Host: E. coli • AA: Met1; 2-529 (full length) • Tag: N-terminal His • MW: 58.6 kDa
Technical Support & Resources

Visit our FAQ

Contact Us

Toll Free Phone (USA and Canada Only): (888) 526-5351
Direct Phone: (734) 975-3888

Request Technical Support

Technical Support Request

To streamline the process attach the appropriate questionnaire to your inquiry.

Download IHC QuestionnaireDownload WB Questionnaire

View Our Privacy Statement for details on how we use and protect your data. In addition, this site is protected by hCaptcha and its Privacy Policy and Terms of Service apply.

Hsf1 (human, recombinant)

Item No. 40253

Technical Information
Synonyms
  • Heat Shock Factor 1
  • Heat Shock Transcription Factor 1
  • HSTF1
Purity
≥70% estimated by SDS-PAGE
Source
Recombinant human N-Terminal His-tagged Hsf1 expressed in E. coli
Amino Acids
2-529
MW
58.6 kDa
Lyophilized from sterile PBS, pH 7.0
UniProt Accession №
Q00613-1
Shipping & Storage Information
Storage
-80°C
Shipping
Dry ice in continental US; may vary elsewhere
Recommended Products

Certificates of Analysis & Batch Specific Data

Provide batch numbers separated by commas to download or request available product inserts, QC sheets, certificates of analysis, data packs, and GC-MS data.

    Add

    Cayman Chemical
    Visit Our Cancer Resource Center
    Find Tools & Resources to Study the Hallmarks of Cancer
    • Cancer cell signaling & regulation
    • Cancer metabolism
    • Tumor microenvironment
    EXPLORE NOW
    Product Description

    Heat-shock factor 1 (Hsf1) is a transcription factor involved in the heat-shock response.1 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.2,1,3 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.1 Hsf1 is ubiquitously expressed and activated by heat shock, as well as a variety of other factors, including inflammation, ischemia, infection, and aging.4,1 It is involved in transactivation of genes involved in these processes, as well as genes involved in development, metabolism, and carcinogenesis.4 Hsf1 is constitutively active in certain cancers and its deficiency in rodent models is associated with a reduction in tumor formation.4,3 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.3 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.

    WARNING This product is not for human or veterinary use.

    References & Product Citations
    Product Description References

    1. Ramos, C.H.I., and Quel, N.G. Heat Shock Factor (HSF): The promoter of chaperone genes. A mini review. Curr. Proteomics 15(1), (2018).

    2. Vihervaara, A., and Sistonen, L. HSF1 at a glance. J. Cell Sci. 127(Pt 2), 261-266 (2014).

    3. Yan, P., Guzman, M.L., Peter, R.I., et alHSF1 and molecular chaperones in biology and cancer. (2020).

    4. Li, J., Labbadia, J., and Morimoto, R.I. Rethinking HSF1 in stress, development and organismal health. Trends Cell Biol. 27(12), 895-905 (2017).