Phospho-EGFR (Tyr1092) Antibody

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Description

Introduction to Phospho-EGFR (Tyr1092) Antibody

Phospho-EGFR (Tyr1092) Antibody is a specialized immunological reagent designed to recognize and bind specifically to the epidermal growth factor receptor (EGFR) protein only when it is phosphorylated at tyrosine residue 1092. This high specificity enables researchers to detect activated EGFR in various experimental contexts. The antibody detects endogenous levels of EGFR exclusively when this specific tyrosine residue is phosphorylated, making it an invaluable tool for studying EGFR signaling dynamics .

It is worth noting that there exists some nomenclature variation in the scientific literature regarding this phosphorylation site. Some researchers refer to this site as Tyr1068, which represents the same position after accounting for the removal of the signal peptide . This distinction is important when comparing research findings across different publications and commercial antibody products.

The production of these antibodies generally involves immunization with synthetic phosphopeptides derived from human EGFR containing the Tyr1092 phosphorylation site. Specifically, many manufacturers use peptides corresponding to amino acids 1061-1110 or similar regions surrounding the phosphorylation site .

For polyclonal antibodies, the production process typically involves:

  1. Immunization of rabbits with the synthetic phosphopeptide

  2. Collection of serum containing antibodies

  3. Purification via antigen affinity chromatography using the immunizing phosphopeptide

Recombinant monoclonal antibodies follow a more sophisticated production pathway:

  1. Isolation of antibody DNA sequences from immunoreactive rabbits

  2. Cloning these sequences into expression vectors

  3. Expression in systems such as HEK293F cells

  4. Screening and selection of optimal clones

  5. Purification through affinity chromatography

Functional Significance of EGFR Tyr1092 Phosphorylation

Understanding the biological significance of Tyr1092 phosphorylation is essential for appreciating the value of antibodies targeting this specific modification. EGFR belongs to the HER/ERbB family of proteins that includes three other receptor tyrosine kinases: ERbB2, ERbB3, and ERbB4 .

The phosphorylation of Tyr1092 occurs following EGFR dimerization, which is triggered by binding of cognate ligands such as Epidermal Growth Factor (EGF) and Transforming Growth Factor alpha (TGF-α) to the extracellular domain. This phosphorylation event creates a critical docking site for downstream signaling molecules .

Particularly significant is the fact that autophosphorylation at Tyr1092 recruits Signal Transducer and Activator of Transcription 3 (STAT3), a transcription factor implicated in cellular proliferation, survival, and oncogenesis . This specific interaction makes Tyr1092 phosphorylation a crucial event in EGFR-mediated signaling pathways relevant to cancer biology and therapeutic intervention strategies.

Western Blot Analysis

Western blotting represents one of the most common applications for Phospho-EGFR (Tyr1092) antibodies. For optimal results, these antibodies are typically used at dilutions ranging from 1:500 to 1:3000 . Key considerations for Western blot applications include:

  • Sample preparation: Cells are often treated with EGF to induce EGFR phosphorylation, as validated in experimental models using HeLa cells

  • Protein denaturation: Standard SDS-PAGE conditions are suitable for detection

  • Expected molecular weight: The phosphorylated EGFR is typically observed at 134-180 kDa

  • Control samples: Inclusion of untreated controls is essential to confirm specificity for the phosphorylated form

Immunohistochemistry and Immunofluorescence

For tissue and cellular localization studies, Phospho-EGFR (Tyr1092) antibodies are employed in both immunohistochemistry (IHC) and immunofluorescence (IF) applications. Typical working dilutions range from 1:50 to 1:200 . These techniques allow visualization of phosphorylated EGFR within cellular contexts, revealing both expression levels and subcellular localization patterns.

ELISA Applications

Enzyme-Linked Immunosorbent Assay (ELISA) represents a highly sensitive quantitative method for detecting phosphorylated EGFR in research samples. For this application, considerably higher dilutions are often employed, sometimes reaching 1:20000 . This high sensitivity makes ELISA particularly valuable for detecting low abundance phosphorylated EGFR in complex biological samples.

Flow Cytometry

For flow cytometry applications, dilutions typically range from 1:50 to 1:200 . This technique allows researchers to quantify phosphorylated EGFR at the single-cell level within heterogeneous populations, offering insights into cellular heterogeneity in EGFR activation states.

EGFR in Oncogenesis

Overexpression and aberrant activation of EGFR have been linked to numerous types of cancer, making it a critical target for both biological and small molecular therapeutics . Phospho-EGFR (Tyr1092) antibodies have been instrumental in studying these processes in various tumor types, including:

  • Head and neck cancer

  • Brain tumors

  • Bladder cancer

  • Breast cancer

  • Lung cancer

  • Endometrial cancer

  • Cervical cancer

  • Ovarian cancer

  • Esophageal cancer

  • Gastric cancer

  • Squamous cell carcinoma

The ability to specifically detect phosphorylated EGFR at Tyr1092 provides researchers with a precise tool to evaluate receptor activation status in these different cancer contexts, potentially correlating with disease progression and therapeutic response.

Therapeutic Development and Monitoring

Given the central role of EGFR in cancer progression, numerous therapeutics targeting this receptor have been developed. Phospho-EGFR (Tyr1092) antibodies serve as essential tools for:

  1. Evaluating the efficacy of EGFR-targeted therapies in preclinical models

  2. Monitoring treatment response in experimental systems

  3. Identifying potential resistance mechanisms involving alterations in EGFR phosphorylation patterns

  4. Developing companion diagnostics for patient stratification in precision medicine approaches

Advanced Imaging Techniques

The development of advanced imaging methodologies, including super-resolution microscopy and multiplexed imaging platforms, opens new possibilities for utilizing Phospho-EGFR (Tyr1092) antibodies in spatial analyses of receptor activation patterns within complex tissues and cellular microenvironments.

Single-Cell Analysis

Emerging single-cell technologies present opportunities to examine EGFR phosphorylation heterogeneity at unprecedented resolution. Phospho-EGFR (Tyr1092) antibodies compatible with single-cell protein analysis methods could reveal critical insights into cellular diversity in receptor activation states within tumors and other heterogeneous tissues.

Liquid Biopsy Applications

The potential adaptation of Phospho-EGFR (Tyr1092) detection methods to liquid biopsy formats represents an exciting frontier. Development of highly sensitive assays capable of detecting phosphorylated EGFR in circulating tumor cells or extracellular vesicles could provide minimally invasive approaches for monitoring treatment response and disease progression.

Product Specs

Form
Supplied at 1.0mg/mL in phosphate buffered saline (without Mg2+ and Ca2+), pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.
Lead Time
Typically, we can ship your order within 1-3 business days of receiving it. The delivery timeframe may vary depending on the chosen purchase method and location. For precise delivery estimates, please consult your local distributors.
Synonyms
Avian erythroblastic leukemia viral (v erb b) oncogene homolog antibody; Cell growth inhibiting protein 40 antibody; Cell proliferation inducing protein 61 antibody; EGF R antibody; EGFR antibody; EGFR_HUMAN antibody; Epidermal growth factor receptor (avian erythroblastic leukemia viral (v erb b) oncogene homolog) antibody; Epidermal growth factor receptor (erythroblastic leukemia viral (v erb b) oncogene homolog avian) antibody; Epidermal growth factor receptor antibody; erb-b2 receptor tyrosine kinase 1 antibody; ERBB antibody; ERBB1 antibody; Errp antibody; HER1 antibody; mENA antibody; NISBD2 antibody; Oncogen ERBB antibody; PIG61 antibody; Proto-oncogene c-ErbB-1 antibody; Receptor tyrosine protein kinase ErbB 1 antibody; Receptor tyrosine-protein kinase ErbB-1 antibody; SA7 antibody; Species antigen 7 antibody; Urogastrone antibody; v-erb-b Avian erythroblastic leukemia viral oncogen homolog antibody; wa2 antibody; Wa5 antibody
Target Names
Uniprot No.

Target Background

Function
Receptor tyrosine kinases bind ligands from the EGF family, activating various signaling cascades that transform extracellular cues into suitable cellular responses. These ligands include EGF, TGFA/TGF-alpha, AREG, epigen/EPGN, BTC/betacellulin, epiregulin/EREG, and HBEGF/heparin-binding EGF. Ligand binding triggers receptor homo- and/or heterodimerization and autophosphorylation on key cytoplasmic residues. The phosphorylated receptor recruits adapter proteins like GRB2, which in turn activates complex downstream signaling cascades. This activation encompasses at least four major downstream signaling cascades, including the RAS-RAF-MEK-ERK, PI3 kinase-AKT, PLCgamma-PKC, and STATs modules. Additionally, it may activate the NF-kappa-B signaling cascade. The receptor directly phosphorylates other proteins such as RGS16, enhancing its GTPase activity and potentially linking EGF receptor signaling to G protein-coupled receptor signaling. It also phosphorylates MUC1, increasing its interaction with SRC and CTNNB1/beta-catenin. EGFR positively regulates cell migration by interacting with CCDC88A/GIV, retaining EGFR at the cell membrane following ligand stimulation. This promotes EGFR signaling, triggering cell migration. EGFR plays a role in enhancing learning and memory performance. Isoform 2 might function as an antagonist to EGF action. In the context of microbial infection, EGFR serves as a receptor for hepatitis C virus (HCV) in hepatocytes, facilitating its cell entry. It mediates HCV entry by promoting the formation of the CD81-CLDN1 receptor complexes, crucial for HCV entry, and by enhancing membrane fusion of cells expressing HCV envelope glycoproteins.
Gene References Into Functions
  1. Amphiregulin, contained in non-small-cell lung carcinoma-derived exosomes, induces osteoclast differentiation through the activation of the EGFR pathway. PMID: 28600504
  2. Combining vorinostat with an EGFRTKI can reverse EGFRTKI resistance in NSCLC. PMID: 30365122
  3. The feasibility of utilizing the radiocobalt labeled antiEGFR affibody conjugate ZEGFR:2377 as an imaging agent has been explored. PMID: 30320363
  4. Among all transfection complexes, 454 lipopolyplexes modified with the bidentate PEG-GE11 agent exhibit the most efficient EGFR-dependent uptake, as well as luciferase and NIS gene expression into PMID: 28877405
  5. EGFR amplification was found to be higher in the OSCC group compared to the control group (P=0.018) and was associated with advanced clinical stage (P=0.013), regardless of age. Patients exhibiting EGFR overexpression had poorer survival rates, as did those with T3-T4 tumors and positive margins. EGFR overexpression negatively impacts disease progression. PMID: 29395668
  6. Clonal analysis reveals that the dominant JAK2 V617F-positive clone in Polycythemia Vera harbors the EGFR C329R substitution. This mutation may contribute to clonal expansion. PMID: 28550306
  7. Baseline Circulating tumor cell count could serve as a predictive biomarker for EGFR-mutated and ALK-rearranged non-small cell lung cancer, providing enhanced guidance and monitoring for patients undergoing molecular targeted therapies. PMID: 29582563
  8. High EGFR expression is linked to cystic fibrosis. PMID: 29351448
  9. These findings suggest a mechanism for EGFR inhibition to suppress respiratory syncytial virus by activating endogenous epithelial antiviral defenses PMID: 29411775
  10. This study identified the emergence of the T790M mutation within the EGFR cDNA in a subset of erlotinib-resistant PC9 cell models through Sanger sequencing and droplet digital PCR-based methods, demonstrating that the T790M mutation can arise de novo following erlotinib treatment. PMID: 29909007
  11. The present study demonstrated that miR145 regulates the EGFR/PI3K/AKT signaling pathway in patients with nonsmall cell lung cancer. PMID: 30226581
  12. Among NSCLC patients treated with EGFR-TKI, those with T790M mutations were found to frequently also exhibit 19 dels, compared to T790M-negative patients. Additionally, T790M-positive patients had a longer PFS. Therefore, screening these patients for T790M mutations may contribute to improved survival. PMID: 30150444
  13. High EGFR expression is associated with Breast Carcinoma. PMID: 30139236
  14. Results indicate that CAV-1 could promote anchorage-independent growth and anoikis resistance in detached SGC-7901 cells. This is associated with the activation of Src-dependent epidermal growth factor receptor-integrin beta signaling, as well as the phosphorylation of PI3K/Akt and MEK/ERK signaling pathways PMID: 30088837
  15. Our findings suggest that FOXK2 inhibits the malignant phenotype of clear-cell renal cell carcinoma and acts as a tumor suppressor, possibly through the inhibition of EGFR. PMID: 29368368
  16. EGFR mutation status in advanced non-small cell lung cancer (NSCLC) patients has changed significantly. PMID: 30454543
  17. Different Signaling Pathways in Regulating PD-L1 Expression in EGFR Mutated Lung Adenocarcinoma PMID: 30454551
  18. Internal tandem duplication of the kinase domain delineates a genetic subgroup of congenital mesoblastic nephroma, transcending histological subtypes PMID: 29915264
  19. The expression level of EGFR increased along with higher stages and pathologic grades of BTCC, and the notably increased expression of HER-2 was statistically associated with clinical stages and tumor recurrence. Furthermore, the expression level of HER-2 increased with higher clinical stage of BTCC. EGFR expression and HER-2 levels were positively associated in BTCC samples. PMID: 30296252
  20. Results demonstrate that GGA2 interacts with the EGFR cytoplasmic domain to stabilize its expression, reducing its lysosomal degradation. PMID: 29358589
  21. Combination therapy of apatinib with icotinib for primary acquired resistance to icotinib may be a viable option for patients with advanced pulmonary adenocarcinoma harboring EGFR mutations. However, physicians must remain cognizant of the side effects associated with this therapy. PMID: 29575765
  22. This report presents a rare case manifesting as multiple lung adenocarcinomas with four different EGFR gene mutations identified in three lung tumors. PMID: 29577613
  23. The study supports the involvement of EGFR, HER2, and HER3 in BCC aggressiveness and tumor differentiation towards distinct histological subtypes. PMID: 30173251
  24. The ratio of sFlt-1/sEGFR could serve as a novel candidate biochemical marker for monitoring the severity of preterm preeclampsia. sEndoglin and sEGFR might be implicated in the pathogenesis of small for gestational age in preterm preelampsia. PMID: 30177039
  25. The study confirmed the prognostic effect of EGFR and VEGFR2 for recurrent disease and survival rates in patients with epithelial ovarian cancer. PMID: 30066848
  26. The data suggest that diagnostic or therapeutic chest radiation may predispose patients with decreased stromal PTEN expression to secondary breast cancer, and that prophylactic EGFR inhibition may mitigate this risk. PMID: 30018330
  27. This research proposes a unique regulatory feature of PHLDA1, inhibiting the ErbB receptor oligomerization process and thereby controlling the activity of the receptor signaling network. PMID: 29233889
  28. The study observed the occurrence not only of the EGFR C797S mutation but also L792F/Y/H in three NSCLC clinical subjects exhibiting acquired resistance to osimertinib treatment. PMID: 28093244
  29. Data indicate that the expression level of epidermal growth factor-like domain 7 (EGFL7) and epidermal growth factor receptor (EGFR) in invasive growth hormone-producing pituitary adenomas (GHPA) is considerably higher than that of non-invasive GHPA. PMID: 29951953
  30. Concurrent mutations in genes such as CDKN2B or RB1 were associated with worse clinical outcome in lung adenocarcinoma patients with EGFR active mutations. PMID: 29343775
  31. The ER-alpha36/EGFR signaling loop promotes growth of hepatocellular carcinoma cells. PMID: 29481815
  32. High EGFR expression is linked to colorectal cancer. PMID: 30106444
  33. High EGFR expression is associated with gefitinib resistance in lung cancer. PMID: 30106446
  34. High EGFR expression is associated with tumor-node-metastasis in nonsmall cell lung cancer. PMID: 30106450
  35. Data suggest that Thr264 in TRPV3 is a key ERK1 phosphorylation site mediating EGFR-induced sensitization of TRPV3 to stimulate signaling pathways involved in regulating skin homeostasis. (TRPV3 = transient receptor potential cation channel subfamily V member-3; ERK1 = extracellular signal-regulated kinase-1; EGFR = epidermal growth factor receptor) PMID: 29084846
  36. The EGFR mutation frequency in Middle Eastern and African patients is higher than that observed in white populations but remains lower than the frequency reported in Asian populations. PMID: 30217176
  37. EGFR-containing exosomes derived from cancer cells could favor the development of a liver-like microenvironment, promoting liver-specific metastasis. PMID: 28393839
  38. The results reveal that the EGF-STAT3 signaling pathway promotes and maintains colorectal cancer (CRC) stemness. Furthermore, crosstalk between STAT3 and Wnt activates the Wnt/beta-catenin signaling pathway, which is also responsible for cancer stemness. Therefore, STAT3 is a potential therapeutic target for CRC treatment. PMID: 30068339
  39. This finding indicates that the T790M mutation is not only associated with EGFR-TKI resistance but may also play a functional role in the malignant progression of lung adenocarcinoma. PMID: 29887244
  40. LOX regulates EGFR cell surface retention to drive tumor progression. PMID: 28416796
  41. In a Han Chinese population, EGFR gene polymorphisms, rs730437 and rs1468727, and haplotype A-C-C were shown to be potential protective factors against the development of Alzheimer's Disease. PMID: 30026459
  42. EGFR proteins at different cellular locations in lung adenocarcinoma might influence the biology of cancer cells and serve as an independent indicator of a more favorable prognosis and treatment response. PMID: 29950164
  43. This report presents the crystal structure of EGFR T790M/C797S/V948R in complex with EAI045, a novel type of EGFR TKI that binds to EGFR reversibly and does not rely on Cys 797. PMID: 29802850
  44. Overexpression of miR-452-3p promoted cell proliferation and mobility while suppressing apoptosis. MiR-452-3p enhanced EGFR and phosphorylated AKT (pAKT) expression but inhibited p21 expression levels. MiR-452-3p promoted hepatocellular carcinoma (HCC) cell proliferation and mobility by directly targeting the CPEB3/EGFR axis. PMID: 29332449
  45. This study demonstrates that the D2A sequence of the UPAR induces cell growth through alphaVbeta3 integrin and EGFR. PMID: 29184982
  46. BRAF and EGFR inhibitors can synergize to enhance cytotoxic effects and diminish stem cell capacities in BRAF(V600E)-mutant colorectal cancer cells. PMID: 29534162
  47. This study confirms a direct correlation between MSI1 and EGFR, potentially supporting the significant role of MSI1 in the activation of EGFR through NOTCH/WNT pathways in esophageal squamous cell carcinoma. PMID: 30202417
  48. Three lines of tyrosine kinase inhibitors (TKIs) therapy can extend survival in non-small cell lung cancer (NSCLC) patients. Elderly patients can benefit from TKI therapy. Patients with EGFR mutations can benefit from second-line or third-line TKI therapy. PMID: 29266865
  49. EGFR 19Del and L858R mutations are valuable biomarkers for predicting the clinical response to EGFR-TKIs. 19Del mutations may lead to a better clinical outcome. PMID: 29222872
  50. HMGA2-EGFR constitutively induced a higher level of phosphorylated STAT5B than EGFRvIII. PMID: 29193056

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Database Links

HGNC: 3236

OMIM: 131550

KEGG: hsa:1956

STRING: 9606.ENSP00000275493

UniGene: Hs.488293

Involvement In Disease
Lung cancer (LNCR); Inflammatory skin and bowel disease, neonatal, 2 (NISBD2)
Protein Families
Protein kinase superfamily, Tyr protein kinase family, EGF receptor subfamily
Subcellular Location
Cell membrane; Single-pass type I membrane protein. Endoplasmic reticulum membrane; Single-pass type I membrane protein. Golgi apparatus membrane; Single-pass type I membrane protein. Nucleus membrane; Single-pass type I membrane protein. Endosome. Endosome membrane. Nucleus.; [Isoform 2]: Secreted.
Tissue Specificity
Ubiquitously expressed. Isoform 2 is also expressed in ovarian cancers.

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