Human EGFRvIII (EGI-H52H4) is expressed from human HEK293 cells. It contains AA Leu 25 - Ser 645 (Accession # NP_005219.2) while the amino acids 30-297 are missing.
Predicted N-terminus: Leu 25
This protein carries a polyhistidine tag at the C-terminus.
The protein has a calculated MW of 40.5 kDa. The protein migrates as 60-70 kDa under reducing (R) condition (SDS-PAGE) due to glycosylation.
Less than 1.0 EU per μg by the LAL method.
>95% as determined by SDS-PAGE.
Lyophilized from 0.22 μm filtered solution in PBS, pH7.4. Normally trehalose is added as protectant before lyophilization.
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Please see Certificate of Analysis for specific instructions.
For best performance, we strongly recommend you to follow the reconstitution protocol provided in the CoA.
For long term storage, the product should be stored at lyophilized state at -20°C or lower.
Please avoid repeated freeze-thaw cycles.
No activity loss is observed after storage at:
- 4-8°C for 12 months in lyophilized state;
- -70°C for 3 months under sterile conditions after reconstitution.
Human EGFRvIII, His Tag on SDS-PAGE under reducing (R) condition. The gel was stained overnight with Coomassie Blue. The purity of the protein is greater than 95%.
The epidermal growth factor receptor (EGFR; ErbB-1; HER1 in humans) is the cell-surface receptor for members of the epidermal growth factor family (EGF-family) of extracellular protein ligands. The epidermal growth factor receptor is a member of the ErbB family of receptors, a subfamily of four closely related receptor tyrosine kinases: EGFR (ErbB-1), HER2/c-neu (ErbB-2), Her 3 (ErbB-3) and Her 4 (ErbB-4). Mutations affecting EGFR expression or activity could result in cancer. The type III EGF deletion-mutant receptor (EGFRvIII) is the most common mutation and was first identified in primary human glioblastoma tumors; EGFR gene amplification is correlated with the structural rearrangement of the gene. The EGFRvIII gene has an in-frame deletion of 801 base pairs, corresponding to exons 2–7 in the mRNA, resulting in the deletion of amino acids 30-297 in the extracellular domain and the generation of a glycine at the fusion point
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