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Thermo Fisher Scientific Phospho-HSF1 (Ser307) Polyclonal Antibody
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Thermo Fisher Scientific Phospho-HSF1 (Ser307) Polyclonal Antibody

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Rabbit polyclonal antibody recognizing phosphorylated HSF1 (Ser307). Validated for WB and ICC/IF applications. Supplied as unconjugated liquid at 1 mg/mL concentration. Recommended positive controls: HUVEC (WB) and HeLa (ICC/IF). For research use only.

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마지막 업데이트 2025. 08. 04. 오후 01:59
Thermo Fisher Scientific PA537599 Phospho-HSF1 (Ser307) Polyclonal Antibody 100 ul pk판매 단위 pk ·
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Thermo Fisher Scientific · Thermo Fisher Scientific Phospho-HSF1 (Ser307) Polyclonal Antibody

Thermo Fisher Scientific Phospho-HSF1 (Ser307) Polyclonal Antibody

Applications and Tested Dilution

Application Tested Dilution
Western Blot (WB) 1:500–1:1,000
Immunocytochemistry (ICC/IF) 1:100–1:200

Product Specifications

Property Description
Host / Isotype Rabbit / IgG
Class Polyclonal
Type Antibody
Immunogen Peptide sequence around phosphorylation site of serine 307 (P-Q-S(p)-P-R) derived from Human HSF1
Conjugate Unconjugated
Form Liquid
Concentration 1 mg/mL
Storage Conditions -20°C
Shipping Conditions Wet ice
RRID AB_2554207

Product Specific Information

  • Suggested positive control for Western blot: HUVEC cells
  • Suggested positive control for ICC/IF: HeLa cells

Target Information

All organisms respond to elevated temperatures and environmental stresses by rapid synthesis of heat shock RNAs and proteins. The regulation of heat shock gene transcription is mediated by heat shock factor (HSF), which binds to heat shock response elements (HSEs)—three repeats of a 5-nucleotide {nGAAn} module arranged in alternating orientation upstream of all heat shock genes.

These HSEs are highly conserved among species, yet HSF proteins from yeast, Drosophila, and human differ in molecular weight and do not show significant immunological cross-reactivity.
Humans have two HSFs, HSF1 and HSF2, sharing 38% sequence identity and binding the same HSEs.

  • HSF1 responds to classical stress signals (heat, heavy metals, oxidative stress).
  • HSF2 is activated during hemin-mediated differentiation of human erythroleukemia cells.

HSF1 exists as a cytoplasmic and nuclear monomer in unstressed cells, lacking DNA-binding activity. Under stress, HSF1 becomes a nuclear-localized trimer that binds DNA, and its phosphorylation is essential for maximal transcription of heat shock genes.

Usage Note

For Research Use Only. Not for use in diagnostic procedures or resale without express authorization.

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