Recombinant Human ErbB3/Her3 Fc Chimera Avi-tag Protein, CF

Recombinant Human ErbB3/Her3 Fc Chimera Avi-tag Protein, CF Summary

Product Specifications

Product Datasheets

Carrier Free

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.

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.

Background: ErbB3/Her3

ErbB3, also called human epidermal growth factor receptor 3 (HER3), 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 (1). Human ErbB3 consists of an extracellular domain (ECD) with four, ligand binding subdomains, I-IV, a transmembrane domain and a cytoplasmic region with a defective kinase domain unique among ErbB family members (1-3). Additionally, the cytoplasmic region 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 (1-3). The mature ECD of human ErbB3 shares 92% amino acid sequence identity with the ECD of mouse and rat ErbB3. ErbB3 is expressed in keratinocytes, melanocytes, skeletal muscle cells, embryonic myoblasts and Schwann cells. ErbB3 appears to play roles in development, cancer, communication at the neuromuscular junction and regulation of cell growth and differentiation (4, 5). 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 (6, 7). Because ErbB3 contains a defective kinase domain, the kinase domain of ErbB2 is responsible for initiating the tyrosine phosphorylation signal through the heterodimeric receptor (8). It has been found that a discrete three amino acid signal in the ErbB3 cytoplasmic domain is critical for transactivation of ErbB2 (9). ErbB3 overexpression in various solid tumor is associated with shorter survival of patients and, subsequently, ErbB3 signaling is a target for cancer therapy. Current clinical results suggested that ErbB3 therapies may have the most efficacy in combination therapy (10). Biotinylated Recombinant Human ErbB3 Fc Chimera Avi-tag protein has high binding affinity to Recombinant Human NRG1-beta 1. Our Avi-tag Biotinylated ErbB3 features biotinylation at a single site contained within the Avi-tag, a unique 15 amino acid peptide. Protein orientation will be uniform when bound to streptavidin-coated surface due to the precise control of biotinylation.

Related Research Areas

• Cancer Biomarkers
• EGF Family
• Receptor Tyrosine Kinases (RTKs)
• Receptor Tyrosine Kinases (RTKs) in the Akt Pathway