EGFR Antibody [Biotin] Summary
Mouse myeloma cell line NS0-derived recombinant mouse EGFR
Accession # Q01279
Detects mouse EGFR in Western blots. In Western blots, approximately 20% cross‑reactivity with recombinant human (rh) EGFR is observed and less than 1% cross‑reactivity with rhErbB2, rhErbB3, and rhErbB4 is observed.
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Packaging, Storage & Formulations
|Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 6 months, -20 to -70 °C under sterile conditions after reconstitution.
Lyophilized from a 0.2 μm filtered solution in PBS with BSA as a carrier protein.
Reconstitute at 0.2 mg/mL in sterile PBS.
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for EGFR Antibody [Biotin]
- avian erythroblastic leukemia viral (v-erb-b) oncogene homolog
- cell growth inhibiting protein 40
- cell proliferation-inducing protein 61
- EC 2.7.10
- EC 188.8.131.52
- EGF R
- epidermal growth factor receptor (avian erythroblastic leukemia viral (v-erb-b)oncogene homolog)
- epidermal growth factor receptor
- Proto-oncogene c-ErbB-1
- Receptor tyrosine-protein kinase erbB-1
The EGFR subfamily of receptor tyrosine kinases comprises four members: EGFR (also known as Her1, ErbB1, or ErbB), ErbB2 (Neu, Her2), ErbB3 (Her3), and ErbB4 (Her4). All family members are type I transmembrane glycoproteins. They contain an extracellular ligand binding domain containing two cysteine-rich domains and a cytoplasmic domain containing a membrane-proximal tyrosine kinase domain followed by multiple tyrosine autophosphorylation sites (1, 2). The mouse EGFR cDNA encodes a 1210 amino acid (aa) precursor with a 24 aa signal peptide, a 623 aa extracellular domain (ECD), a 23 aa transmembrane segment, and a 540 aa cytoplasmic domain (3). Soluble receptors consisting of the extracellular ligand binding domain are generated by alternate splicing in human and mouse (4-6). Within the ECD, mouse EGFR shares 88% and 93% aa sequence identity with human and rat EGFR, respectively. It shares 44-48% aa sequence identity with the ECD of mouse ErbB2, ErbB3, and ErbB4. EGFR binds a subset of the EGF family ligands, including EGF, amphiregulin, TGF-alpha, betacellulin, epiregulin, HB-EGF, and epigen (1, 2). Ligand binding induces EGFR homodimerization as well as heterodimerization with ErbB2, resulting in kinase activation, heterodimerization tyrosine phosphorylation and cell signaling (7-11). EGFR can also be recruited to form heterodimers with the ligand-activated ErbB3 or ErbB4. EGFR signaling regulates multiple biological functions including cell proliferation, differentiation, motility, and apoptosis (12, 13). EGFR is over-expressed in a wide variety of tumors and is the target of several anti-cancer drugs (14).
- Singh, A.B. and R.C. Harris (2005) Cell. Signal. 17:1183.
- Shilo, B.Z. (2005) Development 132:4017.
- Avivi, A. et al. (1991) Oncogene 6:673.
- Reiter, J.L. and N.J. Maihle (1996) Nucleic Acids Res. 24:4050.
- Reiter J.L. et al. (2001) Genomics 71:1.
- Xu, Y.H. et al. (1984) Nature 309:806.
- Graus-Porta, D. et al. (1997) EMBO J. 16:1647.
- Yarden, Y. et al. (1987) Biochemistry 26:1434.
- Burgess, A.W. et al. (2003) Mol. Cell 12:541.
- Lemmon, M.A. et al. (1997) EMBO J. 16:281.
- Cohen, S. et al. (1982) J. Biol. Chem. 257:1523.
- Sibilia, M. and E.F. Wagner (1995) Science 269:234.
- Miettinen, P.J. et al. (1995) Nature 376:337.
- Roskoski Jr., R. (2004) Biochem. Biophys. Res. Commun. 319:1.
This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed
for 1 year from date of receipt.
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