Reactivity | HuSpecies Glossary |
Applications | Bioactivity |
Format | Carrier-Free |
Details of Functionality | Measured by its ability to block anti-ErbB2 mediated inhibition of SK‑BR‑3 human breast cancer cell proliferation. Brodowicz, T. et al. (1997) Int. J. Cancer 73:875. The ED50 for this effect is 0.3-1.2 μg/mL in the presence of 0.6 µg/mL Anti-Human ErbB2/Her2 Monoclonal Antibody
(Trastuzumab, Catalog #
MAB9589). |
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Source | Mouse myeloma cell line, NS0-derived human ErbB2/Her2 protein
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Accession # | |||||||||
N-terminal Sequence | Thr23 |
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Structure / Form | Disulfide-linked homodimer |
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Protein/Peptide Type | Recombinant Proteins |
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Gene | ERBB2 |
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Purity | >90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
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Endotoxin Note | <0.10 EU per 1 μg of the protein by the LAL method. |
Dilutions |
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Theoretical MW | 96.8 kDa (monomer). 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. |
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SDS-PAGE | 125-130 kDa, reducing conditions 220-250 kDa, non-reducing conditions |
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Publications |
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Storage | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Buffer | Lyophilized from a 0.2 μm filtered solution in PBS. |
Purity | >90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Reconstitution Instructions | Reconstitute at 100 μg/mL in sterile PBS. |
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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