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HSF1 Sumoylation Site Antibody 精选
Purified Rabbit Polyclonal Antibody (Pab)
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- 实验流程
- 背景知识
Application 
| IF, WB, E |
|---|---|
| Primary Accession | Q00613 |
| Other Accession | Q08DJ8 |
| Reactivity | Human, Mouse |
| Predicted | Bovine, Rat, Canine, Rabbit |
| Host | Rabbit |
| Clonality | Polyclonal |
| Isotype | Rabbit IgG |
| Calculated MW | 57260 Da |
| Antigen Region | 278-309 aa |
| Gene ID | 3297 |
|---|---|
| Other Names | Heat shock factor protein 1, HSF 1, Heat shock transcription factor 1, HSTF 1, HSF1, HSTF1 |
| Target/Specificity | This HSF1 Sumoylation Site antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 278-309 amino acids from human HSF1 Sumoylation Site. |
| Dilution | IF~~1:10~50 WB~~1:1000 E~~Use at an assay dependent concentration. |
| Format | Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS. |
| Storage | Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
| Precautions | HSF1 Sumoylation Site Antibody is for research use only and not for use in diagnostic or therapeutic procedures. |
For Research Use Only. Not For Use In Diagnostic Procedures.
| 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 insult damage (PubMed:11447121, PubMed:12659875, PubMed:12917326, PubMed:15016915, PubMed:18451878, PubMed:1871105, PubMed:1986252, PubMed:25963659, PubMed:26754925, PubMed:7623826, PubMed:7760831, PubMed:8940068, PubMed:8946918, PubMed:9121459, PubMed:9341107, PubMed:9499401, PubMed:9535852, PubMed:9727490). In unstressed cells, is present in a HSP90-containing multichaperone complex that maintains it in a non-DNA-binding inactivated monomeric form (PubMed:11583998, PubMed:16278218, PubMed:9727490). 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:10359787, PubMed:11583998, PubMed:12659875, PubMed:16278218, PubMed:1871105, PubMed:1986252, PubMed:25963659, PubMed:26754925, PubMed:7623826, PubMed:7935471, PubMed:8455624, PubMed:8940068, PubMed:9499401, PubMed:9727490). 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:26159920, PubMed:8455624). Predominantly nuclear protein in both unstressed and heat shocked cells (PubMed:10359787, PubMed:10413683). 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:26159920, PubMed:8455624). Localizes in subnuclear granules called nuclear stress bodies (nSBs) upon heat shock (PubMed:10359787, PubMed:10747973, PubMed:11447121, PubMed:11514557, PubMed:19229036, PubMed:24581496, PubMed:25963659). Colocalizes with SYMPK and SUMO1 in nSBs upon heat shock (PubMed:10359787, PubMed:11447121, PubMed:11514557, PubMed:12665592, PubMed:14707147) 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
Application Protocols
Provided below are standard protocols that you may find useful for product applications.
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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Discontinued
Cat# AP2501a
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100 µl
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