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Mouse Anti-ERBB4 (AA 1250-1264) Recombinant Antibody (HFR1) (CBMAB-H1057-FY)

This product is mouse antibody that recognizes ERBB4. The antibody HFR1 can be used for immunoassay techniques such as: FC, IF, IHC, IHC-P, IP, WB.
See all ERBB4 antibodies
Published Data

Summary

Host Animal
Mouse
Specificity
Human, Mouse
Clone
HFR1
Antibody Isotype
IgG2b
Application
FC, IF, IHC, IHC-P, IP, WB

Basic Information

Immunogen
Synthetic Peptide: C R S T L Q H P D Y L Q E Y S T
Specificity
Human, Mouse
Antibody Isotype
IgG2b
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Buffer
PBS
Concentration
1 mg/mL
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.
Epitope
AA 1250-1264

Target

Full Name
Erb-B2 Receptor Tyrosine Kinase 4
Introduction
This gene is a member of the Tyr protein kinase family and the epidermal growth factor receptor subfamily. It encodes a single-pass type I membrane protein with multiple cysteine rich domains, a transmembrane domain, a tyrosine kinase domain, a phosphotidylinositol-3 kinase binding site and a PDZ domain binding motif. The protein binds to and is activated by neuregulins and other factors and induces a variety of cellular responses including mitogenesis and differentiation. Multiple proteolytic events allow for the release of a cytoplasmic fragment and an extracellular fragment. Mutations in this gene have been associated with cancer. Alternatively spliced variants which encode different protein isoforms have been described; however, not all variants have been fully characterized.
Entrez Gene ID
Human2066
Mouse13869
UniProt ID
HumanQ15303
MouseQ61527
Alternative Names
Erb-B2 Receptor Tyrosine Kinase 4; V-Erb-B2 Avian Erythroblastic Leukemia Viral Oncogene Homolog 4; Tyrosine Kinase-Type Cell Surface Receptor HER4; Human Epidermal Growth Factor Receptor 4; Proto-Oncogene-Like Protein C-ErbB-4; EC 2.7.10.1; P180erbB4; HER4; V-Erb-A Avian Erythroblastic Leukemia Viral Oncogene Homolog-Like 4
Research Area
Tyrosine-protein kinase that plays an essential role as cell surface receptor for neuregulins and EGF family members and regulates development of the heart, the central nervous system and the mammary gland, gene transcription, cell proliferation, differentiation, migration and apoptosis. Required for normal cardiac muscle differentiation during embryonic development, and for postnatal cardiomyocyte proliferation. Required for normal development of the embryonic central nervous system, especially for normal neural crest cell migration and normal axon guidance. Required for mammary gland differentiation, induction of milk proteins and lactation. Acts as cell-surface receptor for the neuregulins NRG1, NRG2, NRG3 and NRG4 and the EGF family members BTC, EREG and HBEGF. Ligand binding triggers receptor dimerization and autophosphorylation at specific tyrosine residues that then serve as binding sites for scaffold proteins and effectors. Ligand specificity and signaling is modulated by alternative splicing, proteolytic processing, and by the formation of heterodimers with other ERBB family members, thereby creating multiple combinations of intracellular phosphotyrosines that trigger ligand- and context-specific cellular responses. Mediates phosphorylation of SHC1 and activation of the MAP kinases MAPK1/ERK2 and MAPK3/ERK1. Isoform JM-A CYT-1 and isoform JM-B CYT-1 phosphorylate PIK3R1, leading to the activation of phosphatidylinositol 3-kinase and AKT1 and protect cells against apoptosis. Isoform JM-A CYT-1 and isoform JM-B CYT-1 mediate reorganization of the actin cytoskeleton and promote cell migration in response to NRG1. Isoform JM-A CYT-2 and isoform JM-B CYT-2 lack the phosphotyrosine that mediates interaction with PIK3R1, and hence do not phosphorylate PIK3R1, do not protect cells against apoptosis, and do not promote reorganization of the actin cytoskeleton and cell migration. Proteolytic processing of isoform JM-A CYT-1 and isoform JM-A CYT-2 gives rise to the corresponding soluble intracellular domains (4ICD) that translocate to the nucleus, promote nuclear import of STAT5A, activation of STAT5A, mammary epithelium differentiation, cell proliferation and activation of gene expression. The ERBB4 soluble intracellular domains (4ICD) colocalize with STAT5A at the CSN2 promoter to regulate transcription of milk proteins during lactation. The ERBB4 soluble intracellular domains can also translocate to mitochondria and promote apoptosis.
Biological Process
Cardiac muscle tissue regeneration Source: UniProtKB
Cell fate commitment Source: Ensembl
Cell migration Source: UniProtKB
Cellular response to epidermal growth factor stimulus Source: Ensembl
Central nervous system morphogenesis Source: UniProtKB
Embryonic pattern specification Source: UniProtKB
Establishment of planar polarity involved in nephron morphogenesis Source: Ensembl
Heart development Source: UniProtKB
Lactation Source: UniProtKB
Mammary gland alveolus development Source: UniProtKB
Mammary gland epithelial cell differentiation Source: UniProtKB
Mitochondrial fragmentation involved in apoptotic process Source: UniProtKB
Negative regulation of apoptotic process Source: UniProtKB
Negative regulation of cell population proliferation Source: UniProtKB
Nervous system development Source: UniProtKB
Neural crest cell migration Source: UniProtKB
Olfactory bulb interneuron differentiation Source: UniProtKB
Peptidyl-tyrosine phosphorylation Source: UniProtKB
Positive regulation of cardiac muscle cell proliferation Source: UniProtKB
Positive regulation of cell population proliferation Source: UniProtKB
Positive regulation of ERK1 and ERK2 cascade Source: UniProtKB
Positive regulation of kinase activity Source: GO_Central
Positive regulation of phosphatidylinositol 3-kinase activity Source: UniProtKB
Positive regulation of phosphatidylinositol 3-kinase signaling Source: Ensembl
Positive regulation of protein localization to cell surface Source: Ensembl
Positive regulation of protein phosphorylation Source: UniProtKB
Positive regulation of receptor signaling pathway via JAK-STAT Source: UniProtKB
Positive regulation of transcription, DNA-templated Source: UniProtKB
Positive regulation of tyrosine phosphorylation of STAT protein Source: UniProtKB
Protein autophosphorylation Source: UniProtKB
Regulation of cell migration Source: UniProtKB
Signal transduction Source: UniProtKB
Synapse assembly Source: Ensembl
Transmembrane receptor protein tyrosine kinase signaling pathway Source: UniProtKB
Cellular Location
Cell membrane. In response to NRG1 treatment, the activated receptor is internalized.
ERBB4 intracellular domain: Nucleus; Mitochondrion. 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.
Involvement in disease
Amyotrophic lateral sclerosis 19 (ALS19):
A neurodegenerative disorder affecting upper motor neurons in the brain and lower motor neurons in the brain stem and spinal cord, resulting in fatal paralysis. Sensory abnormalities are absent. The pathologic hallmarks of the disease include pallor of the corticospinal tract due to loss of motor neurons, presence of ubiquitin-positive inclusions within surviving motor neurons, and deposition of pathologic aggregates. The etiology of amyotrophic lateral sclerosis is likely to be multifactorial, involving both genetic and environmental factors. The disease is inherited in 5-10% of the cases.
Topology
Extracellular: 26-651
Helical: 652-675
Cytoplasmic: 676-1308
PTM
Isoform JM-A CYT-1 and isoform JM-A 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 a cytoplasmic intracellular domain (E4ICD; E4ICD1/s80Cyt1 or E4ICD2/s80Cyt2, depending on the isoform). 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. Isoform JM-B CYT-1 and isoform JM-B CYT-2 lack the ADAM17 cleavage site and are not processed by ADAM17, precluding further processing by gamma-secretase.
Autophosphorylated on tyrosine residues in response to ligand binding. Autophosphorylation occurs in trans, i.e. one subunit of the dimeric receptor phosphorylates tyrosine residues on the other subunit. Ligands trigger phosphorylation at specific tyrosine residues, thereby creating binding sites for scaffold proteins and effectors. Constitutively phosphorylated at a basal level when overexpressed in heterologous systems; ligand binding leads to increased phosphorylation. Phosphorylation at Tyr-1035 is important for interaction with STAT1. Phosphorylation at Tyr-1056 is important for interaction with PIK3R1. Phosphorylation at Tyr-1242 is important for interaction with SHC1. Phosphorylation at Tyr-1188 may also contribute to the interaction with SHC1. 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. During mitosis, the ERBB4 intracellular domain is ubiquitinated by the APC/C complex and targeted to proteasomal degradation. 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.

Lucas, L. M., Dwivedi, V., Senfeld, J. I., Cullum, R. L., Mill, C. P., Piazza, J. T., ... & Riese, D. J. (2022). The Yin and Yang of ERBB4: Tumor Suppressor and Oncoprotein. Pharmacological Reviews, 74(1), 18-47.

Zaraei, S. O., Sbenati, R. M., Alach, N. N., Anbar, H. S., El-Gamal, R., Tarazi, H., ... & El-Gamal, M. I. (2021). Discovery of first-in-class imidazothiazole-based potent and selective ErbB4 (HER4) kinase inhibitors. European Journal of Medicinal Chemistry, 224, 113674.

El-Gamal, M. I., Mewafi, N. H., Abdelmotteleb, N. E., Emara, M. A., Tarazi, H., Sbenati, R. M., ... & Anbar, H. S. (2021). A review of HER4 (ErbB4) kinase, its impact on cancer, and its inhibitors. Molecules, 26(23), 7376.

Fiori, L. M., Kos, A., Lin, R., Théroux, J. F., Lopez, J. P., Kühne, C., ... & Turecki, G. (2021). miR-323a regulates ERBB4 and is involved in depression. Molecular psychiatry, 26(8), 4191-4204.

Feyen, E., Ricke-Hoch, M., Van Fraeyenhove, J., Vermeulen, Z., Scherr, M., Dugaucquier, L., ... & De Keulenaer, G. W. (2021). ERBB4 and multiple microRNAs that target ERBB4 participate in pregnancy-related cardiomyopathy. Circulation: Heart Failure, 14(7), e006898.

Segers, V. F., Dugaucquier, L., Feyen, E., Shakeri, H., & De Keulenaer, G. W. (2020). The role of ErbB4 in cancer. Cellular oncology, 43(3), 335-352.

Liang, X., Ding, Y., Lin, F., Zhang, Y., Zhou, X., Meng, Q., ... & Liu, Z. (2019). Overexpression of ERBB4 rejuvenates aged mesenchymal stem cells and enhances angiogenesis via PI3K/AKT and MAPK/ERK pathways. The FASEB Journal, 33(3), 4559-4570.

Wang, H., Liu, F., Chen, W., Sun, X., Cui, W., Dong, Z., ... & Mei, L. (2018). Genetic recovery of ErbB4 in adulthood partially restores brain functions in null mice. Proceedings of the National Academy of Sciences, 115(51), 13105-13110.

Forget, A., Martignetti, L., Puget, S., Calzone, L., Brabetz, S., Picard, D., ... & Ayrault, O. (2018). Aberrant ERBB4-SRC signaling as a hallmark of group 4 medulloblastoma revealed by integrative phosphoproteomic profiling. Cancer cell, 34(3), 379-395.

Zeng, F., Wang, Y., Kloepfer, L. A., Wang, S., & Harris, R. C. (2018). ErbB4 deletion predisposes to development of metabolic syndrome in mice. American Journal of Physiology-Endocrinology and Metabolism, 315(4), E583-E593.

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For research use only. Not intended for any clinical use.

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