|ErbB2/Her2 in MCF-7 Human Cell Line. ErbB2/Her2 was detected in immersion fixed MCF‑7 human breast cancer cell line using Goat Anti-Human ErbB2/Her2 Biotinylated Antigen Affinity-purified Polyclonal Antibody (Catalog # BAF1129) at 10 µg/mL for 3 hours at room temperature. Cells were stained using the NorthernLights™ 557-conjugated Streptavidin (yellow; Catalog # NL999) and counterstained with DAPI (blue). View our protocol for Fluorescent ICC Staining of Cells on Coverslips.|
|ErbB2/Her2 in Human Breast Cancer Tissue. ErbB2/Her2 was detected in immersion fixed paraffin-embedded sections of human breast cancer tissue using Goat Anti-Human ErbB2/Her2 Biotinylated Antigen Affinity-purified Polyclonal Antibody (Catalog # BAF1129) at 15 µg/mL overnight at 4 °C. Tissue was stained using the Anti-Goat HRP-DAB Cell & Tissue Staining Kit (brown; Catalog # CTS008) and counterstained with hematoxylin (blue). Specific staining was localized to plasma membrane. View our protocol for Chromogenic IHC Staining of Paraffin-embedded Tissue Sections.|
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 (EGF R), 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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Immunocytochemistry/Immunoflourescence: Human ErbB2/Her2 Biotinylated Antibody [BAF1129]
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