Target: HSF1
Conjugate: RPE
Product Type: Monoclonal
Clone Number: 4B4
Immunogen: Purified recombinant mouse HSF1 protein, epitope mapping to amino acids 425-439
Swiss-Prot: P38532
Purification: Protein G Purified
Storage Buffer: PBS pH 7.4, 50% glycerol, 0.1% sodium azide *Storage buffer may change when conjugated
Concentration: 1 mg/ml
Specificity: Detects ~85kDa (unstressed cell lysates) and ~95kDa (heat shocked cell lysates).
Cellular Localization: Cytoplasm,Nucleus
Scientific Background: HSF1, or heat shock factor 1, belongs to a family of Heat Shock transcription factors that activate the transcription of genes encoding products required for protein folding, processing, targeting, degradation, and function (2). The up-regulation of HSP (heat shock proteins) expression by stressors is achieved at the level of transcription through a heat shock element (HSE) and a transcription factor (HSF) (3, 4, 5). Most HSFs have highly conserved amino acid sequences. On all HSFs there is a DNA binding domain at the N-terminus. Hydrophobic repeats located adjacent to this binding domain are essential for the formation of active trimers. Towards the C-terminal region another short hydrophobic repeat exists, and is thought to be necessary for suppression of trimerization (6). There are two main heat shock factors, 1 and 2. Mouse HSF1 exists as two isoforms, however in higher eukaryotes HSF1 is found in a diffuse cytoplasmic and nuclear distribution in un-stressed cells. Once exposed to a multitude of stressors, it localizes to discrete nuclear granules within seconds. As it recovers from stress, HSF1 dissipates from these granules to a diffuse nuceloplasmic distribution. HSF2 on the other hand is similar to mouse HSF1, as it exists as two isoforms, the alpha form being more transcriptionally active than the smaller beta form (7, 8). Various experiments have suggested that HFS2 may have roles in differentiation and development (9, 10, 11).
References: 1. Cotto J.J., Fox S.G. and Morimoto R.I. (1997) J. Cell Science 110: 2925-2934.2. Morano K.A. and Thiele D.J. (1999). Gene Expression 7 (6): 271-82. 3. Tanaka K.I., et al. (2007). JBC Papers Online Manuscript M704081200.4. Morimoto R. I. (1998) Genes Dev 12: 3788-3796.5. McMillan D. R., et al. (1998) J Bio Chem 273: 7523-7528.6. Jolly C., Usson Y. and Morimoto R.I. (1999) Proc. Natl. Acad. Sci. USA 96 (12): 6769- 6774.7. Fiorenza M.T., et al. (1995) Nucleic Acids Res. 23 (3):467-474.8. Goodson M.L., Park-Sarge O.K. and Sarge K.D. (1995) Mol. Cell. Biol. 15(10): 5288-5293.9. Rallu M., et al. (1997) Proc. Natl. Acad. Sci. USA 94(6): 2392-2397.10. Sarge K.D., et al. (1994) Biol. Reprod. 50(6): 1334-1343.11. Murphy S.P., Gorzowski J.J., Sarge K.D. and Phillips B. (1994) Mol. Cell. Biol. 14(8):5309-5317.
Field of Use: Not for use in humans. Not for use in diagnostics or therapeutics. For in vitro research use only.
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