Detects human EGF R/ErbB1 in ELISAs and Western blots. In ELISAs, this antibody shows less than 3% cross-reactivity with recombinant mouse EGF R 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 EGF R Leu25-Ser645 Accession # CAA25240
Lyophilized from a 0.2 μm filtered solution in PBS with BSA as a carrier protein.
Detection of EGF R/ErbB1 in A431 Human Cell Line by Flow Cytometry. A431 human epithelial carcinoma cell line was stained with Human EGF R/ErbB1 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.
Background: EGF R/ErbB1
The epidermal growth factor receptor (EGF R) subfamily of receptor tyrosine kinases comprises four members: EGF R (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 EGF R 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. EGF R 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 EGF R homodimerization as well as heterodimerization with ErbB2, resulting in kinase activation, tyrosine phosphorylation and cell signaling. EGF R can also be recruited to form heterodimers with the ligand-activated ErbB3 or ErbB4. EGF R signaling has been shown to regulate multiple biological functions including cell proliferation, differentiation, motility and apoptosis. In addition, EGF R 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.
Epidermal Growth Factor Receptor/Receptor Tyrosine Protein Kinase ErbB1
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The data collected includes not only links to publications in PubMed,
but also provides information about sample types, species, and experimental conditions.
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