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Anti-EGFR Antibody, neutralizing, clone LA1
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REFERENCES
Studies of cell signaling in a reconstructed human epidermis exposed to sensitizers: IL-8 synthesis and release depend on EGFR activation.
Frankart, Aurélie, et al. (2012) Archives of dermatological research, (2012)
EGFR and EphA2 are host factors for hepatitis C virus entry and possible targets for antiviral therapy.
Lupberger, Joachim, et al. (2011) Nature medicine, (2011)
Mutant p53 initiates a feedback loop that involves Egr-1/EGF receptor/ERK in prostate cancer cells.
L Sauer,D Gitenay,C Vo,V T Baron (2010) Oncogene.29
Dexamethasone and methylprednisolone do not inhibit neuritic outgrowth while inhibiting outgrowth of fibroblasts from spiral ganglion explants.
Alexis Furze,Deanna Kralick,Anand Vakharia,Korey Jaben,Reid Graves,Eelam Adil,Adrien A Eshraghi,Thomas J Balkany,Thomas R Van de Water (2008) Acta oto-laryngologica.128
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Species Reactivity Key Applications Host Format Antibody Type
H ICC, IP, NEUT, WB Mouse Purified Monoclonal Antibody
Description:
Anti-EGFR Antibody, neutralizing, clone LA1
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Trade Name:
Upstate (Millipore)
Product Overview:
Reacts with external domain of EGF receptor on all human cells. Competes with EGF and TGF-a for binding on human cells.
Specificity:
Recognizes both phosphorylated and non-phosphorylated human EGF receptors.
Molecular Weight:
180 kDa
Immunogen:
Human A431 membrane proteins.
Clone:
LA1
Isotype:
IgG1
Background Information:
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 α (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.
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Species Reactivity:
Human
Control:
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