Anti-Human EGF (Clone 10827)

Purified Recombinant Human EGF (>98%)

This monoclonal antibody has been 0.2 µm filtered and lyophilized from modified Dulbecco's phosphate buffered saline (1X PBS) pH 7.2 - 7.3 containing 5.0% w/v trehalose with no calcium, magnesium or preservatives present.

The lyophilized antibody can be stored desiccated at -20°C to -70°C for up to twelve months. The reconstituted antibody can be stored for at least four weeks at 2-8°C. For long-term storage of the reconstituted antibody, aseptically aliquot into working volumes and store at -20°C to -70°C in a manual defrost freezer. Avoid repeated freeze thaw cycles. No detectable loss of activity was observed after six months.

Next Day Ambient

IHC (NBF/Par.): This antibody should give satisfactory staining results when used at a concentration of 25 µg/ml. The recommended secondary antibody for IHC is PN:M114. For chromogenic detection with high signal and low background use PN:D100 or PN:K107.

Mouse Anti-Human Epidermal Growth Factor (EGF) (Clone 10827) recognizes an epitope on Human EGF. This monoclonal antibody was purified using multi-step affinity chromatography methods such as Protein A or G depending on the species and isotype.

Epidermal growth factor or EGF is a growth factor that plays an important role in the regulation of cell growth, proliferation, and differentiation by binding to its receptor EGFR.¹ EGF acts by binding with high affinity to epidermal growth factor receptor (EGFR) on the cell surface and stimulating the intrinsic protein-tyrosine kinase activity of the receptor. This causes variety of biochemical changes within the cell - a rise in intracellular calcium levels, increased glycolysis and protein synthesis, and increases in the expression of certain genes including the gene for EGFR - that ultimately lead to DNA synthesis and cell proliferation.² EGF has been shown to regulate tumor cell invasion through activation of matrix metalloproteinase-2 (MMP-2) in various tumor cell types.³

1. Cohen, S. et al. (1995) J. Biol. Chem 265: 7709
2. Seroogy, KB. et al. (1995) Science 224: 1107
3. Cosen-Binker, LI. et al. (2009) Biochem Biophys Res Commun. 379: 445