Anti-Phospho-ErbB2/ErbB4 (Y1248/1284) Rabbit Antibody [K1P9]

Catalog No.: F3624

    Application: Reactivity:

    Usage Information

    Dilution
    1:1000-1:5000
    1:30
    1:100
    1:50
    Application
    WB, IP, IF, FCM
    Reactivity
    Human
    Source
    Rabbit
    Storage Buffer
    PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3
    Storage (from the date of receipt)
    -20°C (avoid freeze-thaw cycles), 2 years
    Predicted MW Observed MW
    138 kDa, 147 kDa 180 kDa
    *Why do the predicted and actual molecular weights differ?
    The following reasons may explain differences between the predicted and actual protein molecular weight.
    Positive Control HeLa (starved 4 hours, EGF, 200 ng/ml, 15 minutes at 20 µg); A431 (starved 4 hours, EGF, 200 ng/ml, 15 minutes at 20 µg); SK-BR-3 (starved 4 hours, EGF, 200 ng/ml, 15 minutes at 20 µg)
    Negative Control HeLa; A431

    Datasheet & SDS

    Biological Description

    Specificity
    Phospho-ErbB2/HER2 (Tyr1248) + Phospho-ErbB4/HER4 (Tyr1284) Rabbit mAb detects endogenous levels of total ErbB2/HER2 and ErbB4/HER4 protein only when phosphorylated at Tyr1248 and Tyr1284 respectively.
    Clone
    K1P9
    Synonym(s)
    CD340, HER2, MLN19, NEU, NGL, ERBB2, Receptor tyrosine-protein kinase erbB-2, Metastatic lymph node gene 19 protein, Proto-oncogene Neu, Proto-oncogene c-ErbB-2, Tyrosine kinase-type cell surface receptor HER2, p185erbB2, MLN 19
    Background
    Phospho-ErbB2/HER2 (Tyr1248) and Phospho-ErbB4/HER4 (Tyr1284) are activated forms of two members of the ErbB receptor tyrosine kinase (RTK) family, which also includes EGFR/HER1 and ErbB3/HER3. These single-pass transmembrane glycoproteins have an extracellular ligand-binding domain, a single membrane-spanning region, and an intracellular tyrosine kinase domain. HER2 lacks a direct ligand and functions primarily as a preferred heterodimerization partner, whereas HER4 binds ligands such as neuregulins. Tyr1248 in HER2 and Tyr1284 in HER4 are key autophosphorylation sites within their C-terminal cytoplasmic tails; their phosphorylation creates high-affinity docking sites for SH2- or PTB-domain-containing signaling proteins, initiating downstream pathways including RAS/MAPK and PI3K/AKT. These phosphorylation events are critical for regulating cell proliferation, differentiation, survival, and, in the context of infection, bacterial uptake—such as during Neisseria meningitidis invasion of host cells via HB-EGF–mediated transactivation. Clinically, persistent phosphorylation at Tyr1248 or Tyr1284 is associated with oncogenic signaling in cancers (e.g., HER2-positive breast cancer) and represents an important biomarker and therapeutic target in both oncology and pathogen–host interaction research.
    References
    • https://pubmed.ncbi.nlm.nih.gov/33037285/
    • https://pubmed.ncbi.nlm.nih.gov/24379285/

    Tech Support

    Answers to questions you may have can be found in the inhibitor handling instructions. Topics include how to prepare stock solutions, how to store inhibitors, and issues that need special attention for cell-based assays and animal experiments.

    Handling Instructions

    Tel: +1-832-582-8158 Ext:3
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