| Code | CSB-RA019025A542phHU |
| Size | US$210 |
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| Application | Recommended Dilution |
|---|---|
| WB | 1:500-1:5000 |
| IP | 1:200-1:1000 |
PTPN11, commonly known as SHP-2, serves as a critical regulator of cellular signaling pathways that control proliferation, differentiation, and survival. This tyrosine phosphatase plays essential roles in growth factor and cytokine receptor signaling, with phosphorylation at tyrosine 542 representing a key activation event that enhances its catalytic activity. Dysregulation of PTPN11 signaling has been implicated in developmental disorders and various malignancies, making precise detection of its phosphorylation state valuable for researchers investigating signal transduction mechanisms.
This recombinant monoclonal antibody, generated against a synthetic phosphopeptide corresponding to human Phospho-PTPN11 at Y542, offers the consistency and reproducibility that phospho-specific detection demands. As a sequence-defined recombinant clone, it eliminates the lot-to-lot variability that can compromise longitudinal studies of dynamic phosphorylation events. The rabbit IgG format provides strong signal amplification while maintaining specificity for the phosphorylated epitope.
Validation studies demonstrate reliable performance across multiple experimental platforms. In western blotting applications, the antibody detects a band at the expected 68 kDa molecular weight in HeLa, 293, and A549 cell lysates, with enhanced signal observed following pervanadate treatment to preserve phosphorylation states. Recommended working dilutions range from 1:500 to 1:5000 for western blotting. The antibody also performs effectively in immunoprecipitation assays, successfully enriching phosphorylated PTPN11 from pervanadate-treated HeLa lysates at dilutions between 1:200 and 1:1000.
For researchers studying receptor tyrosine kinase signaling, RAS-MAPK pathway regulation, or phosphatase biology, this antibody provides a dependable tool for monitoring PTPN11 activation dynamics in human cell models.
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