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Email: info@nsjbio.com
- Tel: 858.663.9055
- Email: info@nsjbio.com
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Phospho-Sirtuin 1 (pSer47) antibody targets the phosphorylated form of Sirtuin 1 (SIRT1) at serine 47, a regulatory post-translational modification that influences SIRT1 activity, localization, and protein interactions. SIRT1 is a NAD-dependent protein deacetylase that localizes primarily to the nucleus, with context-dependent shuttling to the cytoplasm, where it regulates transcriptional programs involved in metabolism, stress adaptation, DNA damage responses, and cell survival. Phosphorylation provides an additional layer of control over SIRT1 function, enabling rapid modulation of activity in response to cellular signaling events. Clone FDA-19 recognizes SIRT1 phosphorylated at Ser47 and is designed to support research studies examining signaling-dependent regulation of this key deacetylase.
Functionally, SIRT1 deacetylates histones and a wide range of non-histone substrates, including transcription factors and co-regulators that govern metabolic homeostasis, inflammatory signaling, and cell cycle progression. Phosphorylation at Ser47 has been reported to influence SIRT1 stability and regulatory interactions, linking upstream kinase signaling to downstream epigenetic and transcriptional outcomes. Monitoring phosphorylation at this site provides insight into how signaling pathways modulate SIRT1 beyond changes in expression level alone. A Phospho-SIRT1 antibody therefore enables assessment of pathway engagement that impacts SIRT1-dependent transcriptional control.
Phosphorylated SIRT1 is relevant across multiple biological contexts, including metabolically active tissues, proliferating cells, and cells responding to oxidative or genotoxic stress. Changes in SIRT1 phosphorylation status can alter its ability to coordinate gene expression programs involved in mitochondrial function, stress resistance, and cellular adaptation. Because phosphorylation events are often transient and tightly regulated, detection of phospho-SIRT1 provides a dynamic readout of signaling activity that may not be captured by analysis of total SIRT1 protein alone.
From a biological and disease-relevance perspective, SIRT1 has been extensively studied in aging, metabolic regulation, neurobiology, and cancer-associated signaling pathways. Dysregulation of SIRT1 activity or its post-translational modification profile can influence disease-associated phenotypes, including altered stress responses and metabolic imbalance. Phosphorylation-specific analysis of SIRT1 contributes to understanding how upstream signaling pathways intersect with epigenetic regulation and transcriptional control in both physiological and pathological settings.
At the molecular level, SIRT1 is encoded by the SIRT1 gene and produces a protein that migrates at approximately 110-120 kDa on SDS-PAGE, depending on post-translational modification status. Serine 47 lies within an N-terminal regulatory region that integrates signaling inputs with SIRT1 function. A Phospho-Sirtuin 1 (pSer47) antibody supports research applications focused on signal transduction, post-translational regulation, and functional studies of SIRT1 activity, with NSJ Bioreagents providing reagents intended for research use.
Optimal dilution of the Phospho-Sirtuin 1 (pSer47) antibody should be determined by the researcher.
A synthesized peptide derived from human Sirtuin 1 (pSer47) was used as the immunogen for the Phospho-Sirtuin 1 (pSer47) antibody.
Store the Phospho-Sirtuin 1 (pSer47) antibody at -20oC.
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