• Purity

  >90%, by SDS-PAGE with silver staining

• Endotoxin Level

  <0.10 EU per 1 μg of the protein by the LAL method.  

• Activity

  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 20-80 ng/mL in the presence of 0.6 µg/mL goat anti-hErbB2 (Catalog # AF1129).

• Source

  Mouse myeloma cell line, NS0-derived

  Human Erb B2 (Thr23 - Thr652) Accession # NP_004439	IEGRMD	Human IgG1 (Pro100 - Lys330)	6 His-tag
  N-terminus			C-terminus

• Accession #

• N-terminal Sequence    
  Analysis

  Thr23

• Structure / Form

  Disulfide-linked homodimer

• Predicted Molecular Mass

  96.8 kDa (monomer)

• SDS-PAGE

  125-130 kDa, reducing conditions

  220-250 kDa, non-reducing conditions

Data Images

Background: ErbB2/Her2

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).

• References:

  
  

1. Coussens, L. et. al. (1985) Science 230:1132.

2. Yamamoto, T. et. al. (1986) Nature 319:230.

3. Kanai, Y. et. al. (1995) Biochem. Biophys. Res. Commun. 208:1067.

4. Codony-Servat, J. et. al. (1999) Cancer Res. 59:1196.

5. Carraway, K.L. 3^rd et. al.  (1994) J. Biol. Chem. 269:14303.

6. Emkey, R. and C.R. Kahn (1997) J. Biol. Chem. 272:31172.

7. Schaefer, G. et. al. (1999) J. Biol. Chem. 274:859.

8. Schlessinger, J. (2000) Cell 103:211.

9. Hellyer, N.J. et. al. (2001) J. Biol. Chem. 276:42153.

10. Daly, R.J. (1999) Growth Factors 16:255.

• Long Name:

  Receptor Tyrosine Protein Kinase ErbB2

• Entrez Gene IDs:

  2064 (Human); 13866 (Mouse); 24337 (Rat)

• Alternate Names:

  CD340 antigen; CD340; c-erb B2/neu protein; EC 2.7.10; EGFR2; ErbB2; HER2; HER-2; HER2EC 2.7.10.1; herstatin; Metastatic lymph node gene 19 protein; MLN 19; MLN19; Neu Oncogene; NEUHER-2/neu; neuroblastoma/glioblastoma derived oncogene homolog; NGL; NGLTKR1; p185erbB2; Proto-oncogene c-ErbB-2; Proto-oncogene Neu; receptor tyrosine-protein kinase erbB-2; TKR1; Tyrosine kinase-type cell surface receptor HER2; v-erb-b2 avian erythroblastic leukemia viral oncogene homolog 2(neuro/glioblastoma derived oncogene homolog); v-erb-b2 erythroblastic leukemia viral oncogene homolog 2, neuro/glioblastomaderived oncogene homolog (avian)