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Phospho-EGF Receptor (Tyr1068)

(1H12) Mouse mAb
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  • 询价
  • Cell Signaling Technology已认证
  • USA
  • 2025年11月05日
  • W, IP, IHC-P
  • H,R,Mk
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    • 详细信息
    • 文献和实验
    • 技术资料
    • 抗体英文名

      Phospho-EGF Receptor (Tyr1068) (1H12) Mouse mAb

    • 抗原

      synthetic phosphopeptide corresponding to residues surrounding Tyr1068 of human EGF receptor

    • 应用范围

      W, IP, IHC-P

    • 级别

      详见MSDS文件

    • 适应物种

      H,R,Mk

    • 库存

      大量

    • 保质期

      详见说明书

    • 供应商

      CST

    • 是否单克隆

      1

    • 保存条件

      -20°c

    • 规格

      100 ul (10 western blots)/300 ul (30 western blots)/carrier free & custom formulation / quantity

    规格:产品价格:¥请询价
    规格:100 ul (10 western blots)产品价格:¥请询价
    规格:300 ul (30 western blots)产品价格:¥请询价
    规格:carrier free & custom formulation / quantity产品价格:¥请询价

    pathway more info application references datasheet PDF MSDS PDF protocols

    Applications Key:  W=Western Blotting  IP=Immunoprecipitation  IHC-P=Immunohistochemistry (Paraffin)
    Reactivity Key:  H=Human  R=Rat  Mk=Monkey
    Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.

    Applications Reactivity Sensitivity MW (kDa) Isotype
    W IP IHC-P H R Mk Endogenous 175 Mouse IgG1
    Protocols
    Specificity / Sensitivity

    Phospho-EGF Receptor (Tyr1068) (1H12) Mouse mAb detects endogenous levels of EGF receptor only when phosphorylated at Tyr1068. This antibody does not recognize EGF receptor phosphorylated at other sites, but may cross-react with other activated ErbB family members. Non-specific staining of smooth muscle may be observed in paraffin-embedded tissues.

    Source / Purification

    Monoclonal antibody is produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Tyr1068 of human EGF receptor.

    Western Blotting

    Western Blotting

    Western blot analysis of extracts from A431 cells, untreated or EGF-stimulated (100 ng/ml), using Phospho-EGF Receptor (Tyr1068) (1H12) Mouse mAb (upper) or EGF Receptor (C74B9) Rabbit mAb #2646 (lower).

    IHC-P (paraffin)

    IHC-P (paraffin)

    Immunohistochemical analysis of paraffin-embedded human breast carcinoma, showing membrane localization, using Phospho-EGF Receptor (Tyr1068) (1H12) Mouse mAb.

    IHC-P (paraffin)

    IHC-P (paraffin)

    Immunohistochemical analysis of paraffin-embedded human breast carcinoma, untreated (left) or calf intestinal phosphatase (CIP) treated (right), using Phospho-EGF Receptor (Tyr1068) (1H12 ) Mouse mAb.


    IHC-P (paraffin)

    IHC-P (paraffin)

    Immunohistochemical analyis of paraffin-embedded human glioma using Phospho-EGF Receptor (Tyr1068) (1H12) Mouse mAb.

    IHC-P (paraffin)

    IHC-P (paraffin)

    Immunohistochemical analysis using Phospho-EGF Receptor (Tyr1068) (1H12) Mouse mAb on SignalSlide™ Phospho-EGF Receptor IHC Controls #8102 (paraffin-embedded KYSE450 cell pellets, untreated (left) or EGF-treated (right).

    Background

    The epidermal growth factor (EGF) receptor is a transmembrane tyrosine kinase that belongs to the HER/ErbB protein family. Ligand binding results in receptor dimerization, autophosphorylation, activation of downstream signaling, internalization, and lysosomal degradation (1,2). Phosphorylation of EGF receptor (EGFR) at Tyr845 in the kinase domain is implicated in stabilizing the activation loop, maintaining the active state enzyme, and providing a binding surface for substrate proteins (3,4). c-Src is involved in phosphorylation of EGFR at Tyr845 (5). The SH2 domain of PLCγ binds at phospho-Tyr992, resulting in activation of PLCγ-mediated downstream signaling (6). Phosphorylation of EGFR at Tyr1045 creates a major docking site for the adaptor protein c-Cbl, leading to receptor ubiquitination and degradation following EGFR activation (7,8). The GRB2 adaptor protein binds activated EGFR at phospho-Tyr1068 (9). A pair of phosphorylated EGFR residues (Tyr1148 and Tyr1173) provide a docking site for the Shc scaffold protein, with both sites involved in MAP kinase signaling activation (2). Phosphorylation of EGFR at specific serine and threonine residues attenuates EGFR kinase activity. EGFR carboxy-terminal residues Ser1046 and Ser1047 are phosphorylated by CaM kinase II; mutation of either of these serines results in upregulated EGFR tyrosine autophosphorylation (10).

    1. Hackel, P.O. et al. (1999) Curr Opin Cell Biol 11, 184-9.
    2. Zwick, E. et al. (1999) Trends Pharmacol Sci 20, 408-12.
    3. Cooper, J.A. and Howell, B. (1993) Cell 73, 1051-4.
    4. Hubbard, S.R. et al. (1994) Nature 372, 746-54.
    5. Biscardi, J.S. et al. (1999) J Biol Chem 274, 8335-43.
    6. Emlet, D.R. et al. (1997) J Biol Chem 272, 4079-86.
    7. Levkowitz, G. et al. (1999) Mol Cell 4, 1029-40.
    8. Ettenberg, S.A. et al. (1999) Oncogene 18, 1855-66.
    9. Rojas, M. et al. (1996) J Biol Chem 271, 27456-61.
    10. Feinmesser, R.L. et al. (1999) J Biol Chem 274, 16168-73.
    Application References

    Have you published research involving the use of our products? If so we'd love to hear about it. Please let us know !

    Companion Products

    For Research Use Only. Not For Use In Diagnostic Procedures.

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