Anti-HSF1 (phospho S326) antibody (ab115702)


  • Product nameAnti-HSF1 (phospho S326) antibody
    See all HSF1 primary antibodies
  • Description
    Rabbit polyclonal to HSF1 (phospho S326)
  • Tested applicationsSuitable for: WBmore details
  • Species reactivity
    Reacts with: Human
  • Immunogen

    Synthetic peptide derived from Human HSF1 phosphorylated at Ser 326.

  • Positive control
    • HeLa cell lysate; HeLa cell lysate Heat-Shocked;



Our Abpromise guarantee covers the use of ab115702 in the following tested applications.

The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.

Application Abreviews Notes
WB 1/1000. Detects a band of approximately 85-95 kDa (predicted molecular weight: 57 kDa). (ECL).


  • FunctionDNA-binding protein that specifically binds heat shock promoter elements (HSE) and activates transcription. In higher eukaryotes, HSF is unable to bind to the HSE unless the cells are heat shocked.
  • Sequence similaritiesBelongs to the HSF family.
  • Domainthe 9aaTAD motif is a transactivation domain present in a large number of yeast and animal transcription factors.
  • Post-translational
    Phosphorylated on multiple serine residues, a subset of which are involved in stress-related regulation of transcription activation. Constitutive phosphorylation represses transcriptional activity at normal temperatures. Levels increase on specific residues heat-shock and enhance HSF1 transactivation activity. Phosphorylation on Ser-307 derepresses activation on heat-stress and in combination with Ser-303 phosphorylation appears to be involved in recovery after heat-stress. Phosphorylated on Ser-230 by CAMK2, in vitro. Cadmium also enhances phosphorylation at this site. Phosphorylation on Ser-303 is a prerequisite for HSF1 sumoylation. Phosphorylation on Ser-121 inhibits transactivation and promotes HSP90 binding. Phosphorylation on Thr-142 also mediates transcriptional activity induced by heat. Phosphorylation on Ser-326 plays an important role in heat activation of HSF1 transcriptional activity.
    Sumoylated with SUMO1 and SUMO2 on heat-shock. Heat-inducible sumoylation occurs after 15 min of heat-shock, after which levels decrease and at 4 hours, levels return to control levels. Sumoylation has no effect on HSE binding nor on transcriptional activity. Phosphorylation on Ser-303 is a prerequisite for sumoylation.
  • Cellular localizationCytoplasm. Nucleus. Cytoplasmic during normal growth. On activation, translocates to nuclear stress granules. Colocalizes with SUMO1 in nuclear stress granules.
  • Information by UniProt
  • Database links
  • Alternative names
    • Heat shock factor 1 antibody
    • Heat shock factor protein 1 antibody
    • Heat shock transcription factor 1 antibody
    • HSF 1 antibody
    • hsf1 antibody
    • HSF1_HUMAN antibody
    • HSTF 1 antibody
    • HSTF1 antibody
    see all

Anti-HSF1 (phospho S326) antibody images

  • All lanes : Anti-HSF1 (phospho S326) antibody (ab115702) at 1/1000 dilution

    Lane 1 : MW marker
    Lane 2 : HeLa cell lysate
    Lane 3 : HeLa cell lysate Heat-Shocked (No recovery time)

    Predicted band size : 57 kDa
  • All lanes : Anti-HSF1 (phospho S326) antibody (ab115702) at 1/1000 dilution

    Lane 1 : MW markers
    Lane 2 : Recombinant HSF1
    Lane 3 : Recombinant HSF1 (phospho)

    Predicted band size : 57 kDa

References for Anti-HSF1 (phospho S326) antibody (ab115702)

ab115702 has not yet been referenced specifically in any publications.

Product Wall

J’ai contacté le laboratoire pour savoir si l’un de nos anti- HSF1 (phospho S326) anticorps fonctionnerait chez la vache. Malheureusement, nous n’avons que trois anticorps : ab76076, ab1050 et ab115702 au catalogue et ils ont une homologie de 64%, 77% ...

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Merci de nous avoir contactés.
Nous sommes heureux d’avoir la possibilité de vous proposer un service par Epitomics, une société Abcam qui peut vous préparer des anticorps spécifiques.
Pour plus d'informations, visitez: http://www.epitomics.c...

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