Heat Shock Factor 1 (HSF1)

The synthesis of heat shock proteins is dependent on transcriptional and post-transcriptional control in eukaryotic cells. The regulation of heat shock gene transcription is mediated by the transcriptional activator, Heat Shock Factor (HSF), which binds to heat shock response elements (HSEs) in the upstream region of heat shock gene and activates their transcription. At least three HSFs have been isolated from the human, mouse, chicken and tomato genomes. An additional factor, HSF4, has been identified in humans. HSFs purified from yeast, Drosophila and human have different molecular weights and do not crossreact immunologically. These factors are activated by distinct stimuli. HSF1 responds to cellular stress signals such as heat, heavy metals and oxidative reagents. HSF2 is activated during differentiation. Some laboratories have reported that the constitutive, non-DNA binding, monomeric form of inactive HSF1 is located in the cytoplasm. Upon activation, HSF1 is trimerized and is localized in nucleus where it binds DNA. The phosphorylation of HSF1 may be necessary for maximal transcription of heat shock genes.\n\nApplications:\nSuitable for use in Immunofluorescence, Immunoprecipitation and Western Blot. Other applications not tested.\n\nRecommended Dilutions:\nImmunoprecipitation (Native only): 2ug/mg protein lysate using Protein G\nWestern Blot: 1-2ug/ml\nOptimal dilutions to be determined by the researcher.\n\nSource: Ascites\n\nPositive Control:\nLS174T or MAD109 cells\n\nStorage and Stability:\nMay be stored at 4 degrees C for short-term only. For long-term storage and to avoid repeated freezing and thawing, aliquot and store at -20 degrees C. Aliquots are stable for at least 12 months at -20 degrees C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.

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SPECIFICATIONS

Catalog Number

H1832

Size

250ul

Applications

IF, IP, WB

Hosts

Rat

Reactivities

Hum, Mouse, Rat

Form

Supplied as a liquid in PBS, pH 7.4, 0.2% BSA, 0.09% sodium azide, before the addition of sterile glycerol to 80%. Also available without BSA and azide. See Cat# H1832X.

P Type

Mab

Purity

Purified by ammonium sulfate precipitation.

Isotype

IgG1

References

1. Baler, R., Dahl, G., Voellmy, R. (1993). Activation of human heat shock genes is accompanied by oligomerization, modification, and rapid translocation of heat shock transcription factor HSF1. Molecular & Cellular Biology, 13:2486-96. 2. Clos, J., Westwood, J. T., Becker, P. B., Wilson, S., Lambert, K., and Wu, C. (1990). Molecular cloning and expression of a hexameric Drosophila heat shock factor subject to negative regulation. Cell, 63:1085-97. 3. Cotto,.J. J.; Kline, M.; Morimoto, R.I. (1996). Activation of heat shock factor 1 DNA binding precedes stress-induced serine phosphorylation. Evidence for a multistep pathway of regulation. Journal of Biological Chemistry, 271(7):3355-8. 4. Craig, E. A., Gambill, B. D., and Nelson, R. J. (1993). Heat shock proteins: molecular chaperones of protein biogenesis. Microbiological Rev, 5:402-14.\n5. Edington, B. V., Whelan, S. A., and Hightower, L. E. (1989). Inhibition of heat shock (stress) protein induction by deuterium oxide and glycerol: additional support for the abnormal protein hypothesis of induction. J Cell Phys, 139:219-28. 6. Georgopoulos, C., and Welch, W. J. (1993). Role of the major heat shock proteins as molecular chaperones. Annual Review of Cell Biol, 9:601-34. 7. Gething, M. J., and Sambrook, J. (1992). Protein folding in the cell. Nature, 355:33-45. 8. Hartl, F. U. (1996). Molecular chaperones in cellular protein folding. Nature, 381:571-9. 9. Hendrick, J. P., and Hartl, F. U. (1993). Molecular chaperone functions of heat-shock proteins. Annual Review of Biochem, 62:349-84. 10. Hendrick, J. P., and Hartl, F. U. (1995). The role of molecular chaperones in protein folding. FASEB Journal, 9:1559-69.\nAdditional References: 1. Hightower, L. E. (1991). Heat shock, stress proteins, chaperones, and proteotoxicity. [Review]. Cell, 66:191-7. 2. Jurivich, D. A., Sistonen, L., Kroes, R. A., and Morimoto, R.I. (1992). Effect of sodium salicylate on the human heat shock response. Science 255, 1243-5. 3. Mezger, V., Rallu, M., Morimoto, R. I., Morange, M., and Renard, J. P. (1994). Heat shock factor 2-like activity in mouse blastocysts. Developmental Biology, 166:819-22. 4. Morimoto, R. I., Jurivich, D. A., Kroeger, P. E., Mathur, S.K., Murphy, S. P., Nakai, A., Sarge, K., Abravaya, K., and Sistonen, L. T. (1994). Regulation of Heat Shock Gene Transcription by a Family of Heat Shock Factors. In The Biology of Heat Shock Proteins and Molecular Chaperones, R. I. Morimoto, A. Tissieres and C. Georgopoulos, eds. (Cold Spring Harbor, N.Y.: Cold Spring Harbor Laboratory Press), 417-456. 5. Murphy, S. P., Gorzowski, J., Sarge, K. D., and Phillips, B. (1994). Characterization of constitutive HSF2 DNA-binding activity in mouse embryonal carcinoma cells. Molecular and Cellular Biology, 14:5309-17. 6. Nakai, A., and Morimoto, R. I. (1993). Characterization of a novel chicken heat shock transcription factor, heat shock factor 3, suggests a new regulatory pathway. Molecular and Cellular Biology, 13:1983-97. 7. Parsell, D. A., and Lindquist, S. (1993). The function of heatshock proteins in stress tolerance: degradation and reactivation of damaged proteins. Annual Review of Genetics, 27:437-96. 8. Pelham, H. R. (1986). Speculations on the functions of the major heat shock and glucose-regulated proteins. Cell, 46:959-61. 9. Peteranderl, R., and Nelson, H. C. (1992). Trimerization of the heat shock transcription factor by a triple-stranded alphahelical coiled-coil. Biochemistry, 31:12272-6. 10. Rabindran, S. K., Giorgi, G., Clos, J., and Wu, C. (1991). Molecular cloning and expression of a human heat shock factor, HSF1. Proceedings of the National Academy of Sciences of the United States of America, 88:6906-10. 11. Rabindran, S. K., Haroun, R. I., Clos, J., Wisniewski, J., and Wu, C. (1993). Regulation of heat shock factor trimer formation: role of a conserved leucine zipper. Science, 259:230-4. 12. Sarge, K. D., Murphy, S. P., and Morimoto, R. I. (1993). Activation of heat shock gene transcription by heat shock factor 1 involves oligomerization, acquisition of DNAbinding activity, and nuclear localization and can occur in the absence of stress [published errata appear in Mol Cell Biol, 1993 May; 13(5):3122-3 and 1993 Jun; 13(6):3838-9]. Molecular & Cellular Biology, 13:1392-407. 13. Sarge, K. D., Park, S. O., Kirby, J. D., Mayo, K. E., and Morimoto, R. I. (1994). Expression of heat shock factor 2 in mouse testis: potential role as a regulator of heat-shock protein gene expression during spermatogenesis. Biology of Reprod, 50: 1334-43. 14. Sarge, K. D., Zimarino, V., Holm, K., Wu, C., and Morimoto, R. I. (1991). Cloning and characterization of two mouse heat shock factors with distinct inducible and constitutive DNAbinding ability. Genes and Development, 5:1902-11. 15. Scharf, K. D., Rose, S., Zott, W., Schoff, F., and Nover, L. (1990). Three tomato genes code for heat stress transcription factors with a remarkable degree of homology to the DNAbinding domain of the yeast HSF. EMBO J, 9:4495-4501. 16. Schuetz, T. J., Gallo, G. J., Sheldon, L., Tempst, P., and Kingston, R. E. (1991). Isolation of a cDNA for HSF2: evidence for two heat shock factor genes in humans. Proceedings of the National Academy of Sciences of the United States of America, 88:6911-5. 17. Sistonen, L., Sarge, K. D., and Morimoto, R. I. (1994). Human heat shock factors 1 and 2 are differentially activated and can synergistically induce hsp70 gene transcription. Molecular and Cellular Biology, 14:2087-99. 18. Sistonen, L., Sarge, K. D., Phillips, B., Abravaya, K., and Morimoto, R. I. (1992). Activation of heat shock factor 2 during hemin-induced differentiation of human erythroleukemia cells. Molecular and Cellular Biology, 12:4104-11. 19. Sorger, P. K., Lewis, M. J., and Pelham, H. R. (1987). Heat shock factor is regulated differently in yeast and HeLa cells. Nature, 329:81-4. 20. Sorger, P. K., and Nelson, H. C. (1989). Trimerization of a yeast transcriptional activator via a coiled-coil motif. Cell, 59:807-13.

Additional Info

Recognizes mouse Heat Shock Factor 1 (HSF1) at 70-85kD, depending on the source and state of cells. Species Crosseactivity: human and rat.