Rabbit Anti-EGFR Polyclonal Antibody #abs130340

abs130340-50ug

1-2 Weeks

201

abs130340-100ug

1-2 Weeks

301

Description

EGFR, also known as epidermal growth factor receptor, is a receptor tyrosine kinase that plays a crucial role in cell growth and differentiation. It functions as a receptor for several growth factors, including EGF, TGF-alpha, betacellulin, amphiregulin, heparin-binding EGF-like growth factor, GP30, and vaccinia virus growth factor. This receptor is located on the cell membrane and possesses a single-pass transmembrane tyrosine kinase domain.
When a ligand binds to EGFR, it induces receptor dimerization and triggers autophosphorylation, resulting in the activation of downstream signaling molecules. The activated EGFR can also undergo lysosomal degradation. Src, a non-receptor tyrosine kinase, can phosphorylate and activate EGFR. The phosphorylated EGFR binds to the SH2 domain of phospholipase C-gamma (PLC-gamma), leading to the activation of downstream signaling mediated by PLC-gamma.
Cbl, a ubiquitin ligase, binds to the phosphorylated EGFR, which marks it for ubiquitination and subsequent degradation. Additionally, the phosphorylated EGFR binds to Grb2 and SHC, which are involved in the activation of MAP kinase signaling pathways. Phosphorylation of EGFR on specific serine and threonine residues is believed to play a role in the attenuation of its kinase activity.
EGFR is frequently overexpressed in breast and head and neck cancers, which is associated with poor prognosis. Activating somatic mutations of EGFR have been observed in lung cancer and are correlated with a significant response to EGFR inhibitor Iressa (gefitinib) in a minority of patients. Mutations and amplification of EGFR are also found in glioblastoma, while upregulation of EGFR is observed in colon cancer and other neoplasms.
In preclinical studies using xenografts, EGFR inhibitors have shown synergistic effects with cytotoxic drugs in inhibiting various tumor types. Some of the approved inhibitors targeting EGFR include Iressa/ZD1839, Erbitux, Tarceva, and lapatinib. Alternative splicing of EGFR gives rise to four isoforms with distinct properties.
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Other names

Avian erythroblastic leukemia viral (v erb b) oncogene homolog is a protein known as EGF R or EGFR, which stands for Epidermal growth factor receptor. It is also referred to as EGFR_HUMAN and ERBB1. This protein is involved in cell growth inhibition and cell proliferation induction. It plays a crucial role in various biological processes and is associated with diseases like leukemia. Its function as a receptor tyrosine protein kinase ErbB-1 makes it a potential target for therapeutic interventions. Additionally, it is also known by other names such as Cell growth inhibiting protein 40, Cell proliferation inducing protein 61, Oncogen ERBB, Proto-oncogene c-ErbB-1, and Species antigen 7. Understanding the mechanisms and interactions of this protein is vital for developing effective treatments for related diseases.

Source

Rabbit

Specificity

EGFR Antibody detects endogenous levels of EGFR

Species Reactivity

Human;Mouse;Rat

Application

WB 1:500-1:2000, ELISA(peptide) 1:20000-1:40000

Immunogen

A synthesized peptide derived from human EGFR

Properties

Concentration

1mg/ml

Purification

Immunogen affinity purified

Clonality

Polyclonal Antibody

Stability & Storage

Store at -20 °C for one year. Avoid repeated freeze/thaw cycles

Storage buffer

Rabbit IgG in phosphate buffered saline , pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.Store at -20 °C.Stable for 12 months from date of receipt

Target

Background

Receptor tyrosine kinase binding ligands of the EGF family and activating several signaling cascades to convert extracellular cues into appropriate cellular responses. Known ligands include EGF, TGFA/TGF-alpha, amphiregulin, epigen/EPGN, BTC/betacellulin, epiregulin/EREG and HBEGF/heparin-binding EGF. Ligand binding triggers receptor homo- and/or heterodimerization and autophosphorylation on key cytoplasmic residues. The phosphorylated receptor recruits adapter proteins like GRB2 which in turn activates complex downstream signaling cascades. Activates at least 4 major downstream signaling cascades including the RAS-RAF-MEK-ERK, PI3 kinase-AKT, PLCgamma-PKC and STATs modules. May also activate the NF-kappa-B signaling cascade. Also directly phosphorylates other proteins like RGS16, activating its GTPase activity and probably coupling the EGF receptor signaling to the G protein-coupled receptor signaling. Also phosphorylates MUC1 and increases its interaction with SRC and CTNNB1/beta-catenin. Plays a role in enhancing learning and memory performance (By similarity).

Tissue specificity

Ubiquitously expressed. Isoform 2 is also expressed in ovarian cancers.

Posttranslational modification

Phosphorylation at Ser-695 is partial and occurs only if Thr-693 is phosphorylated. Phosphorylation at Thr-678 and Thr-693 by PRKD1 inhibits EGF-induced MAPK8/JNK1 activation. Dephosphorylation by PTPRJ prevents endocytosis and stabilizes the receptor at the plasma membrane. Autophosphorylation at Tyr-1197 is stimulated by methylation at Arg-1199 and enhances interaction with PTPN6. Autophosphorylation at Tyr-1092 and/or Tyr-1110 recruits STAT3. Dephosphorylated by PTPN1 and PTPN2.Monoubiquitinated and polyubiquitinated upon EGF stimulation; which does not affect tyrosine kinase activity or signaling capacity but may play a role in lysosomal targeting. Polyubiquitin linkage is mainly through 'Lys-63', but linkage through 'Lys-48', 'Lys-11' and 'Lys-29' also occurs. Deubiquitination by OTUD7B prevents degradation. Ubiquitinated by RNF115 and RNF126 (By similarity).Methylated. Methylation at Arg-1199 by PRMT5 stimulates phosphorylation at Tyr-1197.

Celluar localization

Endoplasmic reticulum;Endosome;Extracellular region or secreted;Golgi apparatus;Nucleus;Plasma Membrane;

UniPort

P00533