HSF1 Antibody: RPE

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).

1 µg/ml of SMC-118 was sufficient for detection of HSF1 in 20 µg of heat shocked HeLa cell lysate by ECL immunoblot analysis using Goat anti-rat IgG: HRP as the secondary antibody

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 KI et al. (2007). JBC Papers Online Manuscript M704081200. 4. Morimoto R. I. (1998) Genes Dev 12: 3788-3796. 5. McMillan D. R., Xiao X., Shao L., Graves K., and Benjamin I. J. (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., Farkas T., Dissing M., Kolding D. and Zimarino V. (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.