epitope mapping within an internal region of HSF4b of human origin
recommended for detection of HSF4b of mouse, rat and human origin by WB, IF and ELISA; also reactive with additional species, including equine, canine, bovine and porcine
blocking peptide, sc-19863 P
TransCruz reagent for Gel Supershift and ChIP applications, sc-19863 X, 200 µg/0.1 ml
HSF4b Background Information Prokaryotic and eukaryotic cells respond to thermal and chemical stress by inducing a group of genes collectively designated heat shock genes. In eukar-yotes, this gene expression is regulated primarily at the transcription level. Heat shock transcription factors (HSF, also designated HSF) 1 and 2 are involved in this regulation. HSF1 and HSF2 are upregulated by estrogen, at both the mRNA and protein level. HSF1 transcriptional activity is repressed by constitutive phosphorylation and it is typically found in monomeric form. Upon activation, HSF1 forms trimers, gains DNA binding activity and is trans-located to the nucleus. HSF2 activity is associated with differentiation and development. Like HSF1, HSF2 binds DNA as a trimer. HSF4 exists as two splice variants and is expressed in heart, brain and skeletal muscle as a homotrimer. HSF4a does not contain a DNA-binding domain and inhibits the formation of HSF1 nuclear bodies, thus repressing HSF1 mediated transcription. HSF4b does contain a DNA-binding domain and colocalizes with HSF1 nuclear bodies after heat shock.
