Anti-HSF2 Antibody

DNA-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. HSF2 is expressed in a form that binds DNA constitutively but loses DNA binding by incubation at greater than 41 degrees C.

Immunoblotting: use at 1-5ug/mL. A band of ~69 kDa is detected.Immunohistochemistry / Immuno- fluorescence: use at 1-5 ug/mL. <br><br>Immunoprecipitation: use 1-2ug per 100- 500ug total protein. <br><br>These are recommended concentrations. User should determine optimal concentrations for their application. <br><br>Positive control: Heat-shocked HeLa cell lysate, K562 cell nuclear extract, human pancreatic tumor cells.

This antibody recognizes HSF2 in heat- shocked cell lysates of human, mouse, rat, rabbit, bovine, canine, porcine, guinea pig, hamster, sheep, and monkey.

Heat shock factor 1 (HSF1) is a heat shock transcription factor that activates the transcription of genes encoding products required for protein folding, processing, targeting, degradation, and function. Up- regulation of expression of heat shock proteins in response to stress occurs at the level of transcription through a heat shock element and a HSF transcription factor. Amino acid sequences for most HSFs are highly conserved. A DNA binding domain is at the N-terminus, hydrophobic repeats (essential to the formation of active trimers) are adjacent to this binding domain, and another short hydrophobic repeat (necessary for suppression of trimerization) occurs toward the C-terminus. HSF2 exists as two isoforms, the alpha form being more transcriptionally active than the smaller beta form. Various experiments have suggested that HSF2 may play roles in differentiation and development.