|Application ||WB, IHC|
|Calculated MW||57260 Da|
|Other Names||Heat shock factor protein 1, HSF 1, Heat shock transcription factor 1, HSTF 1, HSF1, HSTF1|
|Target/Specificity||A synthetic peptide corresponding to residues near serine 303 and 307 of human HSF1 was used as an immunogen.|
|Format||50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||HSF1 Antibody Phospho (pS303/307) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||DNA-binding protein that specifically binds heat shock promoter elements (HSE) and activates transcription. In higher eukaryotes, HSF is unable to bind to the HSE unless the cells are heat shocked.|
|Cellular Location||Cytoplasm. Nucleus. Note=Cytoplasmic during normal growth. On activation, translocates to nuclear stress granules. Colocalizes with SUMO1 in nuclear stress granules|
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Provided below are standard protocols that you may find useful for product applications.
Human cells respond to heat stress by inducing the binding of a pre-existing transcriptional activator (heat shock factor, HSF) to DNA (1). Induction of heat shock protein (HSP) gene expression by stress is initiated by binding of HSF1 to HSP gene promoters to increase their transcription. The cytoprotective functions of these HSPs are essential for cell survival, and thus it is critical that inducible HSP gene expression be executed rapidly and efficiently. There is an interaction between heat shock factor 1 (HSF1) and symplekin, a protein known to form a complex with the polyadenylation factors CstF and CPSF. HSF1-symplekin complexes are detected only after stress treatment, and these two proteins co-localize in punctate nuclear structures in stressed cells (2). A chaperone/Hsp functioning as repressor of heat shock transcription factor (HSF) could make activation of hsp genes dependent on protein unfolding. It has been concluded that Hsp90, by itself and/or associated with multichaperone complexes, is a major repressor of HSF1 (3). HSF1 repression has been linked with phosphorylation on serine 303 and 307 by GSK3 and MAPK respectively (4).
1. Rabindran Sk, et al. Proc Natl Acad 88(16):6906-10, 1991
2. Xing H, et al. J Biol Chem 279(11):10551-5, 2004
3. Zou J, et al. Cell 94(4):471-80, 1998
4. Chu B, et al. JBC 273:18640-18646, 1998
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