PathScan® Total HER3/ErbB3 Sandwich ELISA kit #7888
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Supporting Data
| REACTIVITY | H |
Species Cross-Reactivity Key:
- H-Human
Product Information
Product Description
*Antibodies in this kit are custom formulations specific to kit.
Protocol
Specificity / Sensitivity
PathScan® Total HER3/ErbB3 Sandwich ELISA Kit #7888 detects endogenous levels of total HER3/ErbB3 protein in human cells. The kit sensitivity is shown in Figure 1. This kit does not cross-react with other proteins of ErbB family (data not shown). This kit detects proteins from the indicated species, as determined through in-house testing, but may also detect homologous proteins from other species.
Species Reactivity:
Human
Background
HER3/ErbB3 is a member of the ErbB receptor protein tyrosine kinase family, but it lacks tyrosine kinase activity. Tyrosine phosphorylation of ErbB3 depends on its association with other ErbB tyrosine kinases. Upon ligand binding, heterodimers form between ErbB3 and other ErbB proteins, and ErbB3 is phosphorylated on tyrosine residues by the activated ErbB kinase (1,2). There are at least 9 potential tyrosine phosphorylation sites in the carboxy-terminal tail of ErbB3. These sites serve as consensus binding sites for signal transducing proteins, including Src family members, Grb2, and the p85 subunit of PI3 kinase, which mediate ErbB downstream signaling (3). Both Tyr1222 and Tyr1289 of ErbB3 reside within a YXXM motif and participate in signaling to PI3K (4).
Investigators have found that ErbB3 is highly expressed in many cancer cells (5) and activation of the ErbB3/PI3K pathway is correlated with malignant phenotypes of adenocarcinomas (6). Research studies have demonstrated that in tumor development, ErbB3 may function as an oncogenic unit together with other ErbB members (e.g., ErbB2 requires ErbB3 to drive breast tumor cell proliferation) (7). Thus, investigators view inhibiting interaction between ErbB3 and ErbB tyrosine kinases as a novel strategy for anti-tumor therapy.
- Yarden, Y. and Sliwkowski, M.X. (2001) Nat Rev Mol Cell Biol 2, 127-37.
- Guy, P.M. et al. (1994) Proc Natl Acad Sci USA 91, 8132-6.
- Songyang, Z. et al. (1993) Cell 72, 767-78.
- Kim, H.H. et al. (1994) J Biol Chem 269, 24747-55.
- Sithanandam, G. et al. (2003) Carcinogenesis 24, 1581-92.
- Kobayashi, M. et al. (2003) Oncogene 22, 1294-301.
- Holbro, T. et al. (2003) Proc Natl Acad Sci USA 100, 8933-8.
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