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V-Erb-B2 erythroblastic Leukemia Viral Oncogene Homolog 2, Neuro/glioblastoma Derived Oncogene Homolog (Avian) (ERBB2) (pThr1221, pThr1222) antibody
|Synonyms||Neu, HER2, HER-2, c-neu, Erbb-2, c-erbB2, mKIAA3023, NEU, NGL, TKR1, CD340, HER-2/neu|
Alternatives Western Blotting (WB)
|4 references available|
|Price||507.14 $ Plus shipping costs $45.00|
|Availability||Will be delivered in 2 to 3 Business Days|
|Description||Other names: ERBB2, HER2, NEU, NGL, Receptor tyrosine-protein kinase erbB-2, p185erbB2,C-erbB-2,NEU proto-oncogene,Tyrosine kinase-type cell surface receptor HER2,MLN 19|
|Characteristics||Rabbit Monoclonal Antibody|
|Specificity||A phosphor-specific peptide corresponding to residues surrounding tyrosine 1222 of human HER2 was used as an immunogen. This antibody detects HER2 phosphorylated at tyrosine 1222.|
|Molecular Weight||185 kDA|
Background: HER2 (ErbB2, epidermal growth factor receptor 2) is one of the four members of the ErbB receptor family of transmembrane receptor-like tyrosine kinases (1). The kinase activity of HER2 can be activated without ligand if it is overexpressed, and by association with other HER proteins (2). Overexpression of HER2 is detected in almost 40% of human breast cancers (3). HER2 is considered one of the major targets for the treatment of breast cancer and other carcinomas. Binding of c-Cbl ubiquitin ligase to Tyr1112 of HER2 leads to poly-ubiquitination of HER2 and enhances its degradation (4). Similar to other growth factors, HER2 exhibits intrinsic protein tyrosine kinase activity and undergoes autophosphorylation (Y1023, Y1248, Y1139, and Y1222). A phosphorylation at tyrosine 1139 has been identified to induce the binding of Src to HER2, leading to HER2 activation of Stat3 alpha (5).
|Application Notes||The suggested dilution is: WB: ~~ 1:5000|
|Buffer||50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.|
|Storage||HER2 Antibody Phospho (pT1221/T1222) can be stored at -20°C for up to 12 months from time of receipt.|
|Research Area||Ubiquitin-related antibodies, Phospho-specific antibodies, Cell Signaling, Protein Modifications, Cell Structure, Signaling, Chromatin|
|Restrictions||For Research Use only|
Segatto, Lonardo, Pierce et al.: "The role of autophosphorylation in modulation of erbB-2 transforming function." in: The New biologist, Vol. 2, Issue 2, pp. 187-95, 1991 (PubMed).
Muthuswamy, Gilman, Brugge: "Controlled dimerization of ErbB receptors provides evidence for differential signaling by homo- and heterodimers." in: Molecular and cellular biology, Vol. 19, Issue 10, pp. 6845-57, 2000 (PubMed).
Klapper, Waterman, Sela et al.: "Tumor-inhibitory antibodies to HER-2/ErbB-2 may act by recruiting c-Cbl and enhancing ubiquitination of HER-2." in: Cancer research, Vol. 60, Issue 13, pp. 3384-8, 2000 (PubMed).
Montgomery, Makary, Schiffman et al.: "Endogenous anti-HER2 antibodies block HER2 phosphorylation and signaling through extracellular signal-regulated kinase." in: Cancer research, Vol. 65, Issue 2, pp. 650-6, 2005 (PubMed).