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E2645

Sigma-Aldrich

Epidermal Growth Factor Receptor human

lyophilized powder, ≥15,000 units/mg protein (Bradford)

Synonyme(s) :

ERBB, ErbB1, HER1, EGFR

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About This Item

Numéro MDL:
Code UNSPSC :
12352202
Nomenclature NACRES :
NA.32

Source biologique

human

Niveau de qualité

Forme

lyophilized powder

Puissance

>15000.00 units/mg

Activité spécifique

≥15,000 units/mg protein (Bradford)

Poids mol.

~170 kDa

Conditionnement

pkg of 500UN

Conditions de stockage

avoid repeated freeze/thaw cycles

Technique(s)

cell based assay: suitable

Couleur

white

Solubilité

glycerol: 10%, clear to slightly hazy, colorless

Numéro d'accès UniProt

Conditions d'expédition

dry ice

Température de stockage

−20°C

Informations sur le gène

human ... EGFR(1956)

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Description générale

Research area: Cell signaling

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. The EGFR is encoded by the ErbB gene, mapped to chromosome 7 q22. These receptors are attached to the cytoplasmic membrane and consist of an ectodomain (ECD), comprising of four subdomains called DI-DIV, a hydrophobic transmembrane domain, and an intracytoplasmic tyrosine kinase domain.

Actions biochimiques/physiologiques

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.

Définition de l'unité

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.

Forme physique

Lyophilized from a solution in 50 mM HEPES, pH 7.6, 150 mM NaCl, 0.05% Triton X-100, 1 mM dithiothreitol, and 10% trehalose.

Notes préparatoires

Affinity purified from human carcinoma A431 cells.

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


Certificats d'analyse (COA)

Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".

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Consulter la Bibliothèque de documents

A comprehensive pathway map of epidermal growth factor receptor signaling
Oda K, et al.
Molecular Systems Biology (2005)
EGFR/MDM2 signaling promotes NF-?B activation via PPAR? degradation
Xu Y, et al.
Carcinogenesis, 37(2), 215-222 (2016)
Qian Gou et al.
Oncogene, 39(25), 4844-4853 (2020-05-23)
In response to nutrient deficiency, autophagy degrades cytoplasmic materials and organelles in lysosomes, which is nutrient recycling, whereas activation of EGFR mediates autophagy suppression in response to growth factors. It is unclear whether PPARδ could be the regulator of autophagy
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
The Epidermal Growth Factor Receptor Pathway: A Model for Targeted Therapy
Scaltriti M and Baselga J
Journal of Separation Science null

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