85-1784-07　EGFR, Active, Recombinant, Mouse, FLAG-Tag (Epidermal Growth Factor Receptor) 10ug　137268

特徴

• Epidermal growth factor (EGF) receptor is a 170kD tyrosine kinase. Ligand binding results in receptor dimerization, autophosphorylation, activation of downstream signaling and lysosomal degradation. Phosphorylation of Tyr845 in the kinase domain is implicated in stabilizing the activation loop, maintaining the enzyme in an active state and providing a binding surface for substrate proteins. c-Src is involved in phosphorylation of Tyr845. Phospho-tyrosine 992 is a direct binding site for the PLC gamma SH2 domain, resulting in activation of PLC gamma-mediated downstream signaling. Phosphorylation of Tyr1045 creates a major docking site for c-Cbl. Binding of c-Cbl to the activated EGFR leads to receptor ubiquitination and degradation. Phospho-Tyr1068 of activated EGFR is a direct binding site for Grb2. Phospho-tyrosine 1148 and 1173 provide a docking site for SHC. Both sites are involved in the activation of MAP kinase signaling. Phosphorylation of EGFR on serine and threonine residues attenuates EGFR kinase activity. Serines 1046 and 1047 in the carboxy-terminal region of EGFR are sites phosphorylated by CaM kinase II. Mutations to either serine 1046 or 1047 upregulate tyrosine autokinase activity of EGFR.
• Source:Recombinant corresponding to aa670-1210 from mouse EGFR, fused to Flag-tag at C-terminal, expressed in a Baculovirus-infected Sf9 cell expression system.
• Molecular Weight:~62kD
• Specific Activity:~49pmole/min/mg
• Applications:Suitable for use in the study of enzyme kinetics, screening inhibitors, and selectivity profiling. Other applications not tested.
• Recommended Dilution:Optimal dilutions to be determined by the researcher.
• Storage and Stability:Aliquot to avoid repeated freezing and thawing and store at -70°C. Aliquots are stable for 6 months. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.