Rat HER3 / ErbB3 Protein (His Tag)
ERBB3
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| Catalog Number | P80111-R08H |
|---|---|
| Organism Species | Rat |
| Host | Human Cells |
| Synonyms | ERBB3 |
| Molecular Weight | The recombinant rat ERBB3 comprises 633 amino acids and predicts a molecular mass of 69.9 kDa. The apparent molecular mass of the recombinant protein is approximately 112 kDa in SDS-PAGE under reducing conditions due to glycosylation. |
| predicted N | Ser 20 |
| SDS-PAGE |  |
| Purity | > 95 % as determined by SDS-PAGE |
| Protein Construction | A DNA sequence encoding the rat ERBB3 (Q3MHC0) (Met1-His641) was expressed, fused with a polyhistidine tag at the C-terminus. |
| Bio-activity | Measured by its binding ability in a functional ELISA. Immobilized rat ERBB3-His at 10 μg/ml (100 μl/well) can bind biotinylated human NRG1 (P11609-H01H2), The EC50 of biotinylated human NRG1 (P11609-H01H2) is 1.1-2.6 μg/ml. |
| Research Area | Cardiovascular |Angiogenesis |Growth Factor & Receptor |Epidermal Growth Factor (EGF) & Receptor |EGF Receptor |
| Formulation | Lyophilized from sterile PBS, pH 7.4 1. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA. |
| Background | ErbB3, also known as Her3(human epidermal growth factor receptor3), 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., and therefore can not mediate the intracellular signal transduction through protein phosphorylation. However, its heterodimer with ErbB2 or other EGFR members responsible for tyrosine phosphorylation forms a receptor complex with high affinity, and initiates the related pathway which lead to cell proliferation or differentiation. ErbB3 has been shown to implicated 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. |
| Reference |