Product Name: HSF1
Product Number: AB-NN268-2
| Size: | 25 µg | Price: | 89.00 | |
| $US |
Target Full Name: Heat shock factor protein 1
Target Alias: HSTF1; Heat shock transcription factor 1; HSF 1
Product Type Specific: Heat shock/stress protein pan-specific antibody
Antibody Code: NN268-2
Antibody Target Type: Pan-specific
Protein UniProt: Q00613
Protein SigNET: Q00613
Antibody Type: Monoclonal
Antibody Host Species: Rat
Antibody Ig Isotype Clone: IgG1
Antibody Immunogen Source: Purified recombinant mouse HSF1 protein, epitope mapping to amino acids 425-439
Target Alias: HSTF1; Heat shock transcription factor 1; HSF 1
Product Type Specific: Heat shock/stress protein pan-specific antibody
Antibody Code: NN268-2
Antibody Target Type: Pan-specific
Protein UniProt: Q00613
Protein SigNET: Q00613
Antibody Type: Monoclonal
Antibody Host Species: Rat
Antibody Ig Isotype Clone: IgG1
Antibody Immunogen Source: Purified recombinant mouse HSF1 protein, epitope mapping to amino acids 425-439
Production Method: Protein G purified
Antibody Modification: Unconjugated. Contact KInexus if you are interest in having the antibody biotinylated or coupled with fluorescent dyes.
Antibody Concentration: 1 mg/ml
Storage Buffer: Phosphate buffered saline pH 7.4, 50% glycerol, 0.1% sodium azide
Storage Conditions: For long term storage, keep frozen at -40°C or lower. Stock solution can be kept at +4°C for more than 3 months. Avoid repeated freeze-thaw cycles.
Product Use: Western blotting | ICC/Immunofluorescence | Immunoprecipitation | ELISA | GS
Antibody Dilution Recommended: WB (1:1000), ICC/IF (1:100); optimal dilutions for assays should be determined by the user.
Antibody Modification: Unconjugated. Contact KInexus if you are interest in having the antibody biotinylated or coupled with fluorescent dyes.
Antibody Concentration: 1 mg/ml
Storage Buffer: Phosphate buffered saline pH 7.4, 50% glycerol, 0.1% sodium azide
Storage Conditions: For long term storage, keep frozen at -40°C or lower. Stock solution can be kept at +4°C for more than 3 months. Avoid repeated freeze-thaw cycles.
Product Use: Western blotting | ICC/Immunofluorescence | Immunoprecipitation | ELISA | GS
Antibody Dilution Recommended: WB (1:1000), ICC/IF (1:100); optimal dilutions for assays should be determined by the user.
Antibody Potency: Detects a ~85 kDa protein (unstressed cell lysates) and ~95 kDa protein (heat shocked cell lysates).
Antibody Species Reactivity: Human | Mouse | Rat | Bovine | Guinea Pig | Hamster | Monkey | Rabbit
Antibody Positive Control: 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.
Related Product 1: HSF1 pan-specific antibody (Cat. No.: AB-NN268-1)
Related Product 2: HSF1 pan-specific antibody (Cat. No.: AB-NN268-3)
Related Product 3: HSF1 pan-specific antibody (Cat. No.: AB-NN268-4)
Antibody Species Reactivity: Human | Mouse | Rat | Bovine | Guinea Pig | Hamster | Monkey | Rabbit
Antibody Positive Control: 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.
Related Product 1: HSF1 pan-specific antibody (Cat. No.: AB-NN268-1)
Related Product 2: HSF1 pan-specific antibody (Cat. No.: AB-NN268-3)
Related Product 3: HSF1 pan-specific antibody (Cat. No.: AB-NN268-4)
Scientific 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 N-terminus. 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 transcriptionally 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.
[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.
[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.
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