Recombinant Human EGFR His-tag Protein, CF Summary
Leu25-Ser645, with a C-terminal 6-His tag
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.
|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.
When Human EGFR (Research Grade Cetuximab Biosimilar) Antibody (MAB9577) is immobilized at 1 µg/mL (100 µL/well), Recombinant Human EGFR His-tag (Catalog # 11302-ER) binds with an ED50 of 1.25-15.0 ng/mL.
2 μg/lane of Recombinant Human EGFR His-tag Protein (Catalog # 11302-ER) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 94-104 kDa.
Epidermal growth factor receptor (EGFR), also known as HER-1 and ErbB1, is a member of a subfamily of receptor tyrosine kinases comprised of four members: EGFR, ErbB2 (Neu, HER-2), ErbB3 (HER-3), and ErbB4 (HER-4). All family members are type I transmembrane glycoproteins with an extracellular domain (ECD) containing two cysteine-rich domains separated by a spacer region and a cytoplasmic domain containing a tyrosine kinase domain followed by multiple tyrosine autophosphorylation sites (1, 2). Several soluble isoforms lacking the intracellular domain are generated by alternate splicing, along with a tumor specific mutant EGFRvIII, are known to exist (3-5). The ECD of mature, full-length EGFR shares 88% and 89% amino acid sequence identity with mouse and rat EGFR, respectively. 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 (6-8). 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 (6-8). EGFR is overexpressed in a wide variety of tumors, with EGFRvIII overexpressed particularly in glioblastoma multiforme (GMB) and is the target of several anti-cancer therapeutics (5,9,10).
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