Recombinant Human ErbB2/Her2 Fc Chimera Protein, CF

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1 μg/lane of Recombinant Human ErbB2 Fc Chimera was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by silver staining, showing major bands at 125-130 kDa and 220-250 kDa, ...read more

Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

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Recombinant Human ErbB2/Her2 Fc Chimera Protein, CF Summary

Details of Functionality
Measured by its ability to block anti-ErbB2 mediated inhibition of SK‑BR‑3 human breast cancer cell proliferation. Brodowicz, T. et al. (1997) Int. J. Cancer 73:875. The ED50 for this effect is 0.3-1.2 μg/mL in the presence of 0.6 µg/mL Anti-Human ErbB2/Her2 Monoclonal Antibody (Trastuzumab, Catalog # MAB9589).
Source
Mouse myeloma cell line, NS0-derived human ErbB2/Her2 protein
Human Erb B2
(Thr23-Thr652)
Accession # NP_004439
IEGRMD Human IgG1
(Pro100-Lys330)
6 His-tag
N-terminus C-terminus
Accession #
N-terminal Sequence
Thr23
Structure / Form
Disulfide-linked homodimer
Protein/Peptide Type
Recombinant Proteins
Gene
ERBB2
Purity
>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Theoretical MW
96.8 kDa (monomer).
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
SDS-PAGE
125-130 kDa, reducing conditions
220-250 kDa, non-reducing conditions
Publications
Read Publications using
1129-ER in the following applications:

Packaging, Storage & Formulations

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.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS.
Purity
>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 100 μg/mL in sterile PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human ErbB2/Her2 Fc Chimera Protein, CF

  • CD340 antigen
  • CD340
  • c-erb B2/neu protein
  • EC 2.7.10
  • EGFR2
  • ErbB2
  • HER2
  • HER-2
  • HER2EC 2.7.10.1
  • herstatin
  • Metastatic lymph node gene 19 protein
  • MLN 19
  • MLN19
  • Neu Oncogene
  • NEUHER-2/neu
  • neuroblastoma/glioblastoma derived oncogene homolog
  • NGL
  • NGLTKR1
  • p185erbB2
  • Proto-oncogene c-ErbB-2
  • Proto-oncogene Neu
  • receptor tyrosine-protein kinase erbB-2
  • TKR1
  • Tyrosine kinase-type cell surface receptor HER2
  • v-erb-b2 avian erythroblastic leukemia viral oncogene homolog 2(neuro/glioblastoma derived oncogene homolog)
  • v-erb-b2 erythroblastic leukemia viral oncogene homolog 2, neuro/glioblastomaderived oncogene homolog (avian)

Background

ErbB2, also called Neu and Her2 (human epidermal growth factor receptor 2), 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. ErbB2 is widely expressed in epithelial cells and has also been found to be over-expressed in a large number of breast carcinomas. Among ErbB family members, ErbB2 is unique in that it has no identified ligands. Rather, ErbB2 heterodimerizes with the other members of the ErbB family (ErbB1 (EGFR), ErbB3, ErbB4) to form higher affinity signaling complexes. 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. Interestingly, this same three amino acid signal has also been found in ErbB1 and ErbB4. Phosphoinositide 3-kinase has been shown to play a role in ErbB2 signal transduction. The cytoplasmic domain of ErbB2 has been shown to associate with beta-catenin and plakoglobin. Human ErbB2 consists of 1255 amino acids (aa) with a 21 aa signal sequence, a 631 aa extracellular domain, a 23 aa transmembrane region, and a 580 aa cytoplasmic domain. ErbB2 can be shed from the cell surface by proteolytic cleavage by an unidentified protease. ErbB2 appears to play roles in development, cancer, communication at the neuromuscular junction and regulation of cell growth and differentiation (1-10).

  1. Coussens, L. et. al. (1985) Science 230:1132.
  2. Yamamoto, T. et. al. (1986) Nature 319:230.
  3. Kanai, Y. et. al. (1995) Biochem. Biophys. Res. Commun. 208:1067.
  4. Codony-Servat, J. et. al. (1999) Cancer Res. 59:1196.
  5. Carraway, K.L. 3rd et. al.  (1994) J. Biol. Chem. 269:14303.
  6. Emkey, R. and C.R. Kahn (1997) J. Biol. Chem. 272:31172.
  7. Schaefer, G. et. al. (1999) J. Biol. Chem. 274:859.
  8. Schlessinger, J. (2000) Cell 103:211.
  9. Hellyer, N.J. et. al. (2001) J. Biol. Chem. 276:42153.
  10. Daly, R.J. (1999) Growth Factors 16:255.

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Publications for ErbB2/Her2 (1129-ER)(40)

We have publications tested in 4 confirmed species: Human, Mouse, Drosophila, N/A.

We have publications tested in 13 applications: Bioassay, CAR-T (Bioassay), Direct ELISA, ELISA (Capture), ELISA (Standard), ELISA Capture, ELISA Developmet, Flow Cytometry, ICC, Protein Array, Surface Plasmon Resonance, Surface Plasmon Resonance (SPR, Western Blot.


Filter By Application
Bioassay
(19)
CAR-T (Bioassay)
(3)
Direct ELISA
(1)
ELISA (Capture)
(1)
ELISA (Standard)
(1)
ELISA Capture
(3)
ELISA Developmet
(2)
Flow Cytometry
(3)
ICC
(1)
Protein Array
(1)
Surface Plasmon Resonance
(2)
Surface Plasmon Resonance (SPR
(1)
Western Blot
(1)
All Applications
Filter By Species
Human
(24)
Mouse
(4)
Drosophila
(1)
N/A
(6)
All Species
Showing Publications 1 - 10 of 40. Show All 40 Publications.
Publications using 1129-ER Applications Species
M Crauwels, N Van Vaeren, B Kulaya Nee, C Vincke, M D'Huyvette, N Devoogdt, S Muylderman, C Xavier Reshaping Nanobodies for affinity purification on protein A N Biotechnol, 2020;0(0):. 2020 [PMID: 32001339] (Surface Plasmon Resonance (SPR, Human) Surface Plasmon Resonance (SPR Human
M Liberelle, R Magnez, X Thuru, Y Bencheikh, S Ravez, C Quenon, AS Drucbert, C Foulon, P Melnyk, IV Seuningen, N Lebègue MUC4-ErbB2 Oncogenic Complex: Binding studies using Microscale Thermophoresis Sci Rep, 2019;9(1):16678. 2019 [PMID: 31723153] (Bioassay, Human) Bioassay Human
J Medina-Ech, M Hinterberg, M Testori, M Geiger, R Giessel, B Bathke, R Kassub, F Gräbnitz, G Fiore, ST Wennier, P Chaplin, M Suter, H Hochrein, H Lauterbach Synergistic cancer immunotherapy combines MVA-CD40L induced innate and adaptive immunity with tumor targeting antibodies Nat Commun, 2019;10(1):5041. 2019 [PMID: 31695037] (ELISA Capture, Mouse) ELISA Capture Mouse
S Ahn, J Li, C Sun, K Gao, K Hirabayash, H Li, B Savoldo, R Liu, G Dotti Cancer immunotherapy with T cells carrying bispecific receptors that mimic antibodies Cancer Immunol Res, 2019;0(0):. 2019 [PMID: 30842091] (CAR-T (Bioassay), Human) CAR-T (Bioassay) Human
SJ Tobin, DL Wakefield, V Jones, X Liu, D Schmolze, T Jovanovi?- Single molecule localization microscopy coupled with touch preparation for the quantification of trastuzumab-bound HER2 Sci Rep, 2018;8(1):15154. 2018 [PMID: 30310083] (ICC, Human) ICC Human
CW Helsen, JA Hammill, VWC Lau, KA Mwawasi, A Afsahi, K Bezverbnay, L Newhook, DL Hayes, C Aarts, B Bojovic, GF Denisova, JM Kwiecien, I Brain, H Derocher, K Milne, BH Nelson, JL Bramson The chimeric TAC receptor co-opts the T cell receptor yielding robust anti-tumor activity without toxicity Nat Commun, 2018;9(1):3049. 2018 [PMID: 30076299]
M Pruszynski, CM Kang, E Koumariano, G Vaidyanath, MR Zalutsky d-Amino Acid Peptide Residualizing Agents for Protein Radioiodination: Effect of Aspartate for Glutamate Substitution Molecules, 2018;23(5):. 2018 [PMID: 29783774] (Bioassay, N/A) Bioassay N/A
M Kahl, F Settele, P Knick, U Haupts, E Bosse-Doen Mabfilin and Fabfilin - New antibody-scaffold fusion formats for multispecific targeting concepts Protein Expr. Purif., 2018;0(0):. 2018 [PMID: 29704557] (Bioassay) Bioassay
V Tolmachev, TJ Grönroos, CB Yim, J Garousi, Y Yue, S Grimm, J Rajander, A Perols, M Haaparanta, O Solin, R Ferdani, A Orlova, CJ Anderson, AE Karlström Molecular design of radiocopper-labelled Affibody molecules Sci Rep, 2018;8(1):6542. 2018 [PMID: 29695813] (Surface Plasmon Resonance, Human) Surface Plasmon Resonance Human
I Correa, KM Ilieva, S Crescioli, S Lombardi, M Figini, A Cheung, JF Spicer, ANJ Tutt, FO Nestle, P Karagianni, KE Lacy, SN Karagianni Evaluation of Antigen-Conjugated Fluorescent Beads to Identify Antigen-Specific B Cells Front Immunol, 2018;9(0):493. 2018 [PMID: 29628923] (Protein Array, Human) Protein Array Human
Show All 40 Publications.

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FAQs for ErbB2/Her2 (1129-ER). (Showing 1 - 1 of 1 FAQs).

  1. I am interested in getting antibodies for HER that would work in flow cytometry. Could you recommend some choices?
    • A list of our ErbB2 antibodies validated for use in flow cytometry can be found here /productsearch/HER2#fq=common_name%3A%22ErbB2%2FHER2%22&fq=category%3A%22Primary%20Antibodies%22&fq=applications%3A%22Flow%20Cytometry%22

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Gene Symbol ERBB2
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