|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 phospho specific peptide corresponding to residues surrounding serine 320 of human HSF1 was used as an immunogen. This antibody detects HSF1 phosphorlyated on serine 320.|
|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 (pS320) 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. (2). Activation is accompanied by hyperphosphorylation of HSF1. The regulatory importance of this phosphorylation has remained incompletely understood. Phosphorylation of Serine 326 but none of the other Serine residues was found to contribute significantly to activation of the factor by heat stress (3).
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. Guettouche T et al. BMC Biochem 11(6):4, 2005
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