Anti-HER2 / ErbB2 (pY1248)

In 1X PBS, pH 7.4, with 0.09% sodium azide. ErbB2 receptor tyrosine kinase 2 (ERBB2), also known as HER2, is a transmembrane receptor that plays a central role in regulating cell proliferation, survival, and differentiation through activation of intracellular signaling pathways. Phospho-ErbB2 (pY1248) antibody, also referred to as phospho-HER2 antibody and phospho-ERBB2 antibody in the literature, is designed to detect phosphorylation at tyrosine 1248, one of the most widely studied and functionally important sites associated with HER2 activation. Additional HER2 phosphorylation sites can be analyzed using phospho-specific antibodies targeting residues such as pY1221 (signaling docking), pY1222 (signal propagation), and pY1112 (adaptor recruitment).Phosphorylation at Y1248 occurs following receptor dimerization and activation of the intrinsic tyrosine kinase domain. This modification is closely associated with activation of downstream signaling pathways such as PI3K/AKT and MAPK, which regulate cell growth, survival, and metabolic adaptation. Because of this, phosphorylation at Y1248 is widely used as a direct indicator of active HER2 signaling. Detection of this site allows researchers to distinguish between inactive receptor pools and signaling-competent receptor populations, which is critical when studying pathway dynamics.HER2 signaling is particularly relevant in cancer biology, where ERBB2 amplification leads to elevated receptor expression and increased signaling output. In breast carcinoma and other HER2-positive tumors, phosphorylation at Y1248 correlates with enhanced pathway activation, increased proliferation, and aggressive tumor behavior. Monitoring this phosphorylation event provides insight into signaling status and therapeutic response, especially in experimental systems evaluating pathway inhibition.Structurally, Y1248 is located within the intracellular kinase domain of HER2 and functions as part of a coordinated phosphorylation network. Nearby residues such as Y1221 and Y1222 contribute to recruitment of adaptor proteins and early signaling events, while Y1248 reflects overall receptor activation status. This makes Y1248 one of the most reliable and widely used sites for assessing HER2 signaling activity.Phosphorylation of HER2 is not static and is regulated dynamically in response to cellular conditions, including growth factor availability, receptor dimerization, and cellular stress. Detection of phosphorylated ERBB2 at Y1248 therefore provides a snapshot of signaling activity at a given time, enabling researchers to study pathway activation in response to experimental manipulation or disease progression.Phospho-specific detection of ERBB2 at Y1248 enables precise analysis of signaling pathways in both normal and pathological contexts. This approach complements total HER2 detection and provides a more complete understanding of receptor function, activation status, and signaling output.For a full selection of HER2 antibodies for research applications, see our HER2 antibody page.