Phospho-EGFR (Y1148) Rabbit Polyclonal Antibody (HA500580)

UNIPROT #

P00533

PROTEIN NAME

Phospho-EGFR (Y1148)

SYNONYMS

Avian erythroblastic leukemia viral (v erb b) oncogene homolog antibody;Cell growth inhibiting protein 40 antibody;Cell proliferation inducing protein 61 antibody;EGF R antibody;EGFR antibody;EGFR_HUMAN antibody;Epidermal growth factor receptor (avian erythroblastic leukemia viral (v erb b) oncogene homolog) antibody;Epidermal growth factor receptor (erythroblastic leukemia viral (v erb b) oncogene homolog avian) antibody;Epidermal growth factor receptor antibody;erb-b2 receptor tyrosine kinase 1 antibody;ERBB antibody;ERBB1 antibody;Errp antibody;HER1 antibody;mENA antibody;NISBD2 antibody;Oncogen ERBB antibody;PIG61 antibody;Proto-oncogene c-ErbB-1 antibody;Receptor tyrosine protein kinase ErbB 1 antibody;Receptor tyrosine-protein kinase ErbB-1 antibody;SA7 antibody;Species antigen 7 antibody;Urogastrone antibody;v-erb-b Avian erythroblastic leukemia viral oncogen homolog antibody;wa2 antibody;Wa5 antibody

SUBCELLULAR LOCATION

Cell membrane, Endoplasmic reticulum membrane, Golgi apparatus membrane, Nucleus membrane, Endosome, Endosome membrane, Nucleus; Secreted.

FUNCTION

Epidermal growth factor receptor (EGFR) is a transmembrane protein that is activated by binding of its specific ligands, including epidermal growth factor and transforming growth factor alpha (TGF-α). ErbB2 has no known direct activating ligand, and may be in an activated state constitutively or become active upon heterodimerization with other family members such as EGFR. Upon activation by its growth factor ligands, EGFR undergoes a transition from an inactive monomeric form to an active homodimer. – although there is some evidence that preformed inactive dimers may also exist before ligand binding. In addition to forming homodimers after ligand binding, EGFR may pair with another member of the ErbB receptor family, such as ErbB2/Her2/neu, to create an activated heterodimer. There is also evidence to suggest that clusters of activated EGFRs form, although it remains unclear whether this clustering is important for activation itself or occurs subsequent to activation of individual dimers.