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HSF1 antibody (Heat Shock Factor Protein 1) (AA 378-395)

Details for Product anti-HSF1 Antibody No. ABIN361703, Supplier: Log in to see
Antigen
Epitope
AA 378-395
86
31
27
20
19
17
15
15
15
15
14
13
13
10
10
7
6
6
5
3
3
3
3
2
2
2
2
2
2
2
2
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
Reactivity
Cow (Bovine), Guinea Pig, Hamster, Human, Monkey, Mouse (Murine), Rabbit, Rat (Rattus)
361
249
131
69
65
62
60
59
2
2
1
1
1
1
Host
Rat
275
133
28
1
Clonality (Clone)
Monoclonal ()
Conjugate
This HSF1 antibody is un-conjugated
14
14
11
11
11
10
7
7
7
7
7
7
7
7
7
7
7
4
2
2
2
2
2
2
2
2
Application
Gel Shift (GS), Immunocytochemistry (ICC), Immunofluorescence (IF), Immunoprecipitation (IP), ELISA, Western Blotting (WB)
368
221
142
140
132
112
108
47
26
6
5
5
2
1
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Immunogen Purified recombinant mouse HSF1 protein, with epitope mapping to amino acids 378-395
Clone 10H8
Specificity Detects ~85 kDa (unstressed cell lysates), and~95 kDa (heat shocked cell lysates).
Sensitivity 1 µg/mL of SMC-118 was sufficient for detection of HSF1 in 20 µg of heat shocked HeLa cell lysate by ECL immunoblot analysis using Goat anti-rat IgG:HRP as the secondary antibody
Purification Protein G Purified
Alternative Name HSF1 (HSF1 Antibody Abstract)
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).
Cellular Localization: Cytoplasm | Nucleus
Gene ID 15499
NCBI Accession NP_032322
UniProt P38532
Research Area Chromatin and Nuclear Signaling, Transcription Factors, Heat Shock Proteins, Neurology
Application Notes Recommended Dilution: WB (1:1000), ICC/IF (1:200), optimal dilutions for assays should be determined by the user.
Restrictions For Research Use only
Format Liquid
Concentration 1 mg/mL
Buffer PBS pH 7.4, 50 % glycerol, 0.09 % sodium azide
Preservative Sodium azide
Precaution of Use This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Storage -20 °C
Supplier Images
 image for anti-HSF1 antibody (Heat Shock Factor Protein 1) (AA 378-395) (ABIN361703) HSF1 (10H8), HeLa cells mitosis
Background publications Monechi, Fiumalbi, De Monte et al.: "[Investigation on health status of silica exposed workers in 'cotto Fiorentino' companies]" in: Giornale italiano di medicina del lavoro ed ergonomia, Vol. 29, Issue 3 Suppl, pp. 736-7, 2008 (PubMed).

Tanaka, Namba, Arai et al.: "Genetic evidence for a protective role for heat shock factor 1 and heat shock protein 70 against colitis." in: The Journal of biological chemistry, Vol. 282, Issue 32, pp. 23240-52, 2007 (PubMed).

Morano, Thiele: "Heat shock factor function and regulation in response to cellular stress, growth, and differentiation signals." in: Gene expression, Vol. 7, Issue 4-6, pp. 271-82, 1999 (PubMed).

Jolly, Usson, Morimoto: "Rapid and reversible relocalization of heat shock factor 1 within seconds to nuclear stress granules." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 96, Issue 12, pp. 6769-74, 1999 (PubMed).

Morimoto: "Regulation of the heat shock transcriptional response: cross talk between a family of heat shock factors, molecular chaperones, and negative regulators." in: Genes & development, Vol. 12, Issue 24, pp. 3788-96, 1999 (PubMed).

McMillan, Xiao, Shao et al.: "Targeted disruption of heat shock transcription factor 1 abolishes thermotolerance and protection against heat-inducible apoptosis." in: The Journal of biological chemistry, Vol. 273, Issue 13, pp. 7523-8, 1998 (PubMed).

Cotto, Fox, Morimoto: "HSF1 granules: a novel stress-induced nuclear compartment of human cells." in: Journal of cell science, Vol. 110 ( Pt 23), pp. 2925-34, 1998 (PubMed).

Rallu, Loones, Lallemand et al.: "Function and regulation of heat shock factor 2 during mouse embryogenesis." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 94, Issue 6, pp. 2392-7, 1997 (PubMed).

Sarge, Park-Sarge, Kirby et al.: "Expression of heat shock factor 2 in mouse testis: potential role as a regulator of heat-shock protein gene expression during spermatogenesis." in: Biology of reproduction, Vol. 50, Issue 6, pp. 1334-43, 1994 (PubMed).

Murphy, Gorzowski, Sarge et al.: "Characterization of constitutive HSF2 DNA-binding activity in mouse embryonal carcinoma cells." in: Molecular and cellular biology, Vol. 14, Issue 8, pp. 5309-17, 1994 (PubMed).

Fiorenza, Farkas, Dissing et al.: "Complex expression of murine heat shock transcription factors." in: Nucleic acids research, Vol. 23, Issue 3, pp. 467-74, 1995 (PubMed).

Goodson, Park-Sarge, Sarge: "Tissue-dependent expression of heat shock factor 2 isoforms with distinct transcriptional activities." in: Molecular and cellular biology, Vol. 15, Issue 10, pp. 5288-93, 1995 (PubMed).