- Tel: 858.663.9055
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Email: info@nsjbio.com
- Tel: 858.663.9055
- Email: info@nsjbio.com
Phospho-ErbB2 (pS1107) Antibody / Regulatory Site (F48687)
Email: info@nsjbio.com
| Catalog No | Formulation | Size | Price (USD) | ||
|---|---|---|---|---|---|
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F48687-0.4ML | In 1X PBS, pH 7.4, with 0.09% sodium azide | 0.4 ml | 439 | |
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F48687-0.08ML | In 1X PBS, pH 7.4, with 0.09% sodium azide | 0.08 ml | 205 |
| Availability | 1-3 business days |
| Species Reactivity | Human |
| Format | Antigen affinity purified |
| Host | Rabbit |
| Clonality | Polyclonal (rabbit origin) |
| Isotype | Rabbit Ig |
| Purity | Antigen affinity |
| UniProt | P04626 |
| Applications | Western Blot : 1:1000 Dot Blot : 1:500 |
| Limitations | This Phospho-ErbB2 (pS1107) Antibody / Regulatory Site is available for research use only. |
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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 (pS1107) antibody, also referred to as phospho-HER2 antibody and phospho-ERBB2 antibody in the literature, detects phosphorylation at serine 1107, a regulatory residue located within the intracellular domain of HER2.
Phosphorylation of HER2 occurs at multiple residues, including tyrosine and serine sites, which together coordinate receptor activation, signaling output, and regulatory control. While tyrosine phosphorylation is primarily associated with activation of downstream pathways such as PI3K/AKT and MAPK, serine phosphorylation contributes to modulation of receptor activity, influencing signaling dynamics and cellular responses.
Phosphorylation at S1107 reflects regulatory control within the HER2 signaling network, where multiple post-translational modifications work together to fine-tune receptor behavior. This may include modulation of receptor stability, interaction with regulatory proteins, or adjustment of signaling intensity under different cellular conditions.
HER2 signaling is a central driver of tumor biology, particularly in cancers characterized by ERBB2 amplification such as breast carcinoma. In these contexts, regulatory phosphorylation events contribute to how signaling pathways are controlled and sustained. Detection of phosphorylation at S1107 provides insight into these regulatory mechanisms beyond primary activation sites.
S1107 functions within a broader phosphorylation network that includes tyrosine residues such as Y1112, Y1139, Y1221, Y1222, and Y1248, which govern initiation, propagation, and activation of HER2 signaling. Analysis of serine phosphorylation complements detection of these sites and supports a more complete understanding of receptor signaling behavior.
Phospho-specific detection of ERBB2 at S1107 enables investigation of regulatory signaling mechanisms and modulation of receptor activity in both normal and disease contexts.
For detection of activated HER2 phosphorylation, see our HER2 phospho antibody (pY1248).
Titration of the Phospho-ErbB2 (pS1107) Antibody / Regulatory Site may be required due to differences in protocols and secondary/substrate sensitivity.
This Phospho-ErbB2 (pS1107) Antibody was produced from rabbits immunized with a KLH conjugated synthetic phospho-peptide corresponding to amino acid residues surrounding pS1107 of human HER2/ERBB2.
Aliquot the Phospho-ErbB2 (pS1107) Antibody and store frozen at -20oC or colder. Avoid repeated freeze-thaw cycles.
Phospho-ErbB2 (pS1107) antibody, phospho-HER2 Ser1107 antibody, ERBB2 pS1107 antibody, HER2 serine phosphorylation antibody
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