HSF1 Antibody, Clone 4B4: ATTO 390

Heat Shock Factor 1 (HSF1) is a key transcriptional regulator that orchestrates the cellular response to proteotoxic stress by activating genes involved in protein folding, degradation, and quality control. As the primary mediator of the heat shock response, HSF1 binds to heat shock elements (HSEs) in the promoters of heat shock protein (HSP) genes, driving the expression of molecular chaperones essential for maintaining proteostasis. Structurally, HSF1 contains a conserved N-terminal DNA-binding domain and adjacent hydrophobic repeats critical for trimerization and activation. A second hydrophobic region near the C-terminus suppresses trimer formation under non-stress conditions. In unstressed cells, HSF1 is diffusely localized in the cytoplasm and nucleus. Upon exposure to stressors—such as oxidative damage, heat, or protein misfolding—HSF1 rapidly translocates to nuclear stress granules, initiating a transcriptional program that restores protein homeostasis. In the context of neurodegenerative diseases, HSF1 plays a pivotal role in mitigating the toxic accumulation of misfolded proteins, a hallmark of disorders such as Alzheimer’s, Parkinson’s, and Huntington’s disease. By enhancing the expression of protective HSPs, HSF1 supports neuronal survival and function under chronic stress conditions. Its dynamic regulation and neuroprotective potential make HSF1 a compelling therapeutic target in neuroscience and neurodegeneration research.

1 µg/ml of SMC-477 was sufficient for detection of HSF1 in 20 µg of heat shocked HeLa cell lysate by colorimetric immunoblot analysis using Rabbit anti-rat IgG: AP 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 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.

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.