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

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

Purity
> 95 % as determined by SDS-PAGE
Endotoxin
< 1.0 EU per μg of the protein as determined by the LAL method
Activity
Measured by its binding ability in a functional ELISA.
Immobilized human ErbB3-mFc at 10 μg/ml (100 μl/well) can bind biotinylated human NRG1 (Cat:11609-H01H2), The EC50 of biotinylated human NRG1 (Cat:11609-H01H2) is 0.58-1.25 μg/ml.
Protein Construction
A DNA sequence encoding the human ErbB3 (NP_001973.2) (Met1-Thr643)was fused with Fc region of mouse IgG at the C-terminus.
Accession#
Expressed Host
HEK293 Cells
Species
Human
Predicted N Terminal
Ser 20
Molecule Mass
The recombinant human ErbB3/mFc is a disulfide-linked homodimer. The reduced monomer comprises 858 amino acids and has a predicted molecular mass of 95 kDa. The apparent molecular mass of the protein is approximately 119-129 in SDS-PAGE under reducing conditions.
Formulation
Lyophilized from sterile PBS, pH 7.4.
Please contact us for any concerns or special requirements.
Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization.
Please refer to the specific buffer information in the hard copy of CoA.
Shipping
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.
Reconstitution
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
References
  • 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.
  • Optimization of HER3 expression imaging using affibody molecules: Influence of chelator for labeling with indium-111
    Author
    Rinne, SS;Leitao, CD;Mitran, B;Bass, TZ;Andersson, KG;Tolmachev, V;Ståhl, S;Löfblom, J;Orlova, A;
    Year
    2019
    Journal
    Sci Rep
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