EGFR Protein, Human (sf9, His-GST)

EGFR Protein, a receptor tyrosine kinase, binds various ligands like EGF, TGFA, AREG, epigen, BTC, epiregulin, and HBEGF, initiating signaling cascades that mediate cellular responses. This involves receptor dimerization, autophosphorylation, and recruitment of adapter proteins like GRB2, activating downstream pathways such as RAS-RAF-MEK-ERK, PI3 kinase-AKT, PLCgamma-PKC, and STATs. EGFR can also trigger NF-kappa-B signaling, phosphorylate proteins like RGS16, and interact with MUC1, influencing G protein-coupled receptor signaling. Moreover, it enhances cell migration through interactions with CCDC88A, promoting EGFR signaling and triggering cell migration. Additionally, EGFR impacts learning, memory, and pain signaling. EGFR Protein, Human (sf9, His-GST) is the recombinant human-derived EGFR protein, expressed by Sf9 insect cells, with N-His, N-GST labeled tag. The total length of EGFR Protein, Human (sf9, His-GST) is 543 a.a., with molecular weight of ~89.1 kDa.

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Recombinant Proteins