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PDP - Template Name: Monoclonal Antibody
PDP - Template ID: *******c5e4b77
R Recombinant
Recombinant: Superior lot-to-lot consistency, continuous supply, and animal-free manufacturing.

EGF Receptor vIII (D6T2Q) XP® Rabbit mAb #64952

Filter:
  • IHC
  • IF
Immunohistochemistry Image 1: EGF Receptor vIII (D6T2Q) XP® Rabbit mAb
Immunohistochemical analysis of paraffin-embedded human glioblastoma using EGF Receptor vIII (D6T2Q) XP® Rabbit mAb.

To Purchase # 64952

Cat. # Size Qty. Price Ships
64952T 20 µl
$190
64952S 100 µl
$464

Supporting Data

REACTIVITY H
SENSITIVITY Endogenous (IHC-P), Transfected (IF)
MW (kDa)
Source/Isotype Rabbit IgG
Application Key:
  • IHC-Immunohistochemistry 
  • IF-Immunofluorescence 
Species Cross-Reactivity Key:
  • H-Human 

Product Information

Product Usage Information

Application Dilution
Immunohistochemistry (Paraffin) 1:200
Immunofluorescence (Immunocytochemistry) 1:3200

Storage

Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA, 50% glycerol and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the antibody.

For a carrier free (BSA and azide free) version of this product see product #93186.

Protocol

Specificity / Sensitivity

EGF Receptor vIII (D6T2Q) XP® Rabbit mAb recognizes endogenous and transfected levels of EGF Receptor vIII protein by immunohistochemistry and immunofluorescence, respectively.

Species Reactivity:

Human

Source / Purification

Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues near the amino terminus of human EGF Receptor vIII protein.

Background

The epidermal growth factor (EGF) receptor is a transmembrane tyrosine kinase that belongs to the HER/ErbB protein family. Ligand binding results in receptor dimerization, autophosphorylation, activation of downstream signaling, internalization, and lysosomal degradation (1,2). Phosphorylation of EGF receptor (EGFR) at Tyr845 in the kinase domain is implicated in stabilizing the activation loop, maintaining the active state enzyme, and providing a binding surface for substrate proteins (3,4). c-Src is involved in phosphorylation of EGFR at Tyr845 (5). The SH2 domain of PLCγ binds at phospho-Tyr992, resulting in activation of PLCγ-mediated downstream signaling (6). Phosphorylation of EGFR at Tyr1045 creates a major docking site for the adaptor protein c-Cbl, leading to receptor ubiquitination and degradation following EGFR activation (7,8). The GRB2 adaptor protein binds activated EGFR at phospho-Tyr1068 (9). A pair of phosphorylated EGFR residues (Tyr1148 and Tyr1173) provide a docking site for the Shc scaffold protein, with both sites involved in MAP kinase signaling activation (2). Phosphorylation of EGFR at specific serine and threonine residues attenuates EGFR kinase activity. EGFR carboxy-terminal residues Ser1046 and Ser1047 are phosphorylated by CaM kinase II; mutation of either of these serines results in upregulated EGFR tyrosine autophosphorylation (10).

EGFR variant III (EGFRvIII) is a truncated, constitutively active mutant form of EGFR that results from an in-frame deletion of exons 2-7 (11,12). EGFRvIII is expressed in various cancers, most notably glioblastoma, where it is expressed at a frequency of 25-30%. Although complicated by the fact that it is often co-expressed with amplified EGFR, EGFRvIII is a potential therapeutic target (13).

Pathways

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