EGFR, Soluble (human) (rec.)

AdipoGen Life Sciences

EGFR, Soluble (human) (rec.)

10

Research Use Only

>90%

EGFR

epidermal growth factor receptor

ERBB, ERBB1, ERRP, HER1, NISBD2, NNCIS, PIG61, mENA, epidermal growth factor receptor, EGFR vIII, avian erythroblastic leukemia viral (v-erb-b) oncogene homolog, cell growth inhibiting protein 40, cell proliferation-inducing protein 61, epidermal growth factor receptor tyrosine kinase domain, erb-b2 receptor tyrosine kinase 1, proto-oncogene c-ErbB-1, receptor tyrosine-protein kinase erbB-1

Epidermal growth factor receptor

EGFR has been shown to bind a subset of the EGF family ligands, including EGF, amphiregulin, TGF-alpha, betacellulin, epiregulin, heparin-binding EGF and neuregulin-2 in the absence of a co-receptor. Ligand binding induces EGFR homodimerization as well as heterodimerization with ErbB2, resulting in kinase activation, tyrosine phosphorylation and cell signaling. EGFR signaling has been shown to regulate multiple biological functions including cell proliferation, differentiation, motility and apoptosis. In addition, EGFR signaling has also been shown to play a role in carcinogenesis. - Protein. Human EGFR (629aa) is fused at the C-terminus to a Strep-tag. Source: Sf9 cells. Lyophilized. Purity: >90% (SDS-PAGE). EGFR has been shown to bind a subset of the EGF family ligands, including EGF, amphiregulin, TGF-alpha, betacellulin, epiregulin, heparin-binding EGF and neuregulin-2 in the absence of a co-receptor. Ligand binding induces EGFR homodimerization as well as heterodimerization with ErbB2, resulting in kinase activation, tyrosine phosphorylation and cell signaling. EGFR signaling has been shown to regulate multiple biological functions including cell proliferation, differentiation, motility and apoptosis. In addition, EGFR signaling has also been shown to play a role in carcinogenesis.

-20°C,2°C to 8°C

41116100

Human