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E3641

Sigma-Aldrich

Epidermal Growth Factor Receptor human

buffered aqueous glycerol solution, 5,000-30,000 units/mg protein (Lowry)

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Synonym(s):
EGFR
MDL number:
NACRES:
NA.32

biological source

human

Quality Level

form

buffered aqueous glycerol solution

potency

5000.00-30000.00 units/mg

specific activity

5,000-30,000 units/mg protein (Lowry)

mol wt

~170 kDa

packaging

pkg of 500UN

storage condition

avoid repeated freeze/thaw cycles

color

colorless

UniProt accession no.

shipped in

dry ice

storage temp.

−70°C

Gene Information

human ... EGFR(1956)

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This Item
E2645SRP0242SRP0239
vibrant-m

SRP0242

EGFR (T790M L858R) Active human

vibrant-m

SRP0239

EGFR Active human

Quality Level

300

Quality Level

300

Quality Level

-

Quality Level

-

storage temp.

−70°C

storage temp.

−20°C

storage temp.

−70°C

storage temp.

−70°C

storage condition

avoid repeated freeze/thaw cycles

storage condition

avoid repeated freeze/thaw cycles

storage condition

avoid repeated freeze/thaw cycles

storage condition

-

UniProt accession no.

P00533

UniProt accession no.

P00533

UniProt accession no.

P00533

UniProt accession no.

P00533

shipped in

dry ice

shipped in

dry ice

shipped in

dry ice

shipped in

dry ice

General description

Affinity purified from human carcinoma A431 cells.
Epidermal growth factor receptor (EGFR) belongs to a family of cell surface receptors called receptor tyrosine kinases (RTKs), and is also the most studied member of this family. It is made up of an ectodomain (ECD), which contains four subdomains called DI-DIV, a transmembrane region, and a cytoplasmic tyrosine kinase domain (TKD). Binding of the ligand induces conformational changes in the ECD, which leads to the dimerization of EGFR. This results in the activation of the TKD, and the subsequent signal transduction. This receptor has a molecular weight of ∼178kDa.

Biochem/physiol Actions

EGF exerts its actions by binding to the EGF receptor (EGFR), a 170 kDa glycoprotein having EGF-activated protein tyrosine kinase activity. Even in the absence of EGF-like ligands, EGFR can participate in cellular responses elicited by several other stimuli. High levels of EGFR are expressed in approximately one third of human epithelial tumors, and in the cancers of the bladder, breast or lung that have poor clinical prognosis, hence the interest in targeting EGFR.
Epidermal growth factor receptor (EGFR) has an essential role in normal developmental processes, and is mutated in multiple cancers. It is involved in the pathogenesis of epidermoid tumors, and thus, has extreme importance as a cancer therapeutic target. Gefitinib (GEF) and erlotinib act as EGFR inhibitors, and induce apoptosis in non-small cell lung cancer (NSCLC) cells. A truncated isoform, called EGFRvIII is linked to multiple cases of head and neck squamous cell carcinoma (HNSCC). In ~40% of glioblastoma multiforme (GBM), this gene is amplified.

Unit Definition

One unit (U) of the enzyme is defined as the amount needed to incorporate 1 pmol of phosphate into the substrate (KVEKIGEGTYGVVYK: 6 - 20 residue of p34cdc2) in 1 minute.

Physical form

Solution in 50% glycerol, containing 50 mM HEPES, pH 7.6, 150 mM NaCl, 0.1% Triton and 1 mM dithiothreitol

Storage Class

10 - Combustible liquids

wgk_germany

WGK 2

flash_point_f

Not applicable

flash_point_c

Not applicable


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Customers Also Viewed

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1 of 2

Sarah E Wheeler et al.
PloS one, 10(2), e0117781-e0117781 (2015-02-07)
Head and neck squamous cell carcinoma (HNSCC) accounts for more than 5% of all cancers worldwide. The mortality rate of HNSCC has remained unchanged (approximately 50%) over the last few decades. Ubiquitous overexpression of wild type EGFR in many solid
Shohei Sugita et al.
Biochemical and biophysical research communications, 461(1), 28-34 (2015-04-11)
Gefitinib (GEF), an inhibitor for EGFR tyrosine kinase, potently induces autophagy in non-small cell lung cancer (NSCLC) cell lines such as PC-9 cells expressing constitutively activated EGFR kinase by EGFR gene mutation as well as A549 and H226 cells with
Karol Kaszuba et al.
Proceedings of the National Academy of Sciences of the United States of America, 112(14), 4334-4339 (2015-03-26)
The epidermal growth factor receptor (EGFR) regulates several critical cellular processes and is an important target for cancer therapy. In lieu of a crystallographic structure of the complete receptor, atomistic molecular dynamics (MD) simulations have recently shown that they can
Nicholas J Bessman et al.
Cell reports, 9(4), 1306-1317 (2014-12-03)
The epidermal growth factor receptor (EGFR) plays pivotal roles in development and is mutated or overexpressed in several cancers. Despite recent advances, the complex allosteric regulation of EGFR remains incompletely understood. Through efforts to understand why the negative cooperativity observed
Kristen J Champion et al.
Cancer research, 68(12), 4649-4657 (2008-06-19)
von Hippel-Lindau (VHL) disease results from germline and somatic mutations in the VHL tumor suppressor gene and is characterized by highly vascularized tumors. VHL mutations lead to stabilization of hypoxia-inducible factor (HIF), which up-regulates proangiogenic factors such as vascular endothelial

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