*Optimal dilutions/concentrations should be determined by the researcher.
Not tested in other applications.
A431, rat ovary
Localizes blood type A-related determinants on various glycoproteins and glycolipids in addition to specific EGF receptor determinants (only observed in human tissue). Binds an external carbohydrate on the receptor and does not block EGF binding.
Ascites, 15 mM sodium azide
Store as concentrated solution. Centrifuge briefly prior to opening vial. For short-term storage (1-2 weeks), store at 4ºC. For long-term storage, aliquot and store at -20ºC or below. Avoid multiple freeze-thaw cycles.
human carcinoma cell line A431, which expresses high levels of EGF receptors.
For laboratory use only. Not for any clinical, therapeutic, or diagnostic use in humans or animals. Not for animal or human consumption.
Epidermal Growth Factor Receptor,Erbb,Erbb1,Her1,Nisbd2,Pig61,Mena,Egfr
The receptor for Epidermal Growth Factor is an integral cell membrane protein of 170 kDa, which spans the membranes of a wide range of normal and malignant epithelial cells. It is a tyrosine-specific protein kinase with the capacity to phosphorylate tyrosine residues located near its carboxy-terminus. EGF-R has anextracellular region which binds EGF and consequently mediates the initial response of cells to EGF and an intra- cellular region which posseses the tyrosine kinase activity. As a result of EGF binding to its specific receptor, there is increased DNA synthesis as well as other events such as cell proliferation, differentiationand repair of damaged epithelial tissue. The EGF-R has a half-life of approximately 10 hours in human fibroblasts, but in the presence of EGF this value is reduced to about 1 hour. A close similarity has been found between the sequence of the v-erb-B oncogene and the cytoplasmic and transmembrane part of the EGF-R (truncated EGF-R). It is hypothesized that an inappropriate activation of the human erb-B gene either by truncation or overexpression plays a role in the development of the malignancy. This hypothesis is supported by studies which have shown an increased number of EGF-R in various malignant tumors. High levels of EGF-R have been identified in sarcomas, gliomas, gynecological, breast, bladder and lungtumors.