Recombinant Human ErbB3/Her3 Fc Chimera Protein, CF

Catalog # Availability Size / Price Qty
348-RB-050

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Recombinant Human ErbB3/Her3 Fc Chimera Protein, CF Summary

Product Specifications

Purity
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Endotoxin Level
<0.01 EU per 1 μg of the protein by the LAL method.
Activity
Measured by its ability to inhibit the biological activity of Neuregulin-1-beta 1 on MCF‑7 human breast cancer cells. Karey, K.P. et al. (1988) Cancer Research 48:4083. The ED50 for this effect is 1.5-6.0 µg/mL in the presence of 10 ng/mL Recombinant Human NRG1‑ beta 1/HRG1‑ beta 1 Extracellular Domain (Catalog # 377-HB).
Source
Mouse myeloma cell line, NS0-derived human ErbB3/Her3 protein
Human ErbB3
(Ser20-Thr643)
Accession # P21860
IEGRMD Human IgG1
(Pro100-Lys330)
6-His tag
N-terminus C-terminus
Accession #
N-terminal Sequence
Analysis
Ser20
Structure / Form
Disulfide-linked homodimer
Predicted Molecular Mass
96 kDa (monomer)
SDS-PAGE
130-140 kDa, reducing conditions

Product Datasheets

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348-RB

Carrier Free

What does CF mean?

CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.

What formulation is right for me?

In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.

348-RB

Formulation Lyophilized from a 0.2 μm filtered solution in PBS.
Reconstitution Reconstitute at 100 μg/mL in sterile PBS.
Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
Reconstitution Calculator

Reconstitution Calculator

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Background: ErbB3/Her3

ErbB3, also called Her3 (human epidermal growth factor receptor 3), is a type I membrane glycoprotein that is a member of the ErbB family of tyrosine kinase receptors. ErbB family members serve as receptors for the epidermal growth factor (EGF) family of growth factors. Among ErbB family members, ErbB3 is unique in that it contains a defective kinase domain. ErbB3 is expressed in keratinocytes, melanocytes, skeletal muscle cells, embryonic myoblasts and Schwann cells. Monomeric ErbB3 serves as a low affinity receptor for the heregulins (HRG). ErbB3 heterodimerizes with ErbB2 to form a high affinity receptor complex. In contrast, ErbB3 homodimerization or heterodimerization with ErbB4 forms a low affinity heregulin-binding complex. Because ErbB3 contains a defective kinase domain, the kinase domain of ErbB2 is responsible for initiating the tyrosine phosphorylation signal through the heterodimeric receptor. It has been found that a discrete three amino acid signal in the ErbB3 cytoplasmic domain is critical for transactivation of ErbB2. The cytoplasmic domain of ErbB3 also contains six consensus binding motifs for the SH2 domain of the regulatory p85 subunit of phosphoinositide 3-kinase (PI 3-kinase, PI3K) as well as one proline-rich consensus binding motif for the SH3 domain of p85. Human ErbB3 consists of 1342 amino acids (aa) with a 19 aa signal sequence, a 624 aa extracellular domain, a 21 aa transmembrane region, and a 678 aa cytoplasmic domain. ErbB3 appears to play roles in development, cancer, communication at the neuromuscular junction and regulation of cell growth and differentiation

References
  1. Kraus, M.H. et. al. (1989) Proc. Natl. Acad. Sci. 86:9193.
  2. Plowman, G.D. et. al. (1990) Proc. Natl. Acad. Sci. USA 87:4905.
  3. Carraway, K.L. 3rd et. al. (1994) J. Biol. Chem. 269:14303.
  4. Emkey, R. and C.R. Kahn (1997) J. Biol. Chem. 272:31172.
  5. Sundaresan, S. et. al. (1998) Endocrinology 139:4756.
  6. Hellyer, N.J. et. al. (1998) Biochem. J. 333:757.
  7. Schaefer, G. et. al. (1999) J. Biol. Chem. 274:859.
  8. Hellyer, N.J. et. al. (2001) J. Biol. Chem. 276:42153.
  9. Schlessinger, J. (2000) Cell 103:211.
  10. Daly, R.J. (1999) Growth Factors 16:255.
Long Name
Receptor Tyrosine Protein Kinase ErbB3
Entrez Gene IDs
2065 (Human); 13867 (Mouse)
Alternate Names
c-erbB3; EC 2.7.10; EC 2.7.10.1; ErbB3; ErbB-3; erbB3-S; HER3; HER3c-erbB-3; LCCS2; lethal congenital contracture syndrome 2; MDA-BF-1; MGC88033; p180-ErbB3; p45-sErbB3; p85-sErbB3; Proto-oncogene-like protein c-ErbB-3; receptor tyrosine-protein kinase erbB-3; Tyrosine kinase-type cell surface receptor HER3; v-erb-b2 erythroblastic leukemia viral oncogene homolog 3 (avian)

Citations for Recombinant Human ErbB3/Her3 Fc Chimera Protein, CF

R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.

12 Citations: Showing 1 - 10
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  1. Inhibition of HER Receptors Reveals Distinct Mechanisms of Compensatory Upregulation of Other HER Family Members: Basis for Acquired Resistance and for Combination Therapy
    Authors: D Gutsch, R Jenke, T Büch, A Aigner
    Cells, 2021;10(2):.
    Species: Human
    Sample Types: Tissue Homogenates
  2. Evaluation of antibody fragment properties for near-infrared fluorescence imaging of HER3-positive cancer xenografts
    Authors: A El-Sayed, W Bernhard, K Barreto, C Gonzalez, W Hill, L Pastushok, H Fonge, CR Geyer
    Theranostics, 2018;8(17):4856-4869.
    Species: Human
    Sample Types: Recombinant Protein
    Applications: Surface Plasmon Resonance
  3. Soluble HER3 predicts survival in bladder cancer patients
    Authors: AA Memon, SC Gilliver, M Borre, J Sundquist, K Sundquist, E Nexo, BS Sorensen
    Oncol Lett, 2018;15(2):1783-1788.
    Applications: Bioassay
  4. Efficient generation of single domain antibodies with high affinities and enhanced thermal stabilities
    Authors: N Shinozaki, R Hashimoto, K Fukui, S Uchiyama
    Sci Rep, 2017;7(1):5794.
    Species: N/A
    Sample Types: Protein
    Applications: Bioassay
  5. Neuregulin 1 allosterically enhances the anti-tumor effects of the non-competing anti-HER3 antibody 9F7-F11 by increasing its binding to HER3
    Authors: C Le Clorenn, H Bazin, O Dubreuil, C Larbouret, C Ogier, Y Lazrek, V Garambois, MA Poul, P Mondon, JM Barret, G Mathis, JF Prost, A Pèlegrin, T Chardès
    Mol. Cancer Ther., 2017;0(0):.
    Species: Human
    Sample Types: Recombinant Protein
    Applications: Bioassay
  6. Neuregulin-1 type III knockout mice exhibit delayed migration of Schwann cell precursors
    Authors: Y Miyamoto, T Torii, A Tanoue, K Kawahara, M Arai, H Tsumura, T Ogata, M Nagao, N Terada, M Yamamoto, S Takashima, J Yamauchi
    Biochem. Biophys. Res. Commun, 2017;0(0):.
    Species: Rat
    Sample Types: Whole Cells
    Applications: Bioassay
  7. A Highly Diverse and Functional Na�ve Ubiquitin Variant Library for Generation of Intracellular Affinity Reagents
    J. Mol. Biol., 2016;0(0):.
    Species: Human
    Sample Types: Protein
    Applications: Direct ELISA
  8. A Highly Diverse and Functional Na�ve Ubiquitin Variant Library for Generation of Intracellular Affinity Reagents
    Authors: Sachdev S Sidhu
    J. Mol. Biol., 2016;0(0):.
    Applications: Western Blot
  9. A HER2-specific Modified Fc Fragment (Fcab) Induces Antitumor Effects Through Degradation of HER2 and Apoptosis.
    Authors: Leung K, Batey S, Rowlands R, Isaac S, Jones P, Drewett V, Carvalho J, Gaspar M, Weller S, Medcalf M, Wydro M, Pegram R, Mudde G, Bauer A, Moulder K, Woisetschlager M, Tuna M, Haurum J, Sun H
    Mol Ther, 2015;23(11):1722-33.
    Species: Human
    Sample Types: Recombinant Protein
    Applications: Bioassay
  10. Rapid optimization and prototyping for therapeutic antibody-like molecules.
    Authors: Xu, Lihui, Kohli, Neeraj, Rennard, Rachel, Jiao, Yang, Razlog, Maja, Zhang, Kathy, Baum, Jason, Johnson, Bryan, Tang, Jian, Schoeberl, Birgit, Fitzgerald, Jonathan, Nielsen, Ulrik, Lugovskoy, Alexey A
    MAbs, 2013;5(2):237-54.
    Species: Yeast
    Sample Types: Whole Cells
    Applications: Bioassay
  11. Design of an optimized scaffold for affibody molecules.
    Authors: Feldwisch J, Tolmachev V, Lendel C, Herne N, Sjoberg A, Larsson B, Rosik D, Lindqvist E, Fant G, Hoiden-Guthenberg I, Galli J, Jonasson P, Abrahmsen L
    J. Mol. Biol., 2010;398(2):232-47.
    Applications: Dot Blot
  12. Identification of neuregulin as a factor required for formation of aligned spermatogonia.
    Authors: Hamra FK, Chapman KM, Nguyen D, Garbers DL
    J. Biol. Chem., 2007;282(1):721-30.
    Species: Rat
    Sample Types: Whole Cells
    Applications: Bioassay

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Reviews for Recombinant Human ErbB3/Her3 Fc Chimera Protein, CF

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Recombinant Human ErbB3/Her3 Fc Chimera Protein, CF
By Jenna Nguyen on 05/07/2019
Application: Immunoassay Standard

Recombinant Human ErbB3/Her3 Fc Chimera Protein, CF
By Anonymous on 05/18/2016
Application: Binding assay/Protein-protein interaction
Reason for Rating: background is very low, signal is clear