MABF119
Anti-EGFR Antibody, clone 528 (Azide-free)
clone 528, from mouse
Synonym(s):
Epidermal growth factor receptor, Proto-oncogene c-ErbB-1, Receptor tyrosine-protein kinase erbB-1
Sign Into View Organizational & Contract Pricing
All Photos(1)
About This Item
UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41
biological source
mouse
Quality Level
antibody form
purified antibody
antibody product type
primary antibodies
clone
528, monoclonal
species reactivity
human
technique(s)
immunoprecipitation (IP): suitable
neutralization: suitable
isotype
IgG2aκ
NCBI accession no.
UniProt accession no.
shipped in
dry ice
target post-translational modification
unmodified
Gene Information
human ... EGFR(1956)
General description
The epidermal growth factor receptor (EGFR; Proto-oncogene c-ErbB-1) is a ubiquitously receptor tyrosine kinase that is activated by a variety of ligands including EGF, EPGN, TGFA, and EREG. Ligand-bound EGFR undergoes dimerization and autophosphorylation exposing cytoplasmic domains which allow interaction with adaptor proteins and induction of several signaling pathways including PI3-AKT; PLCγ-PKC; Notch1; and Ras-Raf. EGFR therefore contributes to a diverse range of cellular processes inlcuding cell proliferation. Several studies have reported that EGFR signaling plays an important role in the development of various tumors. EGFR is regulated by PTPRJ and PTPRK phosphatases, and by the endocytic machinery including EPS15 that mediates internalization and degradation of the receptor.
Specificity
This antibody recognizes the extracellular domain of EGFR.
Immunogen
Partially purified human EGFR from A431 cells
Application
Anti-EGFR Antibody, clone 528 (Azide-free) detects level of EGFR & has been published & validated for use in Immunoprecipitation, Neutralizing.
Neutralizing Assay Analysis: A representative lot was used by an independent laboratory in A431 cells. (Kawamoto, T., et al. (1984). Journal of Biological Chemistry. 259(12):7761-7766.)
Quality
Evaluated by Immunoprecipitation in A431 cell lysate.
Immunoprecipitation Analysis: 10 µg of this antibody immunoprecipitated EGFR from A431 cell lysate.
Immunoprecipitation Analysis: 10 µg of this antibody immunoprecipitated EGFR from A431 cell lysate.
Target description
~170 kDa observed. Uniprot gives a calculated molecular weight of 135 but can be observed at ~170 kDa due to phosphorylation. (Konishi, A., et al. (2003). The Journal of Biological Chemistry. 278(37):35049–35056.)
Linkage
Replaces: 04-338
Physical form
Format: Purified
Other Notes
Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.
Not finding the right product?
Try our Product Selector Tool.
Storage Class
12 - Non Combustible Liquids
wgk_germany
WGK 2
flash_point_f
Not applicable
flash_point_c
Not applicable
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
Already Own This Product?
Find documentation for the products that you have recently purchased in the Document Library.
Relation of epidermal growth factor receptor concentration to growth of human epidermoid carcinoma A431 cells.
Kawamoto, T, et al.
The Journal of Biological Chemistry, 259, 7761-7766 (1984)
Valencio Salema et al.
mAbs, 8(7), 1286-1301 (2016-07-30)
Most therapeutic antibodies (Abs) target cell surface proteins on tumor and immune cells. Cloning of Ab gene libraries in E. coli and their display on bacteriophages is commonly used to select novel therapeutic Abs binding target antigens, either purified or
Growth stimulation of A431 cells by epidermal growth factor: identification of high-affinity receptors for epidermal growth factor by an anti-receptor monoclonal antibody.
Kawamoto, T, et al.
Proceedings of the National Academy of Sciences of the USA, 80, 1337-1341 (1983)
Antoine Lesur et al.
Proteomics. Clinical applications, 9(7-8), 695-705 (2015-02-07)
We report an immunocapture strategy to extract proteins known to harbor driver mutations for a defined cancer type before the simultaneous assessment of their mutational status by MS. Such a method bypasses the sensitivity and selectivity issues encountered during the
Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.
Contact Technical Service