EGF Receptor, Human Antibody from MILTENYI BIOTEC B.V. & Co. KG

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Antigenic SpecificityEGF Receptor, Human
CloneREA688
Host SpeciesRecombinant Human
Reactive Specieshuman
IsotypeIgG1
FormatVio Bright V423 conjugate
Size100 tests in 200 µL
Concentration1:50
ApplicationsFlow cytometry
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DescriptionEGF Receptor Antibody, anti-human, Vio® Bright V423, REAfinity™. Clone RE688 recognizes the human epidermal growth factor receptor (EGFR) antigen. EGFR is a single-pass type I membrane protein which is also known as receptor tyrosine-protein kinase ErbB-1 or HER1. It is a critical regulator of many normal cellular processes, including cell growth, differentiation, survival, and migration. The EGFR also is implicated in pathological processes of cellular transformation and oncogenesis due to its overexpression in many types of cancers and its ability to induce morphological transformation of cultured cells and tumor formation in nude mice. Many different signaling pathways have been discovered to mediate the effects of EGF, the most notable being Ras-mitogen-activated protein kinase (MAPK) and the phosphatidylinositol 3-kinase pathways. In these pathways EGF binds to the EGFR to induce dimerization, catalytic activation, and autophosphorylation of tyrosines in the C-terminal tail of the EGFR. These phosphorylated tyrosines provide docking sites for adapter proteins such as Grb2, Shc, and Gab2 to link the receptor to the Ras-MAPK, as well as phosphatidylinositol 3-kinase pathways. | Additional information: Clone REA688 displays negligible binding to Fc receptors.
Immunogenn/a
Other NamesEGFR
Gene, Accession #Gene ID: 1956
Catalog #130-128-181
Price$500
Order / More InfoEGF Receptor, Human Antibody from MILTENYI BIOTEC B.V. & Co. KG
Product Specific ReferencesUllrich, A. et al. (1984) Human epidermal growth factor receptor cDNA sequence and aberrant expression of the amplified gene in A431 epidermoid carcinoma cells. Nature 309 (5967): 418-425. | Bell, G. I. et al. (1986) Human epidermal growth factor precursor: cDNA sequence, expression in vitro and gene organization. Nucleic Acids Res. 14 (21): 8427-8446. | Heisermann, G. J. et al. (1988) Epidermal growth factor receptor threonine and serine residues phosphorylated in vivo. J. Biol. Chem. 263 (26): 13152-13158.
MILTENYI BIOTEC B.V. & Co. KG
MILTENYI BIOTEC B.V. & Co. KG
MILTENYI BIOTEC B.V. & Co. KG
Friedrich-Ebert-Straße 68
51429 Bergisch Gladbach GERMANY
P: +49 2204 8306-0
F: +49 2204 85197

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