Anti-EGFR Antibody, neutralizing, clone LA1

Control
Positive Antigen Control: Catalog #12-301, non-stimulated A431 cell lysate. Add 2.5µL of 2-mercaptoethanol/100µL of lysate and boil for 5 minutes to reduce the preparation. Load 20µg of reduced lysate per lane for minigels.

routinely evaluated on RIPA lysates from non-stimulated human A431 cells

Detect EGFR using this Anti-EGFR Antibody, neutralizing, clone LA1 validated for use in Immuncytochemistry, Immunohistochemistry, Immunoprecipitation, Neutralization, and Western Blotting.

Immunocytochemistry (IC) Analysis: 2μg/mL of a representative lot detected EGFR in A431 cells.
Immunohistochemistry (Paraffin) (IHC) Analysis: A 1:50 dilution of this antibody detected EGFR in Human placenta tissue sections.
Immunoprecipitation Analysis: A representative lot of this antibody immunoprecipitated EGFR in Huh-7.5 cells. (Diao, J., et al. (2012). J. Virol. 86(20); 10935-10949).
Western Blotting Analysis: 1 mg/mL of a representative lot detected EGFR in A431 cell lysate.

Research Category
Signaling

Research Sub Category
Growth Factors & Receptors

Recognizes both phosphorylated and non-phosphorylated human EGF receptors.

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

180 kDa

Epidermal growth factor receptor (UniProt: P00533; also known as EC:2.7.10.1, Proto-oncogene c-ErbB-1, Receptor tyrosine-protein kinase erbB-1) is encoded by the EGFR (also known as ERBB, ERBB1, HER1) gene (Gene ID: 1956) in human. EGFR is a single-pass type I membrane glycoprotein that is ubiquitously expressed. It is synthesized with a signal peptide (1-24), which is subsequently cleaved off to produce the mature form that contains an extracellular domain (aa 25-645), a transmembrane domain (aa 646-668), and a long cytoplasmic domain (669-1210). It possesses receptor tyrosine kinase activity and upon binding of ligands activates several signaling cascades. Ligand binding is known to trigger receptor homo- and/or heterodimerization, which stimulates its intrinsic intracellular protein-tyrosine kinase activity. As a result, autophosphorylation of tyrosine residues in the C-terminal domain of EGFR occurs, which results in activation of several downstream signaling cascades, including the Ras-RAF-MEK-ERK, PI3 kinase-Akt, PLCγ-PKC, and STAT. EGFR phosphorylation at serine 695 is reported to be only partial and occurs only if threonine 693 is phosphorylated. EGFR also undergoes mono and polyubiquitination upon EGF stimulation. However, this ubiquitination does not affect tyrosine kinase activity of the receptor or its signaling capacity. EGFR is commonly overexpressed and is mutated in many human malignancies and is often associated with aggressive phenotypes.

Reacts with external domain of EGF receptor on all human cells. Competes with EGF and TGF-α for binding on human cells.

Human A431 membrane proteins.

Replaces: 04-337; 04-338

Format: Purified

Lyophilized protein G Purified mouse immunoglobulin. Lyophilized from 0.1M Tris-glycine, pH 7.4, 0.15M NaCl containing no preservatives.

Protein G Purified

Lyophilized: 2 years at -20°C; Rehydrated: 1 month at 4°C or 6 months at -20°C

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