Human CellExp ErbB3/HER3, human recombinant protein
ERBB3, ErbB-3, HER3, HER-3, LCCS2, MDA-BF-1, MGC88033, c-erbB-3, c-erbB3, erbB3-S, p180-ErbB3, p45-s
|Calculated MW||This protein is fused with a C-terminal 6×his tag and has a calculated MW of 71.5 kDa after removal of signal peptide. The predicted N-terminal is Ser 20. Protein migrates as 100-110 kDa in reduced SDS-PAGE resulting from glycosylation.|
|Other Names||ERBB3, ErbB-3, HER3, HER-3, LCCS2, MDA-BF-1, MGC88033, c-erbB-3, c-erbB3, erbB3-S, p180-ErbB3, p45-sErbB3, p85-sErbB3, Receptor tyrosine-protein kinase erbB-3|
|Results||Measured by its ability to inhibit the biological activity of Neuregulin1-β1 on MCF-7 human breast cancer cells, in the presence of 10 ng/ml recombinant Human NRG1-β1/HRG1-β1 Extracellular Domain. The ED50 for this effect is typically 0.5-3.0 µg/ml|
|Application Notes||Centrifuge the vial prior to opening. Reconstitute in sterile PBS, pH 7.4 to a concentration of 50 µg/ml. Do not vortex. This solution can be stored at 2-8°C for up to 1 month. For extended storage, it is recommended to store at -20°C.|
|Storage||-20°C; Lyophilized from 0.22 µm filtered solution in PBS, pH7.4. Generally 5-8% Mannitol or trehalose is added as a protectant before lyophilization.|
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Provided below are standard protocols that you may find useful for product applications.
ErbB3, also known as Her3 (human epidermal growth factor receptor 3), is a member of the epidermal growth factor receptor (EGFR) family of receptor tyrosine kinases. This membrane-bound glycoprotein has a neuregulin binding domain but has not an active kinase domain. It therefore can bind the ligand but cannot mediate the intracellular signal transduction through protein phosphorylation. However, it does form heterodimers with ErbB2 or other EGFR members responsible for tyrosine phosphorylation to give a receptor complex and initiate the related pathway, which lead to cell proliferation or differentiation. Overexpression of this protein has been reported in numerous cancers, including prostate, bladder, and breast tumors. This protein has different isoforms derived from alternative splicing variants, and among which, the secreted isoform lacking the intermembrane region modulates the activity of membrane-bound form.
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Katoh M.,et al.Biochem. Biophys. Res. Commun. 192:1189-1197(1993).
Kalnine N.,et al.Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
Ota T.,et al.Nat. Genet. 36:40-45(2004).
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