Detects human EGFR in ELISAs and Western blots. In ELISAs, this antibody shows less than 3% cross-reactivity with recombinant mouse EGFR and less than 0.1% cross-reactivity with recombinant human (rh) EGF, rhErbB2, and rhErbB3.
Polyclonal Goat IgG
Mouse myeloma cell line NS0-derived recombinant human EGFR Leu25-Ser645 Accession # CAA25240
Lyophilized from a 0.2 μm filtered solution in PBS with BSA as a carrier protein.
Detection of EGFR in A431 Human Cell Line by Flow Cytometry. A431 human epithelial carcinoma cell line was stained with Human EGFR Biotinylated Antigen Affinity‑purified Polyclonal Antibody (Catalog # BAF231, filled histogram) or control antibody (Catalog # BAF108, open histogram), followed by Streptavidin-Allophycocyanin (Catalog # F0050).
Preparation and Storage
Reconstitute at 0.2 mg/mL in sterile PBS.
The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage
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.
The epidermal growth factor receptor (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 that have an extracellular domain which contains two cysteine-rich domains separated by a spacer region that is involved in ligand binding, and a cytoplasmic domain which has a membrane-proximal tyrosine kinase domain and a C-terminal tail with multiple tyrosine autophosphorylation sites. The human EGFR gene encodes a 1210 amino acid (aa) residue precursor with a 24 aa putative signal peptide, a 621 aa extracellular domain, a 23 aa transmembrane domain, and a 542 aa cytoplasmic domain. EGFR has been shown to bind a subset of the EGF family ligands, including EGF, amphiregulin, TGF-alpha, betacellulin, epiregulin, heparin-binding EGF and neuregulin-2 alpha in the absence of a co-receptor. Ligand binding induces EGFR homodimerization as well as heterodimerization with ErbB2, resulting in kinase activation, tyrosine phosphorylation and cell signaling. EGFR can also be recruited to form heterodimers with the ligand-activated ErbB3 or ErbB4. EGFR signaling has been shown to regulate multiple biological functions including cell proliferation, differentiation, motility and apoptosis. In addition, EGFR signaling has also been shown to play a role in carcinogenesis (1-3).
Daly, R.J. (1999) Growth Factors, 16:255.
Schlessinger, J. (2000) Cell. 103:211.
Maihle, N.J. et al. (2002) Cancer Treat. Res. 107:247.
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species: Human.We have 1 review tested in 1 application: ELISA.