Render Target: STATIC
Render Timestamp:
6/8/2026, 5:50:58 AM EDT
6/8/2026, 9:50:58 AM UTC
Commit: 33ae406c5df2bbc7a7d3c17605228fbeff8ea416
XML generation date: 2026-06-05 17:18:47.462
Product last modified at: 2026-06-06T07:03:58.376Z
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PDP - Template Name: Blocking Peptide
PDP - Template ID: *******6db2f4c

EGF Receptor Blocking Peptide #1165

Inquiry Info. # 1165

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    Product Information

    Product Usage Information

    For Immunohistochemistry, add twice the volume of peptide as volume of antibody used in a 100 ul total volume. Incubate for a minimum of 30 minutes prior to adding the entire volume to the slide. Recommended antibody dilutions can be found on the EGF Receptor (15F8) Rabbit Monoclonal Antibody #4405 datasheet.

    Storage

    Supplied in 20 mM potassium phosphate (pH 7.0), 50 mM NaCl, 0.1 mM EDTA, 1 mg/ml BSA and 5% glycerol. Store at –20°C.

    Product Description

    This peptide can be used to block EGF Receptor (15F8) Rabbit mAb #4405.

    Quality Control

    The quality of the peptide was evaluated by reversed-phase HPLC and by mass spectrometry. The peptide blocks EGF Receptor (15F8) Rabbit mAb #4405 signal completely in immunohistochemistry.

    Background

    The epidermal growth factor (EGF) receptor is a transmembrane tyrosine kinase that belongs to the HER/ErbB protein family. Ligand binding results in receptor dimerization, autophosphorylation, activation of downstream signaling, internalization, and lysosomal degradation (1,2). Phosphorylation of EGF receptor (EGFR) at Tyr845 in the kinase domain is implicated in stabilizing the activation loop, maintaining the active state enzyme, and providing a binding surface for substrate proteins (3,4). c-Src is involved in phosphorylation of EGFR at Tyr845 (5). The SH2 domain of PLCγ binds at phospho-Tyr992, resulting in activation of PLCγ-mediated downstream signaling (6). Phosphorylation of EGFR at Tyr1045 creates a major docking site for the adaptor protein c-Cbl, leading to receptor ubiquitination and degradation following EGFR activation (7,8). The GRB2 adaptor protein binds activated EGFR at phospho-Tyr1068 (9). A pair of phosphorylated EGFR residues (Tyr1148 and Tyr1173) provide a docking site for the Shc scaffold protein, with both sites involved in MAP kinase signaling activation (2). Phosphorylation of EGFR at specific serine and threonine residues attenuates EGFR kinase activity. EGFR carboxy-terminal residues Ser1046 and Ser1047 are phosphorylated by CaM kinase II; mutation of either of these serines results in upregulated EGFR tyrosine autophosphorylation (10).

    Alternate Names

    EGF; epidermal growth factor receptor; Her1

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