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The product of HSF1 is a heat-shock transcription factor. Additionally we are shipping HSF1 Antibodies (498) and HSF1 Proteins (14) and many more products for this protein.
Showing 10 out of 51 products:
a critical role for autophagy in C. elegans stress resistance and hormesis, and reveal a requirement for autophagy in HSF-1 regulated functions in the heat-shock response, proteostasis, and aging.
xyloketal derivatives bound to the DNA binding domain of HSF-1, promoted the conformation of HSF-1, thus strengthened the interaction between the HSF-1 and related DNA. ALA-67, ASN-74 and LYS (show LYZ ELISA Kits)-80 of binding region might be the key amino residues during the interaction.
These functions of HPK-1/HSF-1 undergo rapid down-regulation once animals reach reproductive maturity. We show that HPK-1 fortifies proteostasis and extends longevity by an additional independent mechanism: induction of autophagy.
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.
HSF1 activity is decreased in fibrotic hearts. HSF1 inhibits phosphorylation and nuclear distribution of Smad3 (show SMAD3 ELISA Kits) via direct binding to Smad3 (show SMAD3 ELISA Kits). Active Smad3 (show SMAD3 ELISA Kits) blocks the anti-fibrotic effect of HSF1.
the expression level of NFATc2 (show NFAT1 ELISA Kits), miR (show MLXIP ELISA Kits)-208b and miR (show MLXIP ELISA Kits)-499 suggested that these responses were suppressed in HSF1-null mice
identify 4 huntingtin (show HTT ELISA Kits)-targeting miRNAs viz. miR (show MLXIP ELISA Kits)-125b, miR (show MLXIP ELISA Kits)-146a, miR (show MLXIP ELISA Kits)-150 and miR (show MLXIP ELISA Kits)-214 as candidate miRNAs responsible for observed inhibitory effect of HSF1 on huntingtin (show HTT ELISA Kits) expression.
HSF1 plays an important role in the occurrence of UVR-B-induced cataracts, possibly via regulation of HSPs such as HSP25 (show HSPB1 ELISA Kits).
Targeted deletion of HSF1 results in changes of locomotor function associated with changes in cerebellar calbindin (show CALB1 ELISA Kits) protein levels. These findings suggest a role of HSF1 in regular Purkinje cell calcium homeostasis.
this study shows that HSF1 overexpression protects against TDP-43 (show TARDBP ELISA Kits) pathology by upregulation of chaperones, especially HSP70 (show HSP70 ELISA Kits), rather than enhancing autophagy
Acetylation of the protein triggers TDP-43 (show TARDBP ELISA Kits) pathology in cultured cells and mouse skeletal muscle, which can be cleared through an HSF1-dependent chaperone mechanism that disaggregates the protein.
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.
These findings indicate that activation of HSF1 at Ser326 residue and transcription of HSP27 (show HSPB1 ELISA Kits) is related to the maintenance of gynecological CSCs/CICs.
Results show that HSF1 is a key transcription factor for inducing the expression of DNAJB8 and SOX2 (show SOX2 ELISA Kits) and that cellular stress induces cancer stem-like cells through the expression of DNAJB8 by activation of HSF1 .
The mRNA expression levels of heat shock transcription factor 1 (HSF1) in estrogen receptor (ER (show ESR1 ELISA Kits))-positive breast cancer are associated with both shorter relapse-free and overall survival.
Our study provides evidence that HSF1 functions as a novel oncogene (show RAB1A ELISA Kits) in pancreatic tumors and is implicated as a target for the diagnosis and treatment of pancreatic cancer.
In normal ovarian tissues, HSF1 was barely detected, whereas, high expression of HSF1 was found in malignant epithelial ovarian cancer (EOC) tissues, including serous, mucinous, endometrioid, and clear cell EOC tissues.
Our findings show that miR-487a, mediated by heat shock factor 1, promotes proliferation and metastasis of Hepatocellular carcinoma (HCC) by PIK3R1 and SPRED2 binding, respectively. Our study provides a rationale for developing miR-487a as a potential prognostic marker or a potential therapeutic target against HCC.
Results suggest for targeting heat shock factor 1 (HSF1)activation in combination with bortezomib to enhance multiple myeloma treatment efficacy.
MD simulation of high-resolution X-ray structures reveals post-translational modification dependent conformational changes in HSF-DNA interaction.
We found that HSF1 activation mediated by 1,4-NQ upregulated downstream genes, such as HSPA6 (show HSPA6 ELISA Kits). The results suggest that activation of the HSP90 (show HSP90 ELISA Kits)-HSF1 signal transduction pathway mediated by 1,4-NQ protects cells against 1,4-NQ and that per/polysulfides can diminish the reactivity of 1,4-NQ by forming sulfur adducts.
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