This rabbit anti-EGFR [pY1086] polyclonal antibody is specific to rat and human EGFR [pY1086]. Based on 100% sequence homology, cross reactivity with mouse and pig EGFR when phosphorylated at Tyr1086 1086 is expected. EGFR [pY1086] polyclonal antibody recognizes the expressed product of the EGFR gene. The epidermal growth factor receptor (EGFr) is a receptor tyrosine kinase involved in the regulation of growth in mammalian cells, in both normal and neoplastic conditions. Validated applications for EGFR [pY1086] polyclonal antibody are ELISA, immunocytochemistry, immunofluorescence and Western blotting.

Applications: Validated applications for EGFR [pY1086] polyclonal antibody are ELISA, immunocytochemistry, immunofluorescence and Western blotting.
Host species and isotype: The host species and isotype of the EGFR [pY1086] polyclonal antibody is rabbit IgG.
Polyclonal antibody designation: The rabbit anti-EGFR [pY1086] polyclonal antibody designation is ZMD.310.
Reactivity: rabbit anti-EGFR [pY1086] polyclonal antibody detects rat and human EGFR [pY1086]. Based on 100% sequence homology, cross reactivity with mouse and pig EGFR [pY1086] is expected.
Product size: Rabbit anti-EGFR [pY1086] polyclonal antibody is available in a 50 µg pack size.

The epidermal growth factor receptor (EGFr) is a receptor tyrosine kinase involved in the regulation of growth in mammalian cells, in both normal and neoplastic conditions. Binding of the EGF ligand to EGFr results in receptor dimerization, phosphorylation of specific Tyr residues within the intracellular domain of EGFr, and the activation of intracellular signal transduction pathways. Identified EGFr autophosphorylation sites include tyrosine residues 992, 1068, 1086, 1148, and 1173, all located within the receptor's C-terminus. These autophosphorylation sites are essential for receptor kinase activity and internalization. Multiple phosphorylation of tyrosines 992, 1068, and 1086 is required for conformation change in the C-terminal tail of human EGFr.

The association of EGFr with a variety of intracellular proteins is mediated by its phosphorylated Tyr1068 and Tyr1086 residues. These phospho-tyrosines serve as high affinity binding sites of Grb2/Ash, which regulates the internalization of EGFr in clathrin-coated pits. Tyr1068 and Tyr1086 also interact with and activate STAT3, and act as association sites with the docking protein Gab1 in the activation of MAP kinase and JNK signaling pathways.