| Details | |
| Host / Isotype: | Rabbit |
| Class: | Polyclonal |
| Type: | Antibody |
| Species Reactivity: | Human (Hu) Murine (Ms) Rat (Rt) |
| Immunogen: | Recombinant human HSF1 expressed in E. coli. |
| Ordering Information | ||||
| Pierce Anti-Heat Shock Factor 1 Polyclonal Antibody | ||||
| Product Number | Pkg. Size | Price | Purchase | |
| PA3-017 | 100 µl | $298.00 | ||
| Storage: | -20º C, Avoid Freeze/Thaw Cycles |
| Form: | 100 µl of antiserum diluted in PBS containing 0.05% sodium azide. |
| Applications | Dilution |
| ELISA (ELISA) | Assay dependent |
| Gel Shift (GS) | Assay dependent |
| Immunoprecipitation (IP) | Assay dependent |
| Western Blot (WB) | 1:10,000 ( ECL) |
| Product Specific Information |
| PA3-017 detects heat shock factor 1 (HSF-1) from human, mouse and rat tissues and cells. PA3-017 has been successfully used in Western blot, immunoprecipitation, ELISA, and gel super shift protocols. By Western blot, this antibody detects an ~83 kDa protein representing HSF-1 from NIH-3T3 cell lysate. The PA3-017 immunogen is recombinant human HSF-1 protein expressed in E. coli. |
| General Information |
| All organisms respond to elevated temperatures and a variety of environmental stresses by rapid synthesis of 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). These HSEs are found as three repeats of a 5-nucleotide {nGAAn} module, arranged in alternating orientation and present upstream of all heat shock genes. The HSEs are highly conserved among species yet HSF purified from yeast, Drosophila and human have different molecular weights and the proteins do not show significant immunological cross reaction. Two HSFs have been identified in human cells, HSF1 and HSF2, which bind to the same HSEs and have 38% sequence identity. These factors are activated by distinct stimuli, HSF1 is responsive to classical stress signals such as heat, heavy metals and oxidative reagents, whereas HSF2 is activated during hemin-mediated differentiation of human erythroleukemia cells. HSF1 exists constitutively in the cytoplasm and the nucleus of unstressed cells as a monomer which lacks DNA binding activity. Through an unknown signal generated during stress, HSF1 becomes activated to a nuclear localized, trimeric state which binds to DNA. The phosphorylation of HSF1 is necessary for maximal transcription of heat shock genes. |
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