Recombinant Human ErbB4/Her4 Fc Chimera Protein, CF

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Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

Order Details

Recombinant Human ErbB4/Her4 Fc Chimera Protein, CF Summary

Details of Functionality
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 µg/mL in the presence of 10 ng/mL of Recombinant Human NRG1‑ beta 1/HRG1‑ beta 1 Extracellular Domain (Catalog # 377-HB).
Source
Mouse myeloma cell line, NS0-derived human ErbB4/Her4 protein
Human ErbB4
(Gln26-Arg649)
Accession # Q15303
IEGRMD Human IgG1
(Pro100-Lys330)
6-His tag
N-terminus C-terminus
Accession #
N-terminal Sequence
Amino acid sequencing was blocked, suggesting it is consistent with Gln26 as the first N-terminal amino acid
Structure / Form
Disulfide-linked homodimer
Protein/Peptide Type
Recombinant Proteins
Gene
ERBB4
Purity
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Note
<0.01 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Theoretical MW
97 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
122-132 kDa, reducing conditions
Publications
Read Publications using
1131-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 under reducing conditions and visualized by silver stain
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 ErbB4/Her4 Fc Chimera Protein, CF

  • avian erythroblastic leukemia viral (v-erb-b2) oncogene homolog 4
  • EC 2.7.10
  • EC 2.7.10.1
  • ErbB4
  • HER4
  • HER4MGC138404
  • p180erbB4
  • Proto-oncogene-like protein c-ErbB-4
  • receptor tyrosine-protein kinase erbB-4
  • Tyrosine kinase-type cell surface receptor HER4
  • v-erb-a avian erythroblastic leukemia viral oncogene homolog-like 4
  • v-erb-a erythroblastic leukemia viral oncogene homolog 4 (avian)

Background

ErbB4, also called Her4 (human epidermal growth factor receptor 4), 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. ErbB4 is expressed in normal skeletal muscle, heart, pituitary, brain and several breast carcinomas. ErbB4 ligands include the neuregulins, beta-cellulin and heparin-binding EGF-like growth factor (HB-EGF). Monomeric ErbB4 binds its ligands with low affinity. Typically, heterodimerization with ErbB2 forms the high affinity receptor complex. However, ErbB4 has also been shown to heterodimerize with both ErbB1 and ErbB3. It has been suggested that the identity of the ligand may influence the dimerization partner. 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 been found in ErbB4 and ErbB1 (EGFR). Several ErbB4 isoforms exist. Two of these differ in the presence of juxtamembrane extracellular sequences which regulate the ability of TACE (TNF-alpha converting enzyme) to proteolytically cleave ErbB4 from the cell surface. These isoforms exhibit tissue-specific expression. Another isoform lacks the phosphoinositide 3-kinase activation sequence present in the ErbB4 cytoplasmic domain. Human ErbB4 consists of 1308 amino acids (aa) with a 25 aa signal sequence, a 626 aa extracellular domain, a 24 aa transmembrane region, and a 633 aa cytoplasmic domain. ErbB4 appears to play important roles in neuronal development, development of the heart and cancer.

  1. Plowman, G.D. et al. (1993) Proc. Natl. Acad. Sci. USA 90:1746. 
  2. Elenius, K. et al. (1997) J. Biol. Chem. 272:26761.
  3. Elenius, K. et al. (1999) Oncogene 18:2607.
  4. Rio, C. et al. (2000) J. Biol. Chem. 275:10379.
  5. Emkey, R. and C.R. Kahn (1997) J. Biol. Chem. 272:31172.
  6. Sundaresan, S. et al. (1998) Endocrinology 139:4756.
  7. Schaefer, G. et al. (1999) J. Biol. Chem. 274:859.
  8. Schlessinger, J. (2000) Cell 103:211.
  9. Daly, R.J. (1999) Growth Factors 16:255.

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1131-ER
Species: Hu
Applications: Bioactivity

Publications for ErbB4/Her4 (1131-ER)(8)

We have publications tested in 3 confirmed species: Human, Rat, N/A.

We have publications tested in 6 applications: Bioassay, DirELISA, Dot blot, ELISA capture, ELISA development, WB Standard.


Filter By Application
Bioassay
(3)
DirELISA
(1)
Dot blot
(1)
ELISA capture
(1)
ELISA development
(1)
WB Standard
(1)
All Applications
Filter By Species
Human
(4)
Rat
(1)
N/A
(1)
All Species
Showing Publications 1 - 8 of 8.
Publications using 1131-ER Applications Species
M Yun, DY Kim, JJ Lee, HS Kim, HS Kim, A Pyo, Y Ryu, TY Kim, JH Zheng, SW Yoo, H Hyun, G Oh, J Jeong, M Moon, JH Min, SY Kwon, JY Kim, E Chung, Y Hong, W Lee, HS Kim, JJ Min A High-Affinity Repebody for Molecular Imaging of EGFR-Expressing Malignant Tumors Theranostics, 2017;7(10):2620-2633. 2017 [PMID: 28819451] (ELISA development, N/A) ELISA development N/A
Tom J Parry Effects of neuregulin GGF2 (cimaglermin alfa) dose and treatment frequency on left ventricular function in rats following myocardial infarction Eur. J. Pharmacol, 2016;796(0):76-89. 2016 [PMID: 27993643] (Bioassay, Human) Bioassay Human
A Highly Diverse and Functional Na�ve Ubiquitin Variant Library for Generation of Intracellular Affinity Reagents J. Mol. Biol., 2016;0(0):. 2016 [PMID: 27887869] (DirELISA, Human) DirELISA Human
Sachdev S Sidhu A Highly Diverse and Functional Na�ve Ubiquitin Variant Library for Generation of Intracellular Affinity Reagents J. Mol. Biol., 2016;0(0):. 2016 [PMID: 27887869] (WB Standard) WB Standard
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 A HER2-specific Modified Fc Fragment (Fcab) Induces Antitumor Effects Through Degradation of HER2 and Apoptosis. Mol Ther, 2015;23(11):1722-33. 2015 [PMID: 26234505] (Bioassay, Human) Bioassay Human
Iaci JF, Ganguly A, Finklestein SP, Parry TJ, Ren J, Saha S, Sietsma DK, Srinivas M, Vecchione AM, Caggiano AO Glial growth factor 2 promotes functional recovery with treatment initiated up to 7 days after permanent focal ischemic stroke. Neuropharmacology, 2010;59(7):640-9. 2010 [PMID: 20691195] (ELISA capture, Human) ELISA capture Human
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 Design of an optimized scaffold for affibody molecules. J. Mol. Biol., 2010;398(2):232-47. 2010 [PMID: 20226194] (Dot blot) Dot blot
Hamra FK, Chapman KM, Nguyen D, Garbers DL Identification of neuregulin as a factor required for formation of aligned spermatogonia. J. Biol. Chem., 2007;282(1):721-30. 2007 [PMID: 17098736] (Bioassay, Rat) Bioassay Rat

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Bioinformatics

Gene Symbol ERBB4
Entrez
Uniprot