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Wählen Sie konfigurierbare Panels & Premixed-Kits - ODER - Kits für die zelluläre Signaltransduktion & MAPmates™
Konfigurieren Sie Ihre MILLIPLEX® MAP-Kits und lassen sich den Preis anzeigen.
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Unser breites Angebot enthält Multiplex-Panels, für die Sie die Analyten auswählen können, die am besten für Ihre Anwendung geeignet sind. Unter einem separaten Register können Sie das Premixed-Cytokin-Format oder ein Singleplex-Kit wählen.
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Wählen Sie gebrauchsfertige Kits zur Erforschung gesamter Signalwege oder Prozesse. Oder konfigurieren Sie Ihre eigenen Kits mit Singleplex MAPmates™.
Die folgenden MAPmates™ sollten nicht zusammen analysiert werden: -MAPmates™, die einen unterschiedlichen Assaypuffer erfordern. -Phosphospezifische und MAPmate™ Gesamtkombinationen wie Gesamt-GSK3β und Gesamt-GSK3β (Ser 9). -PanTyr und locusspezifische MAPmates™, z.B. Phospho-EGF-Rezeptor und Phospho-STAT1 (Tyr701). -Mehr als 1 Phospho-MAPmate™ für ein einziges Target (Akt, STAT3). -GAPDH und β-Tubulin können nicht mit Kits oder MAPmates™, die panTyr enthalten, analysiert werden.
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Gewähltes Kit
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96-Well Plate
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48-602MAG
Buffer Detection Kit for Magnetic Beads
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ABE1044
Sigma-AldrichAnti-HSF 1 Antibody
Anti-HSF 1 antibody is an antibody against HSF 1 for use in western blotting, IP & ChIP.
More>>Anti-HSF 1 antibody is an antibody against HSF 1 for use in western blotting, IP & ChIP. Less<<
Anti-HSF 1 Antibody: SDB (Sicherheitsdatenblätter), Analysenzertifikate und Qualitätszertifikate, Dossiers, Broschüren und andere verfügbare Dokumente.
HSF1, also known as Heat shock factor protein 1 (HSF-1) or Heat shock transcription factor 1 (HSTF-1), and encoded by the gene HSF1/HSTF1, is a DNA binding transcription factor that binds heat shock promoter elements (HSE’s) and activates transcription. In higher eukaryotes, HSF1 is unable to bind to HSE regions unless the cells are heat shocked. HSF1 is normally a monomer that interacts with HSP90 and other chaperones in a large complex in the cytoplasm. Upon heat shock HSF1 is released from the complex, dimerizes, and is transported into the nucleus. HSF1 is localized to the cytoplasm during normal growth the protein localizes to the nucleus upon heat shock. HSF1 is part of the cellular stress response, and HSF1 is known to interact with many other stress- induced proteins including NCOA6, SYMPK, RALBP1, HSF2, CEBPB, HSPA1A, Heat shock protein 90kDa alpha and HSPA.
Anti-HSF 1 antibody is an antibody against HSF 1 for use in western blotting, IP & ChIP.
Key Applications
Western Blotting
Immunoprecipitation
Chromatin Immunoprecipitation (ChIP)
Application Notes
Immunoprecipitation Analysis: A representative lot from an independent laboratory immunoprecipitated HSF 1 from HEK293 cell lysates transfected with wild type or mutant hRP1-HA (Fujimoto, M., et al. (2012). Mol Cell. 48(2):182-194.).
Immunoprecipitation Analysis: A representative lot from an independent laboratory immunoprecipitated HSF 1 from hHSF1 transfected MEF cell lysate (Fujimoto, M., et al. (2010). Mol Cell Biol. 21(1):106-116.).
Chromatin Immunoprecipitation Analysis: A representative lot from an independent laboratory immunoprecipitated HSF 1 from wild type and HSF2-null primary MEF cell lysates (Shinkawa, T., et al. (2011). Mol Cell Biol. 22(19):3571-3583.).
Chromatin Immunoprecipitation Analysis: A representative lot from an independent laboratory immunoprecipitated HSF 1 from HeLa and MEF cell lysates which were either untreated or heat shock treated (Prof. A. Nakai, Yamaguchi University School of Medicine).
~75 kDa observed. Uncharacterized band(s) may be observed in some cell lysates.
Physicochemical Information
Dimensions
Materials Information
Toxicological Information
Safety Information according to GHS
Safety Information
Product Usage Statements
Quality Assurance
Evaluated by Western Blotting in HeLa cell lysate.
Western Blotting: A 1:1,000 dilution of this antibody detected HSF 1 in 10 µg of HeLa cell lysate.
Usage Statement
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
Storage and Shipping Information
Storage Conditions
Stable for 1 year at -20°C from date of receipt. Handling Recommendations: Upon receipt and prior to removing the cap, centrifuge the vial and gently mix the solution. Aliquot into microcentrifuge tubes and store at -20°C. Avoid repeated freeze/thaw cycles, which may damage IgG and affect product performance.
Transcription factor access to regulatory elements is prevented by the nucleosome. Heat shock factor 1 (HSF1) is a winged helix transcription factor that plays roles in control and stressed conditions by gaining access to target elements, but mechanisms of HSF1 access are not well known in mammalian cells. Here, we show the physical interaction between the wing motif of human HSF1 and replication protein A (RPA), which is involved in DNA metabolism. Depletion of RPA1 abolishes HSF1 access to the promoter of HSP70 in unstressed condition and delays its rapid activation in response to heat shock. The HSF1-RPA complex leads to preloading of RNA polymerase II and opens the chromatin structure by recruiting a histone chaperone, FACT. Furthermore, this interaction is required for melanoma cell proliferation. These results provide a mechanism of constitutive HSF1 access to nucleosomal DNA, which is important for both basal and inducible gene expression.
Heat shock response is characterized by the induction of heat shock proteins (HSPs), which facilitate protein folding, and non-HSP proteins with diverse functions, including protein degradation, and is regulated by heat shock factors (HSFs). HSF1 is a master regulator of HSP expression during heat shock in mammals, as is HSF3 in avians. HSF2 plays roles in development of the brain and reproductive organs. However, the fundamental roles of HSF2 in vertebrate cells have not been identified. Here we find that vertebrate HSF2 is activated during heat shock in the physiological range. HSF2 deficiency reduces threshold for chicken HSF3 or mouse HSF1 activation, resulting in increased HSP expression during mild heat shock. HSF2-null cells are more sensitive to sustained mild heat shock than wild-type cells, associated with the accumulation of ubiquitylated misfolded proteins. Furthermore, loss of HSF2 function increases the accumulation of aggregated polyglutamine protein and shortens the lifespan of R6/2 Huntington's disease mice, partly through αB-crystallin expression. These results identify HSF2 as a major regulator of proteostasis capacity against febrile-range thermal stress and suggest that HSF2 could be a promising therapeutic target for protein-misfolding diseases.
