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HSF1 Sumoylation site Antibody Blocking Peptide

Synthetic peptide

     
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Product Information
Primary Accession Q00613
Clone Names 2110405
Additional Information
Gene ID 3297
Other Names Heat shock factor protein 1, HSF 1, Heat shock transcription factor 1, HSTF 1, HSF1, HSTF1
Target/Specificity The synthetic peptide sequence used to generate the antibody AP2501a is PLVRVKEEPPSPPQSPR, containing a predicted sumoylation site from the central region of human HSF1. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.
Format Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed.
StorageMaintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.
PrecautionsThis product is for research use only. Not for use in diagnostic or therapeutic procedures.
Protein Information
Name HSF1 (HGNC:5224)
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 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). 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). 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). Plays also 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). Plays also 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).
Research Areas
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Background

Heat shock transcription factor 1 (HSF1) mediates the induction of heat shock protein gene expression in cells exposed to elevated temperature and other stress conditions. In response to stress, HSF1 acquires DNA-binding ability and localizes to nuclear stress granules. SUMO modification of HSF1 converts HSF1 to the DNA-binding form. HSF1 colocalizes with SUMO-1 in nuclear stress granules, which is prevented by mutation of the HSF1 lysine targeted for sumoylation.

References

Hilgarth, et al., Biochem Biophys Res Commun. 2003 Mar 28;303(1):196-200.He, H., et al., J. Biol. Chem. 278(37):35465-35475 (2003).Wang, X., et al., Mol. Cell. Biol. 23(17):6013-6026 (2003).Ignatenko, N.A., et al., Exp. Cell Res. 288(1):1-8 (2003).Soncin, F., et al., Biochem. Biophys. Res. Commun. 303(2):700-706 (2003).

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$ 277.78
Cat# BP2501a
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