Hsf1 (human, recombinant)

Heat Shock Factor 1|Heat Shock Transcription Factor 1|HSTF1

Heat-shock factor 1 (Hsf1) is a transcription factor involved in the heat-shock response.{51550} It is composed of an N-terminal DNA-binding domain, a hydrophobic repeat region (HR-A/B), which mediates oligomerization required for DNA binding, a D domain, a regulatory domain, a repeat region (HR-C), which prevents oligomerization by binding to HR-A/B in its inactive form, and a C-terminal transactivation domain.{51549,51550,51548} When inactive, Hsf1 is monomeric and bound to heat shock proteins (HSPs) but, upon induction of the heat-shock response, it forms homotrimers, is translocated to the nucleus, and binds to heat-shock elements (HSEs) in the promotor region of target genes, such as HSPs.{51550} Hsf1 is ubiquitously expressed and activated by heat shock, as well as a variety of other factors, including inflammation, ischemia, infection, and aging.{51547,51550} It is involved in transactivation of genes involved in these processes, as well as genes involved in development, metabolism, and carcinogenesis.{51547} Hsf1 is constitutively active in certain cancers and its deficiency in rodent models is associated with a reduction in tumor formation.{51547,51548} Protein levels of Hsf1 are increased in breast cancer tumors and this overexpression, as well as nuclear localization of Hsf1, is associated with reduced survival.{51548} Cayman’s Hsf1 (human, recombinant) protein was synthesized from a DNA sequence encoding the mature form of species protein (Asp2-Ser529) with an N-terminal translation-initiating methionine (Met1). The expressed protein consists of 539 amino acids, has a calculated molecular weight of 58.6 kDa, and a predicted N-terminus of Met1. By SDS-PAGE, under reducing conditions, the apparent molecular mass of the protein is approximately 67 kDa potentially due to post-translational modifications or other experimental conditions.

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-80

Lyophilized from sterile PBS, pH 7.0

365

≥70% estimated by SDS-PAGE