Product Name	HSF1 Antibody
Catalog #	SMC-118D
Package size	100ug

Alternate Product Sizes	SMC-118C
Type	Monoclonal
Conjugate	N/A
Datasheet	SMC 118 Heat Shock Factor 1 (HSF1)
Description	Anti-HSF1
Research Area	Heat Shock
Alternative Names	HSTF1
Clone Number	10H8
Host Species	Rat
Isotype	IgG1
Immunogen	Purified recombinant HSF1 of mouse origin, epitope mapping to amino acids 378-395
Applications	WB, IP, ICC, ELISA, Gel mobility shift assay
Species Reactivity	Human, Mouse, Rat, Bovine, Guinea Pig, Hamster, Monkey, Rabbit
Accession Number	NP_005517.1
Gene ID	3297
SwissProt	Q00613
Background Info	Detects an ~85kDa protein in unstressed cell lysates, and an ~95kDa protein in heat shocked cell lysates, corresponding to the molecular mass of inactive and active forms of HSF1 on SDS PAGE immunoblots.
Recommended Dilutions	1 µg/ml was sufficient for detection of HSF1 by ECL immunoblot in 20 µg of HeLa lysate.
Form	Protein G Purified
Storage Buffer	PBS pH7.4, 50% glycerol, 0.09% sodium azide
Concentration	1mg/mL
Certificate of Analysis	1 μg/mL of SMC-118 was sufficient for detection of HSF1 in 20μg of heat shocked HeLa cell lysate by ECL immunoblot analysis using Goat anti-rat IgG: HRP as the secondary antibody
Storage Temp	-20 °C
Shipping Temp	Blue Ice or 4 °C

HSF1 granules present in heat-shocked mitotic cells (green) detected by IF in mitotic heat shocked HeLa cells.
Courtesy of Morimoto Lab, Northwestern University, USA.

Research 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 Nterminus. 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 transciptionally 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 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.
Cited References	1. Asai, M. et al. (2011). Protective effect of a molecular chaperone inducer, paeoniflorin, on the HCl- and ethanol-triggered gastric mucosal injury. Life Sciences. 88 (7-8), 350-357. doi:10.1016/j.lfs.2010.12.014