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The product of HSF1 is a heat-shock transcription factor. Additionally we are shipping HSF1 Antibodies (502) and HSF1 Proteins (16) and many more products for this protein.
Showing 10 out of 49 products:
Diminution in phenotypic variation for both gene expression and life span at 25 degrees C may be a consequence of low level hsf-1-dependent expression of HSP-16.2 and other chaperones at the higher temperature.
We demonstrate that while DAF-16/FOXO is dispensable, the age-dependent suppression of cilia phenotypes in IFT mutants requires cell-autonomous functions of the HSF1 heat shock factor and the Hsp90 chaperone
HSF-1 is a codeterminant of both alcohol and nicotine sensitivity in C. elegans and that this phenotype requires the small HSP, HSP-16.48. HSP-16.48 function in drug sensitivity is unrelated to a chaperone action during the heat shock stress response.
Heat-stress-enhanced ascaroside production appears to be mediated at least in part by HSF-1, which seems to be important in adaptation strategies for coping with heat stress in this nematode.
FUdR treatment can modulate the HSR and proteostasis, and should be used with caution when used to inhibit reproduction.
Excitation of the AFD thermosensory neurons is sufficient to activate HSF1 in another cell, even in the absence of temperature increase. Excitation of the AFD thermosensory neurons enhances serotonin release.
hsf-1 RNAi suppressed the restoration of thrashing reduced by heat stress. In contrast, hsf-1 knockdown cancelled prevention of movement reduction in a daf-2 mutant, but didn't suppress thrashing restoration in daf-2 mutant.
we engaged C. elegans mutants and identified that the p38 MAPK (show MAPK14 ELISA Kits) signaling, insulin (show INS ELISA Kits)/IGF-1 (show IGF1 ELISA Kits) signaling (IIS), and HSF-1 play pivotal roles in the WCESP-mediated host immune response
HSF-1 has a prominent role in cytoskeletal integrity, ensuring cellular function during stress and aging. Overexpression of pat-10 increased actin filament stability, thermotolerance, and longevity, indicating that in addition to chaperone regulation, HSF-1 has a prominent role in cytoskeletal integrity, ensuring cellular function during stress and aging.
HSF-1 represses the expression of daf-7 encoding a TGF-beta (show TGFB1 ELISA Kits) ligand, to induce young larvae to enter the dauer stage, a developmentally arrested, non-feeding, highly stress-resistant, long-lived larval form triggered by crowding and starvation.
These findings provide insight into the role of HSF1 in Leydig cell steroidogenesis, suggesting that it maintains cholesterol transport by recovering StAR under chronic heat stress.
In mammalian cell lines, only heat shock-induced but not basal expression of chaperones is dependent on the mammalian Hsf1 homolog.
Upregulating HSF1 relieves the tau toxicity in N2a-TauRD DeltaK280 by reducing CHOP (show DDIT3 ELISA Kits) and increasing HSP70 (show HSP70 ELISA Kits) a5 (BiP/GRP78 (show HSPA5 ELISA Kits)). Our work reveals how the bidirectional crosstalk between the two stress response systems promotes early tau pathology and identifies HSF1 being one likely key player in both systems.
HSF1 translationally augments the proteotoxic stress response.
HSF1 as a central regulator of cellular bioenergetics.
have demonstrated that the levels of HSF1 and heat shock proteins are significantly reduced in affected neuronal tissues from a TDP-43 (show TARDBP ELISA Kits) transgenic mouse model of amyotrophic lateral sclerosis and patients with sporadic amyotrophic lateral sclerosis.
HSF-1 ablation not only eliminates heat shock response, but it also transcriptionally up-regulates CYP7A1 (show CYP7A1 ELISA Kits) and MDR1/P-gp (show ABCB4 ELISA Kits) axis in WD-diet fed HSF-1(-/-)/LDLr (show LDLR ELISA Kits)(-/-) mice to reduce atherosclerosis.
Role of HSF1 in heart failure.HSF1 up-regulation of AC6 (show ADCY6 ELISA Kits).
Findings suggest that PGC1alpha protects against hyperthermia by cooperating with HSF1 in the induction of a transcriptional program devoted to the cellular protection from thermal insults.
Heat stress-associated increase in skeletal muscle mass may be induced by heat shock transcription factor 1 (HSF1) and/or HSF1-mediated stress response that activates muscle satellite cells and Akt (show AKT1 ELISA Kits)/p70S6K (show RPS6KB1 ELISA Kits) signalling pathway
piR (show PIR ELISA Kits)-823 increased the transcriptional activity of HSF1, the common transcription factor of HSPs, by binding to HSF1 and promoting its phosphorylation at Ser326.
Reporter assay showed that HSF1 increased the transcriptional activity of ATG4B (show ATG4B ELISA Kits) gene promoter, and chromatin immunoprecipitation assay verified that HSF1 bound to the site (-1429 to -1417) in ATG4B (show ATG4B ELISA Kits) gene promoter region.
Knockdown of HSF1 reduced the proliferation, migration and invasion of osteosarcoma cells, while overexpression of HSF1 promoted the proliferation, migration and invasion of osteosarcoma cells.
Data suggest that hnRNPK plays role in heat shock response of cells by regulating HSF1; hnRNPK inhibits HSF1 activity, resulting in reduced expression of HSP27 and HSP70 mRNAs; hnRNPK also down-regulates binding of HSF1 to heat shock response element. (hnRNPK = heterogeneous-nuclear ribonucleoprotein K; HSF1 = heat shock transcription factor 1; HSP = heat-shock protein)
Studies indicate correlations between heat shock transcription factor 1 (HSF1) activity and the incidence of several cancer types.
These findings suggest that HSF1 is important in the ovarian cancer TGFbeta (show TGFB1 ELISA Kits) response and in Epithelial-Mesenchymal Transition.
BRD4 (show BRD4 ELISA Kits) regulates splicing during heat shock by interacting with HSF1 such that under heat stress BRD4 (show BRD4 ELISA Kits) is recruited to nuclear stress bodies, and non-coding SatIII RNA transcripts are up-regulated.
Results demonstrate that p38 MAPK (show MAPK14 ELISA Kits) not only causes phosphorylation of HSF1 at S326 but also at S303/307 , and transcriptionally activates HSF1.
Heat Shock Factor 1 Depletion Sensitizes A172 Glioblastoma Cells to Temozolomide via Suppression of Cancer Stem Cell-Like Properties.
As the 4693-T mutation caused the disruption of microRNA target binding (resulting in the relief of the transcriptional repression), the HSF1 gene is useful in dairy cattle thermal tolerant breeding.
HSF1 is a key trans-acting factor for counteracting transgene promoter silencing in Chlamydomonas.
Data show that activated HSF1 and CRR1 transcription factors mediate the acetylation of histones H3/4, nucleosome eviction, remodeling of the H3K4 mono- and dimethylation marks, and transcription initiation/elongation.
data suggest that HSF1 is a key regulator of the stress response in Chlamydomonas
Data suggest that myocardial HSF1 and HSP70 (show HSP70 ELISA Kits) (70 kDa heat-shock protein (show HSPA9 ELISA Kits)) can be up-regulated by dietary factors (here, antioxidant taurine as a dietary supplement administered to counteract effects of atherogenic diet).
The results indicate that Heat shock protein 70 (Hsp70) mediates distinct stress-related functions in different tissues during transportation. Heat shock factor-1 (HSF-1) levels were reduced at 1 and 4 h only in the hearts of transported pigs.
The transcriptional up-regulation of unc45b, hsp90aa1.1 and smyd1b is specific to zebrafish mutants with myosin folding defects, and is not triggered in other zebrafish myopathy models
data suggest that HSF1 is involved in regulating constitutive lens specific expression of hsp70 (show HSPA1A ELISA Kits) in the embryonic zebrafish
The product of this gene is a heat-shock transcription factor. Transcription of heat-shock genes is rapidly induced after temperature stress. Hsp90, by itself and/or associated with multichaperone complexes, is a major repressor of this gene.
heat shock factor protein
, heat shock transcription factor
, Heat Shock Factor family member (hsf-1)
, HSF 1
, HSTF 1
, heat shock factor protein 1
, heat shock transcription factor 1