| Code | CSB-RA618017A255phHU |
| Size | US$210 |
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| Application | Recommended Dilution |
|---|---|
| IF | 1:20-1:200 |
SMAD2 serves as a critical intracellular mediator of TGF-β signaling, translating extracellular cues into transcriptional responses that govern cell proliferation, differentiation, and epithelial-mesenchymal transition. Phosphorylation at Serine 255 represents a key regulatory modification within the linker region, distinct from the canonical C-terminal phosphorylation sites, and is associated with growth factor-mediated signaling crosstalk. Detecting this specific phosphorylation event enables researchers to dissect the complex regulatory networks that fine-tune SMAD2 activity in both normal physiology and disease states.
This recombinant monoclonal antibody, clone 2A12, offers the consistency and reproducibility that phospho-specific detection demands. Generated against a synthetic phosphopeptide corresponding to human Phospho-SMAD2 at Serine 255, the antibody benefits from sequence-defined specificity inherent to recombinant production. This means researchers can expect reliable performance across experiments and over time, eliminating the lot-to-lot variability that can complicate longitudinal studies or multi-site collaborations.
Validation in immunofluorescence demonstrates clear subcellular localization in A549 human lung carcinoma cells, with recommended working dilutions ranging from 1:20 to 1:200 providing flexibility for optimization across different experimental conditions. The antibody has also been validated for ELISA applications, supporting quantitative detection workflows. Supplied in a glycerol-containing buffer with BSA stabilization, the formulation supports long-term storage stability at -20°C or -80°C.
For researchers investigating TGF-β pathway dynamics, growth factor signaling integration, or the mechanistic basis of SMAD2 regulation in cancer biology and fibrosis, this phospho-specific antibody provides a reliable tool for interrogating a functionally significant post-translational modification.
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