~170 kDa observed. Uniprot gives a calculated molecular weight of 135 but can be observed at ~170 kDa due to phosphorylation. (Konishi, A., et al. (2003). The Journal of Biological Chemistry. 278(37):35049–35056.)

Replaces: 04-338

Format: Purified

Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.