Recombinant Human EGFR Fc Chimera Avi-tag Protein, CF
Recombinant Human EGFR Fc Chimera Avi-tag Protein, CF Summary
Learn more about Avi-tag Biotinylated ProteinsProduct Specifications
Human EGFR (Leu25-Ser645) Accession # CAA25240.1 | IEGRMD | Human IgG1 (Pro100-Lys330) | Avi-tag |
N-terminus | C-terminus | ||
Product Datasheets
AVI344
Carrier Free
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
AVI344
Formulation | Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. |
Reconstitution | Reconstitute at 500 μg/mL in PBS. |
Shipping | 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.
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Scientific Data
When Human EGFR (Research Grade Cetuximab Biosimilar) Antibody (Catalog # MAB9577) is immobilized at 0.25 µg/mL, 100 µL/well, the concentration of Recombinant Human EGFR Fc Chimera Avi-tag (Catalog # AVI344) that produces 50% of the optimal binding response is approximately 2-15 ng/mL.
2 μg/lane of Biotinylated Recombinant Human EGFR Fc Chimera Avi-tag (Catalog # AVI344) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 110-130 kDa and 220-260 kDa, respectively.
Background: EGFR
The EGFR subfamily of receptor tyrosine kinases comprises four members: EGFR (also known as HER-1, ErbB1, or ErbB), ErbB2 (Neu, HER-2), ErbB3 (HER-3), and ErbB4 (HER-4). All family members are type I transmembrane glycoproteins with an extracellular ligand binding domain containing two cysteine-rich domains separated by a spacer region and a cytoplasmic domain containing a membrane-proximal tyrosine kinase domain followed by multiple tyrosine autophosphorylation sites (1-4). Soluble receptors consisting of the extracellular ligand binding domain are generated by alternate splicing in human and mouse (5‑7). Within the mature ECD, human EGFR shares 88% aa sequence identity with mouse and rat EGFR. Human EGFR shares 43%-44% aa sequence identity with the ECD of human 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 (8‑12). 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 (13, 14). EGFR is overexpressed in a wide variety of tumors and is the target of several anti-cancer drugs (15).
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