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Merck

E2645

Sigma-Aldrich

Epidermal Growth Factor Receptor human

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

Sinónimos:

ERBB, ErbB1, HER1, EGFR

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500 UNITS
1030,00 €

1030,00 €


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500 UNITS
1030,00 €

About This Item

Número MDL:
Código UNSPSC:
12352202
NACRES:
NA.32

1030,00 €


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origen biológico

human

Nivel de calidad

Formulario

lyophilized powder

potencia

>15000.00 units/mg

actividad específica

≥15,000 units/mg protein (Bradford)

mol peso

~170 kDa

envase

pkg of 500UN

condiciones de almacenamiento

avoid repeated freeze/thaw cycles

técnicas

cell based assay: suitable

color

white

solubilidad

glycerol: 10%, clear to slightly hazy, colorless

Nº de acceso UniProt

Condiciones de envío

dry ice

temp. de almacenamiento

−20°C

Información sobre el gen

human ... EGFR(1956)

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Descripción general

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.[1] These receptors are attached to the cytoplasmic membrane and [2] consist of an ectodomain (ECD), comprising of four subdomains called DI-DIV, a hydrophobic transmembrane domain, and an intracytoplasmic tyrosine kinase domain.

Acciones bioquímicas o fisiológicas

170 kDa glycoprotein having EGF-activated protein tyrosine kinase activity; 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.
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.[3] It is involved in the pathogenesis of epidermoid tumors, and thus, has extreme importance as a cancer therapeutic target.[4] Gefitinib (GEF) and erlotinib act as EGFR inhibitors, and induce apoptosis in non-small cell lung cancer (NSCLC) cells.[5] 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.[6]

Definición de unidad

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.

Forma física

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.

Nota de preparación

Affinity purified from human carcinoma A431 cells.

Código de clase de almacenamiento

11 - Combustible Solids

Clase de riesgo para el agua (WGK)

WGK 3

Punto de inflamabilidad (°F)

Not applicable

Punto de inflamabilidad (°C)

Not applicable


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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
EGFR/MDM2 signaling promotes NF-?B activation via PPAR? degradation
Xu Y, et al.
Carcinogenesis, 37(2), 215-222 (2016)
A comprehensive pathway map of epidermal growth factor receptor signaling
Oda K, et al.
Molecular Systems Biology (2005)
The Epidermal Growth Factor Receptor Pathway: A Model for Targeted Therapy
Scaltriti M and Baselga J
Journal of Separation Science null
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

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