epitope corresponding to phosphorylated Thr 654 of EGFR of human origin
Modification
Phosphoralated
Modification Notes
Epidermal growth factor mediates its effects on cell growth through its inter-action with a cell surface glycoprotein designated EGFR (EGF receptor). Binding of EGF or TGF alpha to EGFR activates tyrosine-specific protein kinase activity intrinsic to EGFR. The carboxy terminal tyrosine residues on EGFR, Tyr 1068 and Tyr 1173, are the major sites of autophosphorylation, which occurs as a result of EGF binding. Once activated, EGFR mediates the binding of the phosphotyrosine binding (PTB) domain of GRB2 through direct interactions with Tyr 1068 and Tyr 1086 and through indirect interactions with Tyr 1173 in the Ras signaling pathway. Tyr 1173 of EGFR also functions as a kinase substrate. Phosphorylation of Tyr 992, Tyr 1068 and Tyr 1086 is required for conformational change in the C-terminal tail of EGFR. EGFR is also subject to phosphorylation on other amino acid residues, such as Thr 654.
Key Feature
Clonality
Polyclonal
Isotype
IgG
Host Species
Rabbit
Tested Applications
WBIP
recommended for detection of Thr 654 phosphorylated EGFR of mouse, rat and human origin by WB and IP:
Species Reactivity
HumanMouseRat
Concentration
1mg/ml
Purification
Affinity purified
Target Information
Alternative Names
epitope corresponding to phosphorylated Thr 654 of EGFR of human origin
Tissue Specificity
epitope corresponding to phosphorylated Thr 654 of EGFR of human origin