EGFR antibody (10R-1765)

Mouse monoclonal EGFR antibody

Synonyms Monoclonal EGFR antibody, Anti-EGFR antibody, HER1 antibody, PIG61 antibody, Avian erythroblastic leukemia viral (verbb) oncogene homolog antibody, Cell growth inhibiting protein 40 antibody, ERBB antibody, ERBB1 antibody, epidermal growth factor receptor antibody, Proto-oncogene c-ErbB-1 antibody, Oncogene ERBB antibody, Urogastrone antibody, Epidermal growth factor receptor antibody, Cell proliferation inducing protein 61 antibody
Specificity EGFR antibody specific for Human EGFR
Applications ELISA, WB
Immunogen EGFR antibody was raised in mouse using recombinant human EGFR (424-605aa) purified from E. coli as the immunogen.

Images

Schematic Diagram of the Structure of EGFR

EGFR family members share a common domain arrangement comprised of a cysteine-rich extracellular domain, a transmembrane domain and an intracellular tyrosine kinase domain with several phosphorylation sites. The extracellular domains are subdivided and numbered as I-IV. Numerous phosphorylation sites have been elucidated in cytoplasmic domain of EGFR. Monoclonal antibodies target the extracellular domain III. The small molecule tyrosine kinase inhibitors bind with the ATP binding pockets in the tyrosine kinase domain. Several deletion mutations occur in the EGFR which are annotated in the diagram.

Specifications

Host Mouse
Clone 6E3
Isotype IgG2b kappa
Source Anti-human EGFR antibody is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human EGFR protein.
Method of Purification EGFR antibody was purified by protein-G affinity chromatography
Form & Buffer Supplied as a liquid in PBS, pH 7.4, with 0.1% NaN3.
Concentration 1 mg/ml

Usage & Assay Information

Usage Recommendations WB 1:500 to 1:1000

Storage & Safety

Storage Store at 4 deg C for short term storage. Aliquot and store at -20 deg C for long term storage. Avoid repeated freeze/thaw cycles.

General Information

Product Use Monoclonal EGFR antibody specific for Human EGFR for use in ELISA and Western Blot.
Biological Significance Epidermal growth factor receptor (EGFR) is a 170 kDa transmembrane receptor tyrosine kinase. EGFR protein was first identified as a binding partner of EGF. In addition, there are six other different ligands that can bind EGFR; transforming growth factor alpha (TGF alpha or TGFa), epiregulin (EPR), amphiregulin (AR), heparin binding EGF (HBEGF), betacellulin (BTC), and epigen. These ligands control downstream signaling pathways, such as proliferation, survival, differentiation, and migration, and when they bind to the EGFR causing it to dimerize and become activated. Modulation of receptor trafficking and degradation are essential for proper EGFR signaling, and EGFR trafficking studies have primarilty been performed using EGF as the ligand. As a result, the majority of research is focused on examining EGF/EGFR interactions and how they regulate its recycling and degradation, and there is a scarcity of information on how EGFR interacts with its other important ligand partners. When EGFR binds to its cognate ligand EGF, this induces tyrosine phosphorylation and receptor dimerization with other family members leading to enhanced uncontrolled proliferation, which is a major cancer causing signalling pathway.
Expression High expression of EGFR has been reported in a variety of epithelial tumors. EGFR is present in cell membranes and is also secreted from the cell. Specifically it is found in Nuclear membranes, Endoplasmic reticulum membranes, Golgi apparatus membranes, Endosomal membranes and is also secreted through endosomes. Upon EGF binding, EGFR is translocated from the cell membrane to the nucleus via Golgi and ER. Once dimerization occurs and it is activated, it is then endocytosed from the cell.
Implications in Disease The overexpression of EGFR in various epithelial tumors was widely reported and it has been substantiated that deregulation of EGFR itself and its signaling pathways an important role in human cancers. Epidermal growth factor receptors (EGFRs) are a large family of receptor tyrosine kinases (TK) expressed in several types of cancer, including breast, lung, esophageal, and head and neck. Distinct therapeutic approaches currently employed for targeting EGFR in various human malignancies are the use of monoclonal antibodies and small molecule tyrosine kinase inhibitors.
Sequence Information Belongs to the protein kinase superfamily. It contains a catalytic domain of protein tyrosine kinase at amino acids 659-974; a transmembrane domain at amino acids 589-632; and a number of polypeptide binding domains. It also contains a number of Furin-like repeats. Cysteine rich region. Exact function of the domain is not known. Furin is a serine-kinase dependent proprotein processor. Other members of this family include endoproteases and cell surface receptors.
Post-Translational Modifications Src phosphorylates EGFR on tyrosine 845 (Y845) in the Src-EGFR complex. Y845 of EGFR is located in the activation segment of the kinase domain, where many protein kinases contain kinase-activating autophosphorylation sites (e.g., cAMP-dependent protein kinase, Src family kinases, transmembrane receptor type tyrosine kinases) or trans-phosphorylation sites (e.g., cyclin-dependent protein kinase, mitogen-activated protein kinase, Akt protein kinase). A number of studies have demonstrated that Y845 phosphorylation serves an important role in cancer as well as normal cells. It is evident that binding of EGF to EGFR triggers a series autophosphorylation events of specific tyrosine residues (for example Tyr 1045, Tyr 992, Tyr 975, Tyr 1068, Tyr 1173 etc) in its kinase domain i.e activated EGFR protein level will be elevated without changing total EGFR protein level. Methylation at Arg-1199 by PRMT5 positively stimulates phosphorylation at Tyr-1197.
Database Links Entrez Gene: 1956 Human, Omim: 131550 Human, SwissProt: P00533 Human, Unigene: 488293 Human

References
Add a Paper

Parthasarathy Seshacharyulu, Moorthy P. Ponnusamy, Dhanya Haridas, Maneesh Jain, AparK. Ganti, Surinder K. Batra.

Targeting the EGFR signaling pathway in cancer therapy

Expert Opin Ther Targets

Volume: 16 Issue: 1 Page: 15-31 PMID: PMC3291787 DOI: 10.1517/14728222.2011.648617

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Images

  • Schematic Diagram of the Structure of EGFR | EGFR family members share a common domain arrangement comprised of a cysteine-rich extracellular domain, a transmembrane domain and an intracellular tyrosine kinase domain with several phosphorylation sites. The extracellular domains are subdivided and numbered as I-IV. Numerous phosphorylation sites have been elucidated in cytoplasmic domain of EGFR. Monoclonal antibodies target the extracellular domain III. The small molecule tyrosine kinase inhibitors bind with the ATP binding pockets in the tyrosine kinase domain. Several deletion mutations occur in the EGFR which are annotated in the diagram.
  • Western Blot analysis of EGFR antibody (10R-1765) | The extracts of HaCaT (35 ug) were resolved by SDS-PAGE, transferred to PVDF membrane and probed with anti-human EGFR (1:500 or 1000). Proteins were visualized using a goat anti-mouse secondary antibody conjugated to HRP and an ECL detection system.

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Price: $265.00
Size: 100 ul
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