EGF Receptor vIII (D6T2Q) XP® Rabbit mAb (BSA and Azide Free) #93186
- IHC
- IF
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
This formulation is ideal for use with technologies requiring specialized or custom antibody labeling, including fluorophores, metals, lanthanides, and oligonucleotides. It is not recommended for ChIP, ChIP-seq, CUT&RUN or CUT&Tag assays. If you require a carrier free formulation for chromatin profiling, please contact us. Optimal dilutions/concentrations should be determined by the end user.
BSA and Azide Free antibodies are quality control tested by size exclusion chromatography (SEC) to determine antibody integrity.
Formulation
For standard formulation of this product see product #64952.
Storage
Specificity / Sensitivity
Species Reactivity:
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).
- Hackel, P.O. et al. (1999) Curr Opin Cell Biol 11, 184-9.
- Zwick, E. et al. (1999) Trends Pharmacol Sci 20, 408-12.
- Cooper, J.A. and Howell, B. (1993) Cell 73, 1051-4.
- Hubbard, S.R. et al. (1994) Nature 372, 746-54.
- Biscardi, J.S. et al. (1999) J Biol Chem 274, 8335-43.
- Emlet, D.R. et al. (1997) J Biol Chem 272, 4079-86.
- Levkowitz, G. et al. (1999) Mol Cell 4, 1029-40.
- Ettenberg, S.A. et al. (1999) Oncogene 18, 1855-66.
- Rojas, M. et al. (1996) J Biol Chem 271, 27456-61.
- Feinmesser, R.L. et al. (1999) J Biol Chem 274, 16168-73.
- Sugawa, N. et al. (1990) Proc Natl Acad Sci U S A 87, 8602-6.
- Wong, A.J. et al. (1992) Proc Natl Acad Sci U S A 89, 2965-9.
- Padfield, E. et al. (2015) Front Oncol 5, 5.
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