Human embryonic kidney cell, HEK293-derived human ErbB3/Her3 protein
Human ErbB3/Her3 (Ser20-Gly538) Accession # P21860-1
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
<1.0 EU per 1 μg of the protein by the LAL method.
N-terminal sequence Analysis
Predicted Molecular Mass
73-83 kDa, under reducing conditions
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 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).
Recombinant Human ErbB3/Her3 His-tag Protein, CF Scientific Data Examples
Recombinant Human ErbB3/Her3 His-tag Protein Bioactivity
Recombinant Human ErbB3/Her3 His-tag (Catalog # 10368-RB) inhibits the biological activity of Recombinant Human NRG1-beta 1/HRG1-beta 1 ECD Protein (Catalog # 377-HB) on MCF-7 human breast cancer cells. The ED50 for this effect is 0.3-3 µg/mL.
Recombinant Human ErbB3/Her3 His-tag Protein SDS-PAGE
2 μg/lane of Recombinant Human ErbB3/Her3 His-tag (Catalog # 10368-RB) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 73-83 kDa.
Formulation, Preparation and Storage
What does CF mean?
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our
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
Lyophilized from a 0.2 μm filtered solution in PBS.
Reconstitute at 500 μg/mL in PBS.
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.
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.
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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.
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