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Validated All-in-One™ qPCR Primer for HSF1(NM_005526.3) Search again
Product ID:
HQP009068
(click here to view gene annotation page)
Powered by BiozSpecies:
Human
Symbol:
Alias:
HSTF1
Gene Description:
heat shock transcription factor 1
Target Gene Accession:
NM_005526.3(click here to view gene page)
Estimated Delivery:
Approximately 1-3 weeks, but may vary. Please email sales@genecopoeia.com or call 301-762-0888 to confirm ETA.
Important Note:
By default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Validated result:
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| A | B |
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Each All-in-One™ qPCR Primer is experimentally validated to yield a single dissociation curve peak and to generate a single amplification of the correct size for the targeted gene. A cDNA Pool, containing reverse transcript products of 8 different human tissue total RNA(Liver, Testis,Muscle,Thyroid,Brain,Spleen,Stomach,Small Intestine)),was used as the qPCR validation template. qPCR was performed using 0.2 µM primer with 2XAll-in-One™ qPCR Mix (Catalog#: QP001,QP002,QP004,QP005). Reactions were incubated for 10min. at 95°C, followed by 40 cycles of 95°C for 10 sec.; 60°C, 20 sec. and 72°C, 15sec. using Bio-Rad iQ5™ Instrument. At the end of the last cycle, temperature was increased from 72 to 95°C to produce a melting curve. Panel A: Validated Result for Amplification Curve; Panel B: Validated Result for Melting Curve. |
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Summary
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.
Gene References into function
- Heat shock factor 1 represses transcription of the IL-1beta gene through physical interaction with the nuclear factor of interleukin 6
- Retrovirus-mediated transfer of dominant-negative mutant HSF1 leads to massive cell death of breast cancer cells after hyperthermia treatment.
- redox-dependent thiol-disulfide exchange in regulating conformation and activity
- HSF1 granules localize to the 9q11-q12 heterochromatic region. Within this locus, HSF1 binds through direct DNA-protein interaction with a nucleosome-containing subclass of satellite III repeats.
- Binding of the heat shock element of HSP47 by HSF1 is enhanced by TGF-beta or IL-1 beta and is augmented by a combination of both cytokines.
- HSF1 contains two functional domains that mediate transcriptional repression of the c-fos and c-fms genes
- examination of the role of the phosphorylation event in regulating SUMO-1 modification of HSF1
- HSF1 activation by heat is correlated with the thermal activation of nuclear CK2 and overexpression of CK2 activates HSF1
- HSF1 is modified by SUMO-1 and SUMO-2 in a stress-inducible manner.
- elevated expression of heat shock factor (HSF) 2A stimulates HSF1-induced transcription during oxidative stress in cancer cells
- modified heat shock factor can suppress HIV1 promoter activity by a mechanism involving interaction with Sp1 elements in the HIV1 promoter
- HSF1 binding to 14-3-3 epsilon requires HSF1 phosphorylation on serines 303 and 307, the serine phosphorylation-dependent binding of HSF1 to 14-3-3 epsilon results in the transcriptional repression of HSF1 and its sequestration in the cytoplasm.
- HSF1 does not have a role in transcriptional regulation of the human RANK ligand gene
- HSF1 regulates HSP gene expression at not one but two different steps of the expression pathway, functioning both as a transcription factor and a polyadenylation stimulatory factor
- HSF is an important transcription factor involved in up-regulation of VDUP1 expression by stresses such as high density and serum deprivation cultures
- results suggest that ASC-2 is a novel coactivator for HSF1 and heat shock stress may contribute to the strong active transcription complex through sequential recruitment of HSF1 and ASC-2.
- regulation by N-terminal truncated form of p73alpha
- HSF1 plays a functional role in cancer cells under nonstress conditions and influences cell cycle behavior and progression through mitosis and promotes the development of the aneuploid state
- Results suggest that mutant HSF1 abolishes thermotolerance in Bcap37 cells by enhancing Jun kinase and caspase-3 pathways after hyperthermia.
- HSF1 associates with ERK1 and 14-3-3epsilon during heat shock to modulate the amplitude of the response and lead to efficient termination of HSP expression on resumption of growth conditions
- The induction of HSF1 gene expression is associated with sporadic colon cancer.
- phosphorylation of HSF1 by PLK1 is an essential step for HSF1 nuclear translocation by heat stress
- Inactive, stress-responsive form of HSF1 accumulates in the nucleus due to a relatively potent import signal, which can be recognized by importin-alpha/beta, and simultaneously undergoes continuous nucleocytoplasmic shuttling.
- Phosphorylation of HSF1 residue serine326 plays a critical role in the induction of the factor's transcriptional competence by heat stress; phosphoSer326 also contributes to activation of HSF1 by chemical stress
- Hsp90 is involved in hsp70 mRNA stabilisation and the HSF1 activation can be suppressed by high hydrostatic pressure
- HSF1 has a strong inhibitory effect on polyglutamine aggregate formation in vivo and in vitro
- HSF1 phosphorylation by MAPK-activated protein kinase 2 on serine 121, inhibits transcriptional activity and promotes HSP90 binding
- CHIP directly interacts with C-terminal deleted HSF1 but not with full-length HSF1 under non-stressed conditions, and with full-length HSF1 under heat shock treatment; interaction requires conformational change of HSF1 by heat stress.
- endogenous stress pressure in cancer cells sustained the high level expression of HSF1 and subsequently suppressed XAF1 expression, implicating the synergized effect of two anti-apoptotic protein families in cytoprotection under stress circumstances
- HSF1 can activate MDR-1 expression in a stress-independent manner that differs from the canonical heat shock-activated mechanism involved in HSP induction.
- Both NF-kappaB and HSF-1 are systemically activated in human acute pancreatitis. HSF-1 activation may protect against severity of pancreatitis.
- HSP25 and HSP70i activate HSF1 and have roles in inhibition of ERK1/2 phosphorylation
- Wild-type and constitutively active forms of HSF1 induce anticoagulation and relaxation factors in vascular endothelial cells and could therefore be used to treat cardiovascular disease.
- Both HSF1 and HSF2 were able to bind the hsp70 promoter not only in response to heat shock but also during hemin-induced differentiation of K562 erythroleukemia cells.
- identification of genes regulated directly and indirectly by HSF1
- HSF1 is directly involved in the regulation of HO-1 with an anti-oxidative role
- IL-6, via the PI3-kinase/Akt pathway leads to inhibition of the repressive kinases MAPK/pERK and GSK3beta, and this converts inactive HSF-1 to an intermediate DNA-binding form augmenting transcriptional activation in the presence of a second stressor.
- activation of HSF1 and stabilization of Bcl-X(L) mediate a protective response that may contribute significantly to the cellular biology of lipid peroxidation
- Human cancer lines of diverse origins show much greater dependence on HSF1 function to maintain proliferation and survival than their nontransformed counterparts.
- HSP mRNA export escapes stress inhibition via HSF1-mediated recruitment of the nuclear pore-associating protein TPR to HSP genes, functionally connecting the first and last nuclear steps of the gene expression pathway, transcription and mRNA export.
- study shows HSF1 binds to MTA1 in vitro & in breast carcinoma; repression of estrogen-dependent transcription may contribute to role of HSF1 in cancer
- Two of the three putative heat shock-responsive elements (HSEs) in bag3 promoter interact with the heat shock factor (HSF) 1 in vitro and in vivo.
- HSP70 and constitutively active HSF1 mediate protection against CDCrel-1-mediated toxicity
- the lack of a trimerization domain prevents HSF1 activation, which suggests that iHI-m noncovalent trimerization is a precondition of SS-I bond formation.
- Hsf-1 causes specific and saturable inhibition of the transport activity of Ralbp1 and that the combination of Hsf-1 and POB1 causes nearly complete inhibition through specific bindings with Ralbp1.
- CoREST is bound to the hsp70 gene promoter under basal conditions and that its binding increases during heat shock response.
- Insight into the mechanism that regulates HSF1 turnover, and identifies the degradation of HSF1 as a target for therapeutics intervention
- Endotoxin tolerance and HS appear to share a common immune suppressive effect, possibly through HSF-1-mediated competitive inhibition of NF-kappaB nuclear binding.
- Hsf1 is required for p53 nuclear importation and activation, which implies that heat shock factors play a role in the regulation of p53.
- demonstrated dynamic age-dependent changes in the regulation but not the amount of HSF1
- results provide a mechanistic basis for the requirement of HSF1 in the regulation of life span and establish a role for SIRT1 in protein homeostasis and the heat shock response