HSF1 Antibody, Clone 4B4

Rat Anti-Mouse HSF1 Monoclonal IgG1

Product Specifications

Background

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.

CAS Number

9007-83-4

Specifications

Detects ~85kDa (unstressed cell lysates) and ~95kDa (heat shocked cell lysates).

Product Name Alternative

HSF1, Heat shock factor protein 1, Heat shock transcription factor 1, HSTF1, HSF 1

Synonyms

HSF1 Antibody, Clone 4B4

UNSPSC

12352203

UN Code

Non-hazardous

Hazard Statement

Non-hazardous

Gene ID

15499

Swiss Prot

P38532

Accession Number

NP_032322.1

Cellular Locus

Cytoplasm | Nucleus

Host

Rat

Species Reactivity

Human,Mouse,Rat,Bovine,Guinea Pig,Hamster,Monkey,Rabbit

Immunogen

Purified recombinant mouse HSF1 protein, epitope mapping to amino acids 425-439

Target

HSF1

Clonality

Monoclonal

Isotype

IgG1

Clone

4B4

Conjugation

Unconjugated

Type

Monoclonal

Applications

WB | IHC | ICC/IF | IP | ELISA | GS

Validated Applications

WB,IHC,ICC/IF,IP,ELISA,GS

Field of Research

Purification

Protein G Purified

Limit Of Detection

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.

Concentration

1 mg/ml

Dilution

WB (1:1000), IHC (1:2000), ICC/IF (1:100) ; optimal dilutions for assays should be determined by the user.

Weight

0.1

Buffer

PBS pH7.4, 50% glycerol, 0.1% sodium azide *Storage buffer changes when conjugated

Precautions

Not for use in humans. Not for use in diagnostics or therapeutics. For in vitro research use only.

References & Citations

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.

Shipping Conditions

Blue Ice or 4ºC

Storage Conditions

-20ºC

Specificity

Detects ~85kDa (unstressed cell lysates) and ~95kDa (heat shocked cell lysates) .

Background Reference 01

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.