Key features and details
- Rabbit polyclonal to ErbB4 / HER4 (phospho Y1284)
- Suitable for: ICC/IF
- Reacts with: Mouse, Rat, Human
- Isotype: IgG
Product nameAnti-ErbB4 / HER4 (phospho Y1284) antibody
See all ErbB4 / HER4 primary antibodies
DescriptionRabbit polyclonal to ErbB4 / HER4 (phospho Y1284)
Detects endogenous levels of ErbB4 / HER4 only when phosphorylated at tyrosine 1284.
Tested applicationsSuitable for: ICC/IFmore details
Species reactivityReacts with: Mouse, Rat, Human
Synthetic peptide corresponding to Human ErbB4/ HER4. Synthetic phosphopeptide derived from human ErbB4/ HER4 around the phosphorylation site of tyrosine 1284 (P-E-YP-L-S)
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We are also updating the applications & species that this product has been “predicted to work with,” however this information is not covered by our Abpromise guarantee.
Applications & species from publications and Abreviews that have not been tested in our own labs or in those of our suppliers are not covered by the Abpromise guarantee.
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Storage instructionsShipped at 4°C. Store at -20°C. Stable for 12 months at -20°C.
Storage bufferpH: 7.40
Preservative: 0.02% Sodium azide
Constituents: PBS, 50% Glycerol, 0.87% Sodium chloride
Without Mg2+ and Ca2+
Concentration information loading...
PurityImmunogen affinity purified
Purification notesThe antibody against non-phosphopeptide was removed by chromatography using non-phosphopeptide corresponding to the phosphorylation site.
Our Abpromise guarantee covers the use of ab61059 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
|ICC/IF||1/100 - 1/500.|
FunctionSpecifically binds and is activated by neuregulins, NRG-2, NRG-3, heparin-binding EGF-like growth factor, betacellulin and NTAK. Interaction with these factors induces cell differentiation. Not activated by EGF, TGF-A, and amphiregulin. The C-terminal fragment (CTF) of isoform JMA-A CYT-2 (containing E4ICD2) can stimulate transcription in the presence of YAP1. ERBB4 intracellular domain is involved in the regulation of cell growth. Conflicting reports are likely due at least in part to the opposing effects of the isoform-specific and nuclear-translocated ERBB4 intracellular domains (E4ICD1 and E4ICD2). Overexpression studies in epithelium show growth inhibition using E4ICD1 and increased proliferation using E4ICD2. E4ICD2 has greater in vitro kinase activity than E4ICD1. The kinase activity is required for the nuclear translocation of E4ICD2.
Tissue specificityExpressed at highest levels in brain, heart, kidney, in addition to skeletal muscle, parathyroid, cerebellum, pituitary, spleen, testis and breast. Lower levels in thymus, lung, salivary gland, and pancreas. Isoform JM-A CYT-1 and isoform JM-B CYT-1 are expressed in cerebellum, but only the isoform JM-B is expressed in the heart.
Sequence similaritiesBelongs to the protein kinase superfamily. Tyr protein kinase family. EGF receptor subfamily.
Contains 1 protein kinase domain.
modificationsIsoform JM-A CYT-1 and isoform JM-A CYT-2 but not isoform JM-B CYT-1 and isoform JM-B CYT-2 are processed by ADAM17. Proteolytic processing in response to ligand or 12-O-tetradecanoylphorbol-13-acetate stimulation results in the production of 120 kDa soluble receptor forms and intermediate membrane-anchored 80 kDa fragments (m80HER4), which are further processed by a presenilin-dependent gamma-secretase to release the respective cytoplasmic intracellular domain E4ICD (either E4ICD1/s80Cyt1 or E4ICD2/s80Cyt2). Membrane-anchored 80 kDa fragments of the processed isoform JM-A CYT-1 are more readily degraded by the proteasome than fragments of isoform JM-A CYT-2 suggesting a prevalence of E4ICD2 over E4ICD1.
Ligand-binding increases phosphorylation on tyrosine residues. Isoform JM-A CYT-2 is constitutively phosphorylated on tyrosine residues in a ligand-independent manner. E4ICD2 but not E4ICD1 is phosphorylated on tyrosine residues.
Ubiquitinated. The ERBB4 intracellular domain is ubiquitinated and targeted to proteosomal degradation during mitosis mediated by the APC/C complex. Isoform JM-A CYT-1 and isoform JM-B CYT-1 are ubiquitinated by WWP1. The ERBB4 intracellular domain (E4ICD1) is ubiquitinated, and this involves NEDD4.
Cellular localizationMembrane and Nucleus. Following proteolytical processing E4ICD (E4ICD1 or E4ICD2 generated from the respective isoforms) is translocated to the nucleus. Significantly more E4ICD2 than E4ICD1 is found in the nucleus. E4ICD2 colocalizes with YAP1 in the nucleus.
- Information by UniProt
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ab61059 staining ErbB4 / HER4 (phospho Y1284) in rat heart tissue sections by ICC/IF (Immunocytochemistry/immunofluorescence). Sections were fixed with paraformaldehyde, permeabilized with 0.05% Tween20 and blocked with 5% BSA + normal goat serum for 4 hours at 21°C. Samples were incubated with primary antibody (1/30 in 5% BSA + 0.05% Tween20 in TBS) for 12 hours at 4°C. ab150077, a goat anti-rabbit Alexa 488 (1/200) was used as the secondary antibody.
1/100-1/500 ab61059 staining phosphorilated ErbB4 / HER4 on HeLa cells treated with 200nM EGF for 5 minutes, in the absence (left) or presence (right) of the immunizing phosphopeptide.
ab61059 has been referenced in 4 publications.
- Yin Y et al. Tongxinluo Attenuates Myocardiac Fibrosis after Acute Myocardial Infarction in Rats via Inhibition of Endothelial-to-Mesenchymal Transition. Biomed Res Int 2019:6595437 (2019). PubMed: 31317035
- Wang J et al. Qiliqiangxin protects against anoxic injury in cardiac microvascular endothelial cells via NRG-1/ErbB-PI3K/Akt/mTOR pathway. J Cell Mol Med 21:1905-1914 (2017). PubMed: 28271613
- Depboylu C et al. Systemically administered neuregulin-1ß1 rescues nigral dopaminergic neurons via the ErbB4 receptor tyrosine kinase in MPTP mouse models of Parkinson's disease. J Neurochem 133:590-7 (2015). IHC-FoFr ; Mouse . PubMed: 25581060
- Rösler TW et al. Biodistribution and brain permeability of the extracellular domain of neuregulin-1-ß1. Neuropharmacology 61:1413-8 (2011). IHC-FoFr ; Mouse . PubMed: 21903113