Overview

Description

  • NatureRecombinant
  • SourceInsect cells
  • Amino Acid Sequence
    • SpeciesHuman
    • Amino acids708 to 993

Specifications

Our Abpromise guarantee covers the use of ab61640 in the following tested applications.

The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.

  • Applications

    SDS-PAGE

    Functional Studies

  • Purity> 90 % by SDS-PAGE.

  • FormLiquid
  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

    Aliquot and store at -80°C. Avoid repeated freeze / thaw cycles.

    Preservative: None
    Constituents: 50% Glycerol, 0.05% Tween 20, 5mM Glutathione, 3mM DTT, 25mM Tris HCl, 100mM Sodium chloride, pH 8.0

General info

  • Alternative names
    • 4ICD
    • ALS19
    • Avian erythroblastic leukemia viral oncogene homolog 4
    • Avian erythroblastic leukemia viral v erb b2 oncogene homolog 4
    • E4ICD
    • EC 2.7.10.1
    • ErbB4
    • ERBB4 intracellular domain
    • ERBB4_HUMAN
    • HER 4
    • HER4
    • Mer4
    • MGC138404
    • Oncogene ERBB4
    • P180erbB4
    • Proto-oncogene-like protein c-ErbB-4
    • Receptor protein tyrosine kinase erbB 4 precursor
    • Receptor tyrosine protein kinase erbB 4
    • s80HER4
    • Tyrosine kinase type cell surface receptor HER4
    • Tyrosine kinase-type cell surface receptor HER4
    • v erb a avian erythroblastic leukemia viral oncogene homolog like 4
    • v erb a erythroblastic leukemia viral oncogene homolog 4
    • v-erb-a erythroblastic leukemia viral oncogene homolog 4 (avian)
    • V-ERB-B2 avian erythroblastic leukemia viral oncogene homolog 4
    • Verba avian erythroblastic leukemia viral oncogene homolog like 4
    • Verba erythroblastic leukemia viral oncogene homolog 4
    • VERBB2
    see all
  • 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.
  • Post-translational
    modifications
    Isoform 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.
  • Target information above from: UniProt accession Q15303 The UniProt Consortium
    The Universal Protein Resource (UniProt) in 2010
    Nucleic Acids Res. 38:D142-D148 (2010) .

    Information by UniProt

Human ErbB 4 protein fragment images

References for Human ErbB 4 protein fragment (ab61640)

ab61640 has not yet been referenced specifically in any publications.

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