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Phospho-EGF Receptor (Tyr1068) Antibody
synthetic phosphopeptide corresponding to residues surrounding Tyr1068 of human EGF receptor
W, IHC-P
Rabbit
H,M,R
CST
详见MSDS文件
大量
详见说明书
2
-20°c
100 ul (10 western blots)/300 ul (30 western blots)/carrier free & custom formulation / quantity
规格: | 产品价格: | ¥请询价 | |
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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 IHC-P=Immunohistochemistry (Paraffin)
Reactivity Key: H=Human M=Mouse R=Rat
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) | Source |
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W IHC-P | H M R | Endogenous | 175 | Rabbit |
Protocols |
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Specificity / Sensitivity | Phospho-EGF Receptor (Tyr1068) Antibody detects endogenous levels of EGF receptor only when phosphorylated at tyrosine 1068. The antibody may cross-react with other activated EGF receptor family members (e.g. ErbB2), and cross-reacts slightly with activated PDGF receptor . |
Source / Purification | Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Tyr1068 of human EGF receptor. Antibodies are purified by protein A and peptide affinity chromatography. Western BlottingWestern blot analysis of MDA-468 cells untreated and treated with EGF, using Phospho-EGF Receptor (Tyr1068) Antibody. IHC-P (paraffin)Immunohistochemical analysis of paraffin-embedded human breast tumor, showing membrane and cytoplasmic localization, using Phospho-EGF Receptor (Tyr1068) Antibody. IHC-P (paraffin)Immunohistochemical annalysis of paraffin-embedded MDA-MB-468 cells, untreated (left), EGF treated (middle), or EGF and Tarceva® treated (right), using Phospho-EGF Receptor (Tyr1068) Antibody. |
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).
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Application References |
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Companion Products |
For Research Use Only. Not For Use In Diagnostic Procedures. |
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