Anti-HSF1 Antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application
| WB, IHC-P, IHC-F, ICC |
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Primary Accession | Q00613 |
Host | Rabbit |
Reactivity | Human, Mouse, Rat |
Clonality | Polyclonal |
Format | Lyophilized |
Description | Rabbit IgG polyclonal antibody for Heat shock factor protein 1(HSF1) detection. Tested with WB, IHC-P, IHC-F, ICC in Human;Mouse;Rat. |
Reconstitution | Add 0.2ml of distilled water will yield a concentration of 500ug/ml. |
Gene ID | 3297 |
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Other Names | Heat shock factor protein 1, HSF 1, Heat shock transcription factor 1, HSTF 1, HSF1, HSTF1 |
Calculated MW | 57260 MW KDa |
Application Details | Immunocytochemistry , 0.5-1 µg/ml, Human, Mouse, Rat Immunohistochemistry(Frozen Section), 0.5-1 µg/ml, Rat, Human, Mouse Immunohistochemistry(Paraffin-embedded Section), 0.5-1 µg/ml, Human, Mouse, Rat, By Heat Western blot, 0.1-0.5 µg/ml, Human, Rat, Mouse |
Subcellular Localization | Cytoplasm. Nucleus. Cytoplasmic during normal growth. On activation, translocates to nuclear stress granules. Colocalizes with SUMO1 in nuclear stress granules. |
Protein Name | Heat shock factor protein 1(HSF 1) |
Contents | Each vial contains 5mg BSA, 0.9mg NaCl, 0.2mg Na2HPO4, 0.05mg Thimerosal, 0.05mg NaN3. |
Immunogen | A synthetic peptide corresponding to a sequence in the middle region of human HSF1(380-397aa DKNELSDHLDAMDSNLDN), identical to the related rat and mouse sequences. |
Purification | Immunogen affinity purified. |
Cross Reactivity | No cross reactivity with other proteins |
Storage | At -20˚C for one year. After r˚Constitution, at 4˚C for one month. It˚Can also be aliquotted and stored frozen at -20˚C for a longer time.Avoid repeated freezing and thawing. |
Name | HSF1 (HGNC:5224) |
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Synonyms | HSTF1 |
Function | 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 insult 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 recovery phase period of the HSR, returns to its unactivated form (PubMed:11583998, PubMed:16278218). Binds to inverted 5'-NGAAN-3' pentamer DNA sequences (PubMed:1986252, PubMed:26727489). Binds to chromatin at heat shock gene promoters (PubMed:25963659). Activates transcription of transcription factor FOXR1 which in turn activates transcription of the heat shock chaperones HSPA1A and HSPA6 and the antioxidant NADPH-dependent reductase DHRS2 (PubMed:34723967). Also serves several other functions independently of its transcriptional activity. Involved in the repression of Ras-induced transcriptional activation of the c-fos gene in heat-stressed cells (PubMed:9341107). Positively regulates pre-mRNA 3'-end processing and polyadenylation of HSP70 mRNA upon heat-stressed cells in a symplekin (SYMPK)-dependent manner (PubMed:14707147). Plays a role in nuclear export of stress- induced HSP70 mRNA (PubMed:17897941). Plays a role in the regulation of mitotic progression (PubMed:18794143). Also plays a role as a negative regulator of non-homologous end joining (NHEJ) repair activity in a DNA damage-dependent manner (PubMed:26359349). Involved in stress-induced cancer cell proliferation in a IER5-dependent manner (PubMed:26754925). |
Cellular Location | Nucleus. Cytoplasm. Nucleus, nucleoplasm. Cytoplasm, perinuclear region. Cytoplasm, cytoskeleton, spindle pole. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome Chromosome, centromere, kinetochore Note=The monomeric form is cytoplasmic in unstressed cells (PubMed:8455624, PubMed:26159920). Predominantly nuclear protein in both unstressed and heat shocked cells (PubMed:10413683, PubMed:10359787). Translocates in the nucleus upon heat shock (PubMed:8455624). Nucleocytoplasmic shuttling protein (PubMed:26159920). Colocalizes with IER5 in the nucleus (PubMed:27354066). Colocalizes with BAG3 to the nucleus upon heat stress (PubMed:8455624, PubMed:26159920). Localizes in subnuclear granules called nuclear stress bodies (nSBs) upon heat shock (PubMed:11447121, PubMed:11514557, PubMed:10359787, PubMed:25963659, PubMed:10747973, PubMed:24581496, PubMed:19229036). Colocalizes with SYMPK and SUMO1 in nSBs upon heat shock (PubMed:11447121, PubMed:12665592, PubMed:11514557, PubMed:14707147, PubMed:10359787) Colocalizes with PRKACA/PKA in the nucleus and nSBs upon heat shock (PubMed:21085490). Relocalizes from the nucleus to the cytoplasm during the attenuation and recovery phase period of the heat shock response (PubMed:26159920). Translocates in the cytoplasm in a YWHAE- and XPO1/CRM1-dependent manner (PubMed:12917326). Together with histone H2AX, redistributed in discrete nuclear DNA damage-induced foci after ionizing radiation (IR) (PubMed:26359349). Colocalizes with calcium- responsive transactivator SS18L1 at kinetochore region on the mitotic chromosomes (PubMed:18794143). Colocalizes with gamma tubulin at centrosome (PubMed:18794143). Localizes at spindle pole in metaphase (PubMed:18794143). Colocalizes with PLK1 at spindle poles during prometaphase (PubMed:18794143). |
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Background
HSF1(HEAT-SHOCK TRANSCRIPTION FACTOR 1), also called HEAT-SHOCK FACTOR 1, is a protein that in humans is encoded by the HSF1 gene. The product of HSF1 gene is a heat-shock transcription factor. The International Radiation Hybrid Mapping Consortium maps the HSF1 gene to chromosome 8. HSF1 exists as an inactive monomer in a complex with Hsp40/Hsp70 and Hsp90. Upon stress, such as elevated temperature, HSF1 is released from the chaperone complex and trimerizes. HSF1 is then transported into the nucleus where it is hyperphosphorylated and binds to DNA containing heat shock elements. HSF1's target genes include major inducible heat shock proteins such as Hsp72, and interestingly, noncoding RNA within Satellite III repeat regions. In a novel in vitro system human HSF1 can be activated by nonnative protein, heat, and geldanamycin. HSR1 is constitutively expressed in human and rodent cells and its homologs are functionally interchangeable. Furthermore, Hsf1-deficient mice had a longer free-running period than wildtype littermates.
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