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Email: info@nsjbio.com
- Tel: 858.663.9055
- Email: info@nsjbio.com
Phospho-Tau Antibody (pS396) [clone FCO-13] (RQ5330)
Email: info@nsjbio.com
| Catalog No | Formulation | Size | Price (USD) | ||
|---|---|---|---|---|---|
|
RQ5330 | Antibody in PBS with 0.02% sodium azide, 50% glycerol and 0.4-0.5mg/ml BSA | 100 ul | 439 |
| Availability | 1-2 weeks |
| Species Reactivity | Human |
| Format | Purified |
| Clonality | Rabbit Monoclonal |
| Isotype | Rabbit IgG |
| Clone Name | FCO-13 |
| Purity | Affinity purified |
| UniProt | P10636 |
| Applications | Western Blot : 1:1000 Immunohistochemistry (FFPE) : 1:50 |
| Limitations | This phospho-Tau antibody (pS396) is available for research use only. |
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Phospho Tau antibody pS396 is a highly specific research reagent for studying tau phosphorylation and neurodegenerative disease. The encoded protein, tau, is a microtubule associated protein that stabilizes microtubules and supports axonal transport in neurons. Aberrant phosphorylation of tau at multiple serine and threonine residues is a defining feature of tauopathies, including Alzheimer disease and frontotemporal dementia. This antibody recognizes tau only when serine at amino acid 396 is phosphorylated, enabling precise detection of a modification closely associated with pathological tau aggregation.
Phosphorylation at serine 396 occurs within the C terminal region of tau, a domain that influences microtubule binding and tau filament assembly. Modification at this site reduces tau's affinity for microtubules and promotes abnormal conformations that lead to oligomerization and neurofibrillary tangle formation. Phospho specific antibodies targeting S396 are widely used as biomarkers of disease progression and as tools to track pathological changes in experimental models of dementia.
In Alzheimer disease brains, tau phosphorylated at S396 is a prominent component of paired helical filaments and tangles. Accumulation of phosphorylated tau disrupts axonal transport, destabilizes the cytoskeleton, and triggers synaptic dysfunction. These events contribute directly to neuronal loss and cognitive decline. Monitoring phosphorylation at this residue provides insights into the molecular cascade that drives tau pathology and helps evaluate therapeutic strategies aimed at reducing tau hyperphosphorylation.
Regulation of phosphorylation at serine 396 involves kinases such as glycogen synthase kinase 3 beta, cyclin dependent kinase 5, and MAP kinases. Phosphatases, particularly PP2A, counteract these modifications. The dynamic interplay of these enzymes determines the balance between physiological and pathological tau states. Phospho Tau antibody pS396 allows researchers to measure these changes with high sensitivity, providing a window into kinase and phosphatase activity in neuronal systems.
The Phospho Tau antibody pS396 is commonly applied in western blotting, immunohistochemistry, immunofluorescence, and ELISA to identify site specific phosphorylation patterns. These applications are essential for research into tau driven neurodegeneration, biomarker development, and therapeutic testing. For investigators studying tauopathies, cytoskeletal biology, or kinase signaling, this antibody provides a dependable and specific detection tool. NSJ Bioreagents supplies validated antibodies designed to deliver accuracy and reproducibility in advanced molecular research.
Optimal dilution of the phospho-Tau antibody (pS396) should be determined by the researcher.
A synthetic peptide specific to human Tau / MAPT (surrounding pS396) was used as the immunogen for the phospho-Tau antibody.
Store the phospho-Tau antibody (pS396) at -20oC.
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