EGFR Recombinant Protein Antigen

• Reactivity: Hu
• Applications: AC

EGFR Recombinant Protein Antigen Summary

• Description: A recombinant protein antigen with a N-terminal His6-ABP tag corresponding to human EGFR.
  
  

  Source: E. coli

  Amino Acid Sequence: EFKDSLSINATNIKHFKNCTSISGDLHILPVAFRGDSFTHTPPLDPQELDILKTVKEITGFLLIQAWPENRTDLHAFENLEIIRGRTKQHGQFSLAVVSLNITSLGLRSLKEISDGDVIISGNKNLCYANTINWKKLFGTSGQKTKIIS

  Fusion Tag: N-terminal His6ABP (ABP = Albumin Binding Protein derived from Streptococcal Protein G)

  This product is intended to be used as a blocking antigen for antibody competition assays. Any other use of this antigen is done at the risk of the user. The use of this product for commercial production is strictly prohibited. Please contact technical support if you have any questions.

• Source: E. coli
• Protein/Peptide Type: Recombinant Protein Antigen
• Gene: EGFR
• Purity: >80% by SDS-PAGE and Coomassie blue staining

Applications/Dilutions

• Dilutions:
  • Antibody Competition 10 - 100 molar excess
• Application Notes: This recombinant antigen is only intended to be used as a blocking agent to confirm antibody specificity with the corresponding antibody, catalog number NBP1-84815.

  It is purified by IMAC chromatography, and the expected concentration is greater than 0.5 mg/ml.

  For current lot information, including availability, please contact our technical support team click nb-technical@bio-techne.com

• Theoretical MW: 34 kDa.
  Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.

Packaging, Storage & Formulations

• Storage: Store at -20C. Avoid freeze-thaw cycles.
• Buffer: PBS and 1M Urea, pH 7.4.
• Preservative: No Preservative
• Purity: >80% by SDS-PAGE and Coomassie blue staining

Alternate Names for EGFR Recombinant Protein Antigen

• avian erythroblastic leukemia viral (v-erb-b) oncogene homolog
• cell growth inhibiting protein 40
• cell proliferation-inducing protein 61
• EC 2.7.10
• EC 2.7.10.1
• EGF R
• EGFR
• epidermal growth factor receptor (avian erythroblastic leukemia viral (v-erb-b)oncogene homolog)
• epidermal growth factor receptor
• ErbB
• ErbB1
• ERBB1PIG61
• HER1
• HER-1
• mENA
• Proto-oncogene c-ErbB-1
• Receptor tyrosine-protein kinase erbB-1

Background

Epidermal growth factor receptor (EGFR), also known as ErbB1 and HER1, is a type I glycoprotein that belongs the ErbB subfamily of receptor tyrosine kinases (RTKs), which includes ErbB2/HER2, ErbB3/HER3, and ErbB4/HER4 (1,2). EGFR plays an important role in epithelial cell development and homeostasis and as a driver of tumorigenesis in cancer (1,2). The human EGFR is protein 1210 amino acids (aa) in length with a theoretical molecular weight (MW) of 134 kDa (1). The protein consists of a short signal peptide, an extracellular domain (ECD) divided into four subdomains (I-IV), a transmembrane region, an intracellular juxtamembrane segment, a tyrosine kinase domain, and C-terminal tail (1-3). Within the ECD, human EGFR has 88-90% aa sequence identity with mouse and rat EGFR. EGFR has four known specific ligands: EGF, amphiregulin, epigen, and transforming growth factor alpha (TGF-alpha). EGFR ligands betacellulin, epiregulin, and herapin binding (HB)-EGF have dual specificity with ErbB4 (1,3). Ligand binding to the extracellular domain of EFGR leads to receptor homodimerization, or heterodimerization with other ErbB family members, and EGFR activation. This results in subsequent phosphorylation and activation of intracellular signaling pathways, such as MAPK and PI3K/Akt (2,3). EGFR signaling is essential for many cellular processes including proliferation, differentiation, migration, and apoptosis (1,3,5).

In addition to its role in normal development, EGFR mutations or overexpression is observed in many tumors, including breast cancer, non-small cell lung carcinoma (NSCLC), colon cancer, and more (3-6). Small molecule tyrosine kinase inhibitors (TKIs), like gefitinib, erlotinib, and afatinib, have shown great efficacy in treating patients with EGFR activating mutations, especially for NSCLC (4-6). However, most patients eventually develop acquired resistance to TKIs and thus combination and alternative therapies are in development (4-6). A third-generation TKI, osimertinib, is approved for NSCLC patients with resistance to first-line EGFR TKI treatment (6). Additionally, combination therapies of EGFR TKIs with monoclonal antibody immunotherapies, like anti-PD-L1, are being further investigated in clinical trials (6).

References

1. Roskoski R Jr. Small molecule inhibitors targeting the EGFR/ErbB family of protein-tyrosine kinases in human cancers. Pharmacol Res. 2019; 139:395-411. https://doi.org/10.1016/j.phrs.2018.11.014

2. Sigismund S, Avanzato D, Lanzetti L. Emerging functions of the EGFR in cancer. Mol Oncol. 2018; 12(1):3-20. https://doi.org/10.1002/1878-0261.12155

3. Normanno N, De Luca A, Bianco C, et al. Epidermal growth factor receptor (EGFR) signaling in cancer. Gene. 2006; 366(1):2-16. https://doi.org/10.1016/j.gene.2005.10.018

4. Liu Q, Yu S, Zhao W, Qin S, Chu Q, Wu K. EGFR-TKIs resistance via EGFR-independent signaling pathways. Mol Cancer. 2018; 17(1):53. https://doi.org/10.1186/s12943-018-0793-1

5. Harrison PT, Vyse S, Huang PH. Rare epidermal growth factor receptor (EGFR) mutations in non-small cell lung cancer. Semin Cancer Biol. 2020; 61:167-179. https://doi.org/10.1016/j.semcancer.2019.09.015

6. Wu SG, Shih JY. Management of acquired resistance to EGFR TKI-targeted therapy in advanced non-small cell lung cancer. Mol Cancer. 2018; 17(1):38. https://doi.org/10.1186/s12943-018-0777-1

Limitations

This product is for research use only and is not approved for use in humans or in clinical diagnosis. Peptides and proteins are guaranteed for 3 months from date of receipt.

Bioinformatics

• Gene Symbol: EGFR