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Description
Biotinylated EGFRvIII His&Avi Tag Protein, HumanProduct Specification Species Human Synonyms EGFRvIII, ERBB, ERBB1, HER1, mENA, NISBD2, PIG61 Accession NP_001333870. 1 Amino Acid Sequence Leu25 Ser378, with C terminal His and Avitag Expression System HEK293 Molecular Weight 60 75kDa (Reducing) Purity 95% by SDS PAGE Endotoxin <1EU g Conjugation Biotin Tag Avi Tag, His Tag Physical Appearance Lyophilized Powder Storage Buffer PBS, pH7. 4. Reconstitution Reconstitute at 0. 1 1 mg ml according to the
Product Specification
| Species | Human |
| Synonyms | EGFRvIII, ERBB, ERBB1, HER1, mENA, NISBD2, PIG61 |
| Accession | NP_001333870.1 |
| Amino Acid Sequence | Leu25-Ser378, with C-terminal His and Avitag |
| Expression System | HEK293 |
| Molecular Weight | 60-75kDa (Reducing) |
| Purity | ＞95% by SDS-PAGE |
| Endotoxin | <1EU/μg |
| Conjugation | Biotin |
| Tag | Avi Tag, His Tag |
| Physical Appearance | Lyophilized Powder |
| Storage Buffer | PBS, pH7.4. |
| Reconstitution | Reconstitute at 0.1-1 mg/ml according to the size in ultrapure water after rapid centrifugation. |
| Stability & Storage | · 12 months from date of receipt, lyophilized powder stored at -20 to -80℃. · 3 months, -20 to -80℃ under sterile conditions after reconstitution. · 1 week, 2 to 8℃ under sterile conditions after reconstitution. · Please avoid repeated freeze-thaw cycles. |
| Reference | 1. Hui K. Gan,The epidermal growth factor receptor variant III (EGFRvIII):where wild things are altered,the FEBS journal,Received 2 April 2013, revised 10 June 2013, accepted 13 June 2013 |
Background
The epidermal growth factor receptor (EGFR) is overexpressed in a variety of human epithelial tumors, often as a consequence of gene amplification. Tumors with EGFR gene amplification frequently contain EGFR gene rearrangements, with the most common extracellular domain mutation being EGFRvIII. This mutation leads to a deletion of exons 2–7 of the EGFR gene and renders the mutant receptor incapable of binding any known ligand. Despite this, EGFRvIII displays low-level constitutive signaling that is augmented by reduced internalization and downregulation. Aberrant EGFRvIII signaling has been shown to be important in driving tumor progression and often correlates with poor prognosis. It is clear that EGFRvIII is expressed in a considerable proportion of patients with glioblastoma multiforme (GBM). The presence of EGFRvIII in other tumor types, however, remains controversial.
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