Recombinant Human ErbB3/Her3 His-tag 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 ED 50 for this effect is 0.3-3 µg/mL in the presence of 10 ng/mL Recombinant Human NRG1‑ beta 1/HRG1‑ beta 1 Extracellular Domain
(Catalog #
377-HB). |
Source |
Human embryonic kidney cell, HEK293-derived human ErbB3/Her3 protein Human ErbB3/Her3 (Ser20-Gly538) Accession # P21860-1 | YSKGSQSRMGGGGALQWNCSGGIQ | 6-His tag
| N-terminus | | C-terminus | |
|
Accession # |
|
N-terminal Sequence |
Ser20 |
Protein/Peptide Type |
Recombinant Proteins |
Purity |
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Endotoxin Note |
<1.0 EU per 1 μg of the protein by the LAL method. |
Applications/Dilutions
Dilutions |
|
Theoretical MW |
61 kDa. 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 |
73-83 kDa, under reducing conditions |
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 |
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Reconstitution Instructions |
Reconstitute at 500 μg/mL in PBS. |
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human ErbB3/Her3 His-tag Protein, CF
Background
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.
- Kraus, M.H. et al. (1989) Proc. Natl. Acad. Sci. 86:9193.
- Plowman, G.D. et al. (1990) Proc. Natl. Acad. Sci. USA 87:4905.
- Carraway, K.L. 3rd et al. (1994) J. Biol. Chem. 269:14303.
- Emkey, R. and C.R. Kahn (1997) J. Biol. Chem. 272:31172.
- Sundaresan, S. et al. (1998) Endocrinology 139:4756.
- Hellyer, N.J. et al. (1998) Biochem. J. 333:757.
- Schaefer, G. et al. (1999) J. Biol. Chem. 274:859.
- Hellyer, N.J. et al. (2001) J. Biol. Chem. 276:42153.
- Schlessinger, J. (2000) Cell 103:211.
- Daly, R.J. (1999) Growth Factors 16:255.
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