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- Tel: 858.663.9055
- Email: info@nsjbio.com
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ErbB2 receptor tyrosine kinase 2 (ERBB2), also known as HER2, is a transmembrane receptor that regulates cell proliferation, survival, and differentiation through activation of intracellular signaling pathways. Phospho-ErbB2 (pY1005) antibody, also referred to as phospho-HER2 antibody and phospho-ERBB2 antibody in the literature, detects phosphorylation at tyrosine 1005, a residue located within the intracellular domain of HER2 that contributes to early signaling events following receptor activation.
Phosphorylation of HER2 occurs at multiple tyrosine residues that collectively coordinate receptor-mediated signaling. Y1005 is positioned within the proximal intracellular region of HER2 and participates in the early stages of signal transduction, prior to full pathway amplification. This makes it useful for monitoring initial receptor engagement and the onset of intracellular signaling cascades.
Upon receptor activation, HER2 undergoes conformational changes and autophosphorylation at multiple sites, creating docking points for downstream signaling components. While major residues such as Y1221, Y1222, and Y1248 are strongly associated with signal propagation and activation, phosphorylation at Y1005 reflects an earlier stage in this process, where signaling pathways begin to be engaged but are not yet fully amplified.
HER2 signaling plays a central role in cancer biology, particularly in tumors characterized by ERBB2 amplification such as breast carcinoma. In these contexts, phosphorylation at residues including Y1005 is associated with activation of receptor-driven signaling that supports tumor cell proliferation and survival. Detection of phosphorylation at this site provides insight into early signaling dynamics and receptor activation status.
Y1005 functions within a broader phosphorylation network that includes residues such as Y1112, Y1139, Y1221, Y1222, and Y1248. Together, these sites regulate the progression of HER2 signaling from initiation through propagation to sustained activation. Analysis of Y1005 phosphorylation complements detection of these other sites and contributes to a more complete understanding of HER2 signaling behavior.
Phospho-specific detection of ERBB2 at Y1005 enables investigation of early receptor activation and signaling initiation. This supports studies focused on receptor engagement, pathway onset, and early cellular responses in both normal and disease contexts.
For detection of activated HER2 phosphorylation, see our HER2 phospho antibody (pY1248).
Titration of the Phospho-ErbB2 (pY1005) Antibody / Early Signaling Site may be required due to differences in protocols and secondary/substrate sensitivity.
This Phospho-ErbB2 (pY1005) Antibody was produced from rabbits immunized with a KLH conjugated synthetic phospho-peptide corresponding to amino acid residues surrounding pY1005 of human ERBB2.
Aliquot the Phospho-ErbB2 (pY1005) Antibody and store frozen at -20oC or colder. Avoid repeated freeze-thaw cycles.
Phospho-ErbB2 (pY1005) antibody, phospho-HER2 Tyr1005 antibody, ERBB2 pY1005 antibody, HER2 early signaling antibody
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