Rat anti-HSF1 (Clone : 10H8) - SMC-118D
|Product Name ||HSF1 Antibody|
|Catalog # ||SMC-118D|
|Package size ||100ug|
|Alternate Product Sizes ||SMC-118C|
|Datasheet ||SMC 118 Heat Shock Factor 1 (HSF1)|
|Research Area ||Heat Shock|
|Alternative Names ||HSTF1|
|Clone Number ||10H8|
|Host Species ||Rat|
|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|
|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|
|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|