Recombinant Human ErbB2/Her2 Fc Chimera Avi-tag Protein, CF Summary
Accession # P04626-1
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.
|Formulation||Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose.|
|Reconstitution||Reconstitute at 500 μg/mL in PBS.|
|Shipping||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.
2 μg/lane of Biotinylated Recombinant Human ErbB2/Her2 Fc Chimera Avi-tag (Catalog # AVI1129) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® blue staining, showing bands at 120-138 kDa and 240-280 kDa, respectively.
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).
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