Anti-EGFR (cytoplasmic domain) Antibody, clone 8G6.2

Evaluated by western blot on A431 cell lysate
Western Blot Analysis:
1:2,000 dilution of this antibody was used to detect EGFR in A431 cell lysate.

Detect EGFR (cytoplasmic domain) using this Anti-EGFR (cytoplasmic domain) Antibody, clone 8G6.2 validated for use in IC, IH, IP & WB.

Immunocytochemistry Analysis:
A431 cells were grown, fixed, permeablized, and stained with anti-EGFR, clone 8G6.2

Confocal Immunocytochemistry Analysis:
A431 cells were grown, fixed, permeablized, and stained with anti-EGFR, clone 8G6.2

Immunoprecipitation:
100 μg of A431 whole cell lysate was lysed in RIPA buffer and immunoprecipitated (IP) with 5 μg of Anti-EGFR, cytoplasmic domain, clone 8G6.2

Immunohistochemistry Analysis:
Tissue was stained with anti-EGFR, cytoplasmic domain, clone 8G6.2 at a 1:100 dilution and IHC-Select Detection with HRP-DAB reagents.

This antibody detects the cytoplasmic domain of EGFR.

180 kDa

The epidermal growth factor receptor (EGFR; ErbB-1; HER1 in humans) is the cell-surface receptor for members of the epidermal growth factor family (EGF-family) of extracellular protein ligands. The epidermal growth factor receptor is a member of the ErbB family of receptors, a subfamily of four closely related receptor tyrosine kinases: EGFR (ErbB-1), HER2/c-neu (ErbB-2), Her 3 (ErbB-3) and Her 4 (ErbB-4). Mutations affecting EGFR expression or activity could result in cancer. EGFR (epidermal growth factor receptor) exists on the cell surface and is activated by binding of its specific ligands, including epidermal growth factor and transforming growth factor alpha (TGFα). Upon activation by its growth factor ligands, EGFR undergoes a transition from an inactive monomeric form to an active homodimer. In addition to forming homodimers after ligand binding, EGFR may pair with another member of the ErbB receptor family, such as ErbB2/Her2/neu, to create an activated heterodimer. There is also evidence to suggest that clusters of activated EGFRs form, although it remains unclear whether this clustering is important for activation itself or occurs subsequent to activation of individual dimers. EGFR dimerization stimulates its intrinsic intracellular protein-tyrosine kinase activity. As a result, autophosphorylation of five tyrosine (Y) residues in the C-terminal domain of EGFR occurs. These are Y992, Y1045, Y1068, Y1148 and Y1173. This autophosphorylation elicits downstream activation and signaling by several other proteins that associate with the phosphorylated tyrosines through their own phosphotyrosine-binding SH2 domains. These downstream signaling proteins initiate several signal transduction cascades, principally the MAPK, Akt and JNK pathways, leading to DNA synthesis and cell proliferation. Such proteins modulate phenotypes such as cell migration, adhesion, and proliferation. The kinase domain of EGFR can also cross-phosphorylate tyrosine residues of other receptors it is aggregated with, and can itself be activated in that manner.

Recombinant protein encoding the cytoplasmic domain (C-terminal) of human EGF Receptor.

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

Replaces: 04-338

Format: Purified