Anti-HSF1 Antibody

Nucleus, Cytoplasm, Nucleus, nucleoplasm, Cytoplasm, perinuclear region, Cytoplasm, cytoskeleton, spindle pole, Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, Chromosome, centromere, kinetochore

Functions as a stress-inducible and DNA-binding transcription factor that plays a central role in the transcriptional activation of the heat shock response (HSR), leading to the expression of a large class of molecular chaperones heat shock proteins (HSPs) that protect cells from cellular insults' damage (PubMed:1871105, PubMed:11447121, PubMed:1986252, PubMed:7760831, PubMed:7623826, PubMed:8946918, PubMed:8940068, PubMed:9341107, PubMed:9121459, PubMed:9727490, PubMed:9499401, PubMed:9535852, PubMed:12659875, PubMed:12917326, PubMed:15016915, PubMed:25963659, PubMed:26754925, PubMed:18451878). In unstressed cells, is present in a HSP90-containing multichaperone complex that maintains it in a non-DNA-binding inactivated monomeric form (PubMed:9727490, PubMed:11583998, PubMed:16278218). Upon exposure to heat and other stress stimuli, undergoes homotrimerization and activates HSP gene transcription through binding to site-specific heat shock elements (HSEs) present in the promoter regions of HSP genes (PubMed:1871105, PubMed:1986252, PubMed:8455624, PubMed:7935471, PubMed:7623826, PubMed:8940068, PubMed:9727490, PubMed:9499401, PubMed:10359787, PubMed:11583998, PubMed:12659875, PubMed:16278218, PubMed:25963659, PubMed:26754925). Upon heat shock stress, forms a chromatin-associated complex with TTC5/STRAP and p300/EP300 to stimulate HSR transcription, therefore increasing cell survival (PubMed:18451878). Activation is reversible, and during the attenuation and rPubMed:10359787, PubMed:11447121, PubMed:11583998, PubMed:12659875, PubMed:12917326, PubMed:14707147, PubMed:15016915, PubMed:16278218, PubMed:17897941, PubMed:18451878, PubMed:1871105, PubMed:18794143, PubMed:1986252, PubMed:25963659, PubMed:26359349, PubMed:26727489, PubMed:26754925, PubMed:7623826, PubMed:7760831, PubMed:7935471, PubMed:8455624, PubMed:8940068, PubMed:8946918, PubMed:9121459, PubMed:9341107, PubMed:9499401, PubMed:9535852, PubMed:9727490}.; (Microbial infection) Plays a role in latent human immunodeficiency virus (HIV-1) transcriptional reactivation. Binds to the HIV-1 long terminal repeat promoter (LTR) to reactivate viral transcription by recruiting cellular transcriptional elongation factors, such as CDK9, CCNT1 and EP300. {PubMed:27189267}.

Immunoblotting: use at 1-2ug/mL. A band of ~85 and/or ~95 kDa is detected. <br><br>Immunocytochemistry: use at 10ug/mL. <br><br>Immunoprecipitation: use at 12.5ug/mL <br><br>These are recommended concentrations. User should determine optimal concentrations for their application. <br><br>Positive control: HeLa cell lysate

This antibody recognizes an ~85 kDa protein (inactive form) in unstressed cell lysates and an ~95 kDa protein (active form) in heat-shocked cell lysates of human, mouse, rat, rabbit, bovine, guinea pig, hamster, and monkey.

Heat shock factor 1 (HSF1) is a heat shock transcription factor that activates the transcription of genes encoding products required for protein folding, processing, targeting, degradation, and function. Up- regulation of expression of heat shock proteins in response to stress occurs at the level of transcription through a heat shock element and a HSF transcription factor. Amino acid sequences for most HSFs are highly conserved. A DNA binding domain is at the N-terminus, hydrophobic repeats (essential to the formation of active trimers) are adjacent to this binding domain, and another short hydrophobic repeat (necessary for suppression of trimerization) occurs toward the C-terminus. In higher eukaryotes, HSF1 is distributed diffusely in the cell cytoplasm and nucleus in unstressed cells. On exposure to heat shock or other stresses, HSF1 localizes to discrete nuclear granules; on recovery from stress, it returns to a diffuse nuclear- cytoplasmic distribution.