Recombinant Human EGFR Isoform vIII Fc Avi-tag Protein, CF Summary
|Human EGFR Isoform vIII|
Accession # NP_001333870.1
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 Isoform vIII antibody (Novus Catalog # BNP-50599) is immobilized at 0.1 μg/mL (100 μL/well), Biotinylated Recombinant Human EGFR Isoform vIII Fc Chimera Avi-tag (AVI10494) binds with an ED50 of 25-150 ng/mL.
2 μg/lane of Biotinylated Recombinant Human EGFR Isoform vIII Fc Avi-tag Protein (AVI10494) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 95-115 kDa and 190-230 kDa, respectively.
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 (3‑4). EGFRvIII is a tumor‐specific mutation that results from an in‐frame deletion removing 267 amino acids from the ECD and insertion of a glycine residue (5). EGFRvIII has a molecular mass of approximately 145 kDa and has been shown to have weaker activity than full-length EGFR (6). 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 (7‑9). 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 (7-9). 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 (5,10,11). Our Avi-tag Biotinylated Recombinant Human EGFRvIII features biotinylation at a single site contained within the Avi-tag, a unique 15 amino acid peptide. Protein orientation will be uniform when bound to streptavidin-coated surface due to the precise control of biotinylation and the rest of the protein is unchanged so there is no interference in the protein's bioactivity.
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Citation for Recombinant Human EGFR Isoform vIII Fc Avi-tag Protein, CF
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1 Citation: Showing 1 - 1
A Rational Designed Novel Bispecific Antibody for the Treatment of GBM
Authors: R Sun, Y Zhou, L Han, Z Pan, J Chen, H Zong, Y Bian, H Jiang, B Zhang, J Zhu
Applications: Surface Plasmon Resonance (SPR
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