
Thermo Fisher Scientific Phospho-HSF1 (Ser326) Polyclonal Antibody
HSF1의 Ser326 인산화 형태를 특이적으로 인식하는 rabbit polyclonal antibody. Western blot, IHC, ICC 등 다양한 응용 가능. 인간 및 랫트 시료 반응성. PBS/glycerol buffer에 보관, -20°C에서 안정적 저장.
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Applications and Tested Dilutions
| Application | Tested Dilution |
|---|---|
| Western Blot (WB) | 1:1,000–1:3,000 |
| Immunohistochemistry (Paraffin) (IHC-P) | 1:50–1:200 |
| Immunocytochemistry (ICC/IF) | Assay-dependent |
Product Specifications
| 항목 | 내용 |
|---|---|
| Species Reactivity | Human, Rat |
| Host / Isotype | Rabbit / IgG |
| Class | Polyclonal |
| Type | Antibody |
| Immunogen | A synthesized peptide derived from human HSF1 (Accession Q00613), corresponding to amino acid residues around phosphorylated Ser326. |
| Conjugate | Unconjugated |
| Form | Liquid |
| Concentration | 1 mg/mL |
| Purification | Sequential chromatography |
| Storage Buffer | PBS, pH 7.4, with 50% glycerol |
| Contains | 0.02% sodium azide |
| Storage Conditions | -20°C |
| Shipping Conditions | Wet ice |
| RRID | AB_2815852 |
Product Specific Information
This antibody detects endogenous levels of HSF1 only when phosphorylated at Ser326.
Target Information
All organisms respond to elevated temperatures and various environmental stresses by rapidly synthesizing heat shock RNAs and proteins. The regulation of heat shock gene transcription is mediated by the transcriptional activator, heat shock factor (HSF), which binds to heat shock response elements (HSEs).
HSEs consist of three repeats of a 5-nucleotide {nGAAn} module arranged in alternating orientation upstream of all heat shock genes. These sequences are highly conserved among species, yet HSF purified from yeast, Drosophila, and human differ in molecular weight and do not show significant immunological cross-reactivity.
Two HSFs have been identified in human cells: HSF1 and HSF2, sharing 38% sequence identity and binding to the same HSEs.
- HSF1 is activated by classical stress signals such as heat, heavy metals, and oxidative reagents.
- HSF2 is activated during hemin-mediated differentiation of human erythroleukemia cells.
HSF1 exists constitutively in the cytoplasm and nucleus of unstressed cells as a monomer lacking DNA-binding activity. Upon stress, HSF1 is converted to a nuclear-localized trimeric form that binds DNA. Phosphorylation of HSF1 is required for maximal transcription of heat shock genes.
For Research Use Only.
Not for use in diagnostic procedures.
Not for resale without express authorization.
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