详细说明
HER4 / ErbB4 Phospho (pY1162) Antibody Rabbit Monoclonal Antibody Cat.# 2295-1 Clone ID: EP2270YSwiss Prot: Q15303 Mol Weight: 180 kDaSize: 100ul
Description HER4 / ErbB4 is a receptor tyrosine kinase that belongs to the human epidermal growth factor receptor (EGFR) family. ErbB4/HER4 is most predominantly expressed in several breast carcinoma cell lines, and in normal skeletal muscle, heart, pituitary, brain, and cerebellum (1). ErbB4/HER4 is activated by neuregulins (NRG), betacellulin (BTC), and heparin-binding EGF-like growth factor (2). Neuregulins regulate the expression of ligand- and voltage-gated channels in neurons and skeletal muscle by the activation of ErbB 1-4. The erbB4/HER4 receptor is unique among these receptors because its C-terminal tail binds to a protein motif known as the PDZ domain (3). | |
Recommended Applications WB, IHC, IP | | Applications and Recommended Dilution Factors | | WB | IHC | ICC | FC | IP | | 1:25,000 | 1:100 | | | 1:30 | |
Species Reactivity* | | Human | Mouse | Rat | | Positive | Negative | Negative | *Cross reactivity determined by western blot only. | |
Product Data |
| | A. Western blot analysis on A431 cell lysates using anti-Phospho-Her4/ErbB-4 (pY1162) RabMAb (cat. #2295-1), 1:500 dilution. Cells were either (A) untreated (B) treated with EGF. | B. Immunohistochemical analysis of paraffin-embedded human breast carcinoma using anti-HER-4 RabMAb (cat. # 2295-1). | |
Specificity A phospho specific peptide corresponding to residues surrounding tyrosine 1162 of human Her4/ErbB-4 was used as an immunogen. This antibody detects Her4/ErbB-4 phosphorylated on tyrosine 1162. |
Storage Buffer & Conditions 50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA. |
Alternative Names ERBB4, HER4, Receptor tyrosine-protein kinase erbB-4, p180erbB4;Tyrosine kinase-type cell surface receptor HER4 |
Description References 1. Plowman, G.D., et al. Proc Natl Acad Sci U S A. 90: 1746 2. Elenius, K., et al. J Biol Chem. 272: 26761 3. Garcia, R.A., et al. Proc Natl Acad Sci U S A. 97: 3596 |