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Email: info@nsjbio.com
- Tel: 858.663.9055
- Email: info@nsjbio.com
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Phosphorylation of Heat shock factor protein 1 can either activate or inhibit its activity, depending on the specific sites that are modified. This intricate regulatory mechanism allows cells to fine-tune their response to stress and optimize their survival. Studies have shown that phosphorylation of HSF1 at certain sites can enhance its ability to bind to DNA and activate the expression of heat shock proteins. On the other hand, phosphorylation at other sites can inhibit HSF1 activity and promote its degradation. This delicate balance between activation and inhibition is critical for maintaining cellular homeostasis under stress conditions.
Optimal dilution of the Phospho-HSF1 antibody (pS326) should be determined by the researcher.
A synthetic peptide specific to the region of human HSF1 protein surrounding phosphorylated serine 326 protein was used as the immunogen for the Phospho-HSF1 antibody (pS326).
Store the Phospho-HSF1 antibody at -20oC.
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