| Code | CSB-RA026244A127phHU |
| Size | US$210 |
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| Application | Recommended Dilution |
|---|---|
| WB | 1:500-1:5000 |
| IHC | 1:50-1:200 |
YAP1 serves as a critical transcriptional coactivator in the Hippo signaling pathway, where its activity is tightly regulated through phosphorylation. Phosphorylation at serine 127 represents a key regulatory event that promotes cytoplasmic retention of YAP1 through 14-3-3 protein binding, effectively suppressing its transcriptional activity. This phosphorylation site has become essential for researchers investigating Hippo pathway dynamics, organ size control, and the dysregulation of YAP1 signaling frequently observed in cancer progression.
This recombinant monoclonal antibody, generated against a synthetic phosphopeptide corresponding to human Phospho-YAP1 at S127, offers the consistency and reproducibility that phospho-specific detection demands. Because recombinant antibodies are produced from a defined sequence, researchers can expect reliable lot-to-lot performance, which is particularly valuable when tracking subtle changes in phosphorylation status across experimental conditions. The rabbit IgG format and affinity-chromatography purification ensure high specificity for this critical phospho-epitope.
Validation studies demonstrate robust performance across multiple applications. Western blot analysis in HepG2 whole cell lysates, with and without Calyculin A treatment, confirms detection of the expected 65 kDa band, providing researchers with a reliable system for monitoring phosphatase-dependent regulation of YAP1. Immunohistochemistry validation in paraffin-embedded human endometrial cancer tissue further extends the antibody's utility for studying YAP1 phosphorylation in clinical specimens and tissue-based research contexts.
For investigators exploring signal transduction mechanisms, particularly those examining how upstream kinases and phosphatases modulate YAP1 localization and activity, this antibody provides a dependable tool for dissecting Hippo pathway regulation in human samples.
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