EGFR was detected in immersion fixed frozen sections of human skin using Goat Anti-Human EGFR Antigen Affinity-purified Polyclonal Antibody (Catalog # AF231) at 1 µg/mL for 1 hour at room temperature ...read more
EGFR was detected in immersion fixed A431 human epithelial carcinoma cell line using Goat Anti-Human EGFR Antigen Affinity-purified Polyclonal Antibody (Catalog # AF231) at 1 µg/mL for 3 hours at room ...read more
Western blot shows lysates of HeLa human cervical epithelial carcinoma cell line and MDA‑MB‑231 human breast cancer cell line. PVDF membrane was probed with 1 µg/mL of Goat Anti-Human EGFR Antigen ...read more
A431 human epithelial carcinoma cell line was stained with Goat Anti-Human EGFR Antigen Affinity-purified Polyclonal Antibody (Catalog # AF231, filled histogram) or isotype control antibody (Catalog # AB-108-C, ...read more
Mouse myeloma cell line NS0-derived recombinant human EGFR Leu25-Ser645 Accession # CAA25240
Detects human EGFR in ELISAs and Western blots. In sandwich ELISAs, approximately 3% cross-reactivity with recombinant mouse EGFR is observed and less than 0.1% cross-reactivity with recombinant human (rh) ErbB2 and rhErbB3 is observed.
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The epidermal growth factor receptor (EGFR) subfamily of receptor tyrosine kinases comprises four members: EGFR (also known as HER1, ErbB1 or ErbB), ErbB2 (Neu, HER2), ErbB3 (HER3), and ErbB4 (HER4). All family members are type I transmembrane glycoproteins that have an extracellular domain which contains two cysteine-rich domains separated by a spacer region that is involved in ligand binding, and a cytoplasmic domain which has a membrane-proximal tyrosine kinase domain and a C-terminal tail with multiple tyrosine autophosphorylation sites. The human EGFR gene encodes a 1210 amino acid (aa) residue precursor with a 24 aa putative signal peptide, a 621 aa extracellular domain, a 23 aa transmembrane domain, and a 542 aa cytoplasmic domain. EGFR has been shown to bind a subset of the EGF family ligands, including EGF, amphiregulin, TGF-alpha, betacellulin, epiregulin, heparin-binding EGF and neuregulin-2 alpha in the absence of a co-receptor. Ligand binding induces EGFR homodimerization as well as heterodimerization with ErbB2, resulting in kinase activation, tyrosine phosphorylation and cell signaling. EGFR can also be recruited to form heterodimers with the ligand-activated ErbB3 or ErbB4. EGFR signaling has been shown to regulate multiple biological functions including cell proliferation, differentiation, motility and apoptosis. In addition, EGFR signaling has also been shown to play a role in carcinogenesis (1 - 3).
Daly, R.J. (1999) Growth Factors, 16:255.
Schlessinger, J. (2000) Cell. 103:211.
Maihle, N.J. et al. (2002) Cancer Treat. Res. 107:247.
This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed for 1 year from date of receipt.
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Using EGF Protein from Novus Biologicals EGF (epidermal growth factor) stimulates differentiation, proliferation and cell growth by binding to its receptor, EGFR. EGF was first discovered in the mouse submandibular gland in 1986 by Stanley Cohen of Vanderbilt University, leading to a Nobel P... Read full blog post.
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