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Invitrogen
Human HSF1 (aa 13-160) Control Fragment Recombinant Protein
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Product Details
RP-89449
Product Specifications
Species
Human
Expression System
E. coli
Amino acid sequence
SNVPAFLTKLWTLVSDPDTDALICWSPSGNSFHVFDQGQFAKEVLPKYFKHNNMASFVRQLNMYGFRKVVHIEQGGLVKPERDDTEFQHPCFLRGQEQLLENIKRKVTSVSTLKSEDIKIRQDSVTKLLTDVQLMKGKQECMDSKLLA
Tag
His-ABP-tag
Class
Recombinant
Type
Protein
Purity
>80% by SDS-PAGE and Coomassie blue staining
Conjugate
Form
Liquid
Concentration
≥5.0 mg/mL
Purification
purified
Storage buffer
1M urea/PBS, pH 7.4
Contains
no preservative
Storage conditions
-20°C, Avoid Freeze/Thaw Cycles
Shipping conditions
Wet ice
Product Specific Information
Highest antigen sequence indentity to the following orthologs: Mouse (99%), Rat (99%).
This recombinant protein control fragment may be used for blocking experiments. In IHC/ICC and WB experiments, we recommend a 100x molar excess of the protein fragment control based on the concentration and the molecular weight. Pre-incubate the antibody-protein control fragment mixture for 30 min at room temperature.
Target 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.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
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Bioinformatics
Protein Aliases: Heat shock factor protein 1; Heat shock transcription factor 1; HSF 1; HSF1; HSTF 1; unnamed protein product
Gene Aliases: HSF1; HSTF1
UniProt ID: (Human) Q00613
Entrez Gene ID: (Human) 3297
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