Mouse HSF1 Antibody

HSF1 (Heat Shock Factor 1; also HSTF 1) is a 67-75 kDa member of the HSF family of proteins. It is constitutively expressed and functions as a transcriptional activator under heat shock conditions. Normally, it exists as an inactive, monomeric member of the HSP multichaperone complex. Following stress, it dissociates from the complex, homotrimerizes, undergoes multiple phosphorylations, and translocates to the nucleus. Nuclear HSF1 is SUMOylated on Lys298 and binds to heat shock elements in select genes such as HSP70. Mouse HSF1 is 525 amino acids (aa) in length. It contains a DNA binding domain (aa 15-120), two hydrophobic oligomerization regions (aa 130-203 and 380-405), a regulatory domain (aa 221-310), and a transactivation domain (aa 367-525). There are at least 13 potential Ser/Thr phosphorylation sites. When highly phosphorylated, HSF1 appears to run at about 82-85 kDa in SDS-PAGE; when SUMOylated, it runs anomalously at around 170 kDa in SDS-PAGE. One splice variant exists that shows a deletion of aa 413-434. Over aa 124-247, mouse HSF1 shares 94% and 99% aa identity with human and rat HSF1, respectively.