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MilliporeSigma™ anti-EGFR Ab-2, Polyclonal, ™ (Upstate™) Non-distribution product as customer accommodation.

Manufacturer:  MilliporeSigma™ 06847/DEL

Catalog No. 50-172-142

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Description

Description

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. GenBank Number: NM_005228. MW: 180kDa.

Immunoprecipitation, Western Blotting

Abbreviations: AP=Affinity Purification, ChIP=Chromatin IP, CM=Confocal Microscopy, DB=Dot Blot, EIA=ELISA, EM=Electron Microscopy, FC=Flow Cytometry, GS=Gel Supershift, IC=Immunocytochemistry, IF=Immunofluorescence, IH=Immunohistology/Immunohistochemistry, IP=Immunoprecipitation, IPK=IP Kinase Assay, KA=Kinase Assay, NEUT=Neutralization, PIA=Peptide Inhibition Assay, RIA=Radioimmunossay, TCA=T Cell Activation, WB=Western Blotting, Species: Am=Amphibian, Av=Avian, B=Bovine, Ca=Cat ,Ck=Chicken, D=Dog, Dr=Deer, Ds=Drosophila, El=Elk, Fg=Frog, Fs=Fish, Ft=Ferret, G=Goat, Gp=Guinea Pig, H=Horse, Hm=Hamster, Hu=Human, K=Kangaroo, Ms=Mouse, Nhp=Non-Human Primate, O=Ovine, P=Porcine, Rb=Rabbit, Rp=Reptile, Rt=Rat, Ys=Yeast, Xn=Xenopus, (wk)=cross reacts weakly

Specifications

Specifications

EGFR
Semi-purified
Ovalbumin-conjugated synthetic peptide (ETKPNGIFKGPTAENAEYLRVAPPSSEFIGA) corresponding to amino acids 1156-1186 of the processed mouse EGF receptor C-terminal domain
200μg
Cell Signaling
Polyclonal
Unconjugated
Rabbit
IgG
RUO
Primary
Hamster, Human, Murine, Rat
Documents
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