HER3 / ERBB3 Protein, Human, Recombinant (Fc Tag)


HER3 / ERBB3 Protein, Human, Recombinant (Fc Tag): Product Information

> 90 % as determined by SDS-PAGE
< 1.0 EU per μg of the protein as determined by the LAL method
Measure by its ability to bind with human NRG1-β1 in a functional ELISA.
Protein Construction
A DNA sequence encoding the extracellular domain (Met 1-Thr 643) of human ErbB3 (NP_001973.2) precursor was expressed with the C-terminal fused Fc region of human IgG1.
Expressed Host
HEK293 Cells
Predicted N Terminal
Ser 20
Molecule Mass
The mature recombinant human ErbB3/Fc chimera is a disulfide-linked homodimeric protein after the removal of signal peptide. The monomer consists of 862 amino acids and has a calculated molecular mass of 95.4 kDa. As a result of glycosylation, the recombinant monomer migrates as an approximately 130-140 kDa protein in SDS-PAGE under reducing conditions.
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.
2. Please contact us for any concerns or special requirements.
Please refer to the specific buffer information in the hard copy of CoA.
In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature.
Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise.
Stability & Storage
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃
Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.

HER3 / ERBB3 Protein, Human, Recombinant (Fc Tag): Images

HER3 / ERBB3 Protein, Human, Recombinant (Fc Tag): Alternative Names

c-erbB-3 Protein, Human; c-erbB3 Protein, Human; EEBB3 Protein, Human; ErbB-3 Protein, Human; erbB3-S Protein, Human; HER3 Protein, Human; LCCS2 Protein, Human; MDA-BF-1 Protein, Human; p180-ErbB3 Protein, Human; p45-sErbB3 Protein, Human; p85-sErbB3 Protein, Human

HER3 / ERBB3 Background Information

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.
Full Name
erb-b2 receptor tyrosine kinase 3
  • Kraus M.H., et al.,(1989), Isolation and characterization of ERBB3, a third member of the ERBB/epidermal growth factor receptor family: evidence for overexpression in a subset of human mammary tumors. Proc. Natl. Acad. Sci. U.S.A. 86:9193-9197.
  • Plowman G.D., et al., (1990), Molecular cloning and expression of an additional epidermal growth factor receptor-related gene.Proc. Natl. Acad. Sci. U.S.A. 87:4905-4909.
  • Katoh M., et al.,(1993), c-erbB3 gene encodes secreted as well as transmembrane receptor tyrosine kinase.Biochem. Biophys. Res. Commun. 192:1189-1197.
  • Molecular Design of HER3-Targeting Affibody Molecules: Influence of Chelator and Presence of HEHEHE-Tag on Biodistribution of 68Ga-Labeled Tracers
    Dahlsson Leitao, C;Rinne, SS;Mitran, B;Vorobyeva, A;Andersson, KG;Tolmachev, V;Ståhl, S;Löfblom, J;Orlova, A;
    Int J Mol Sci
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