Phospho-mouse ERBB2(Y1223) Antibody
Affinity Purified Rabbit Polyclonal Antibody (Pab)
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application
| DB, E |
---|---|
Primary Accession | P70424 |
Other Accession | P06494, NP_001003817.1 |
Reactivity | Mouse |
Predicted | Rat |
Host | Rabbit |
Clonality | Polyclonal |
Isotype | Rabbit IgG |
Calculated MW | 138579 Da |
Gene ID | 13866 |
---|---|
Other Names | Receptor tyrosine-protein kinase erbB-2, Proto-oncogene Neu, Proto-oncogene c-ErbB-2, p185erbB2, CD340, Erbb2, Kiaa3023, Neu |
Target/Specificity | This mouse ERBB2 Antibody is generated from rabbits immunized with a KLH conjugated synthetic phosphopeptide corresponding to amino acid residues surrounding Y1223 of mouse ERBB2. |
Dilution | DB~~1:500 |
Format | Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification. |
Storage | Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
Precautions | Phospho-mouse ERBB2(Y1223) Antibody is for research use only and not for use in diagnostic or therapeutic procedures. |
Name | Erbb2 |
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Synonyms | Kiaa3023, Neu |
Function | Protein tyrosine kinase that is part of several cell surface receptor complexes, but that apparently needs a coreceptor for ligand binding. Essential component of a neuregulin-receptor complex, although neuregulins do not interact with it alone. GP30 is a potential ligand for this receptor. Regulates outgrowth and stabilization of peripheral microtubules (MTs). Upon ERBB2 activation, the MEMO1-RHOA-DIAPH1 signaling pathway elicits the phosphorylation and thus the inhibition of GSK3B at cell membrane. This prevents the phosphorylation of APC and CLASP2, allowing its association with the cell membrane. In turn, membrane-bound APC allows the localization of MACF1 to the cell membrane, which is required for microtubule capture and stabilization (By similarity). |
Cellular Location | Cell membrane {ECO:0000250|UniProtKB:P04626}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P04626} Cell projection, ruffle membrane {ECO:0000250|UniProtKB:P04626}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P04626} Early endosome {ECO:0000250|UniProtKB:P04626}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P04626}. Nucleus {ECO:0000250|UniProtKB:P04626}. Note=Translocation to the nucleus requires endocytosis, probably endosomal sorting and is mediated by importin beta-1/KPNB1. Also detected in endosome-to-TGN retrograde vesicles. Internalized from the cell membrane in response to EGF stimulation. {ECO:0000250|UniProtKB:P04626} |
Tissue Location | Expressed predominantly in uterine epithelial cells. In the muscle, expression localizes to the synaptic sites of muscle fibers |
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Background
This gene encodes a member of the epidermal growth factor (EGF) receptor family of receptor tyrosine kinases. This protein has no ligand binding domain of its own and therefore cannot bind growth factors. However, it does bind tightly to other ligand-bound EGF receptor family members to form a heterodimer, stabilizing ligand binding and enhancing kinase-mediated activation of downstream signalling pathways, such as those involving mitogen-activated protein kinase and phosphatidylinositol-3 kinase. Allelic variations at amino acid positions 654 and 655 of isoform a (positions 624 and 625 of isoform b) have been reported, with the most common allele, Ile654/Ile655, shown here. Amplification and/or overexpression of this gene has been reported in numerous cancers, including breast and ovarian tumors. Alternative splicing results in several additional transcript variants, some encoding different isoforms and others that have not been fully characterized.
References
Cabodi, S., et al. FASEB J. 24(10):3796-3808(2010)
Johnson, E., et al. J. Biol. Chem. 285(38):29491-29501(2010)
Huck, L., et al. Proc. Natl. Acad. Sci. U.S.A. 107(35):15559-15564(2010)
Chuang, T.D., et al. J. Biol. Chem. 285(31):23598-23606(2010)
Simeone, L., et al. J. Neurosci. 30(19):6620-6634(2010)
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