Analytical Data
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Gene name
HSF1
- Application
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Alternative Names
HSF1;HSTF1;Heat shock factor Protein 1
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q00613
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Expression Region
1-529aa
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AA Sequence
MDLPVGPGAAGPSNVPAFLTKLWTLVSDPDTDALICWSPSGNSFHVFDQG QFAKEVLPKYFKHNNMASFVRQLNMYGFRKVVHIEQGGLVKPERDDTEFQ HPCFLRGQEQLLENIKRKVTSVSTLKSEDIKIRQDSVTKLLTDVQLMKGK QECMDSKLLAMKHENEALWREVASLRQKHAQQQKVVNKLIQFLISLVQSN RILGVKRKIPLMLNDSGSAHSMPKYSRQFSLEHVHGSGPYSAPSPAYSSS SLYAPDAVASSGPIISDITELAPASPMASPGGSIDERPLSSSPLVRVKEE PPSPPQSPRVEEASPGRPSSVDTLLSPTALIDSILRESEPAPASVTALTD ARGHTDTEGRPPSPPPTSTPEKCLSVACLDKNELSDHLDAMDSNLDNLQT MLSSHGFSVDTSALLDLFSPSVTVPDMSLPDLDSSLASIQELLSPQEPPR PPEAENSSPDSGKQLVHYTAQPLFLLDPGS VDTGSNDLPVLFELGEGS YFSEGDGFAEDPTISLLTGSEPPKAKDPTVS
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
HSF1 (Heat Shock Factor 1) is a key regulator of the heat shock response, a fundamental cellular protective mechanism that is activated under conditions of thermal stress, oxidative stress, and other physiological challenges. This transcription factor plays a critical role in maintaining protein homeostasis by inducing the expression of heat shock proteins (HSPs), which assist in the proper folding, repair, and degradation of denatured proteins. Research on recombinant HSF1 has gained traction due to its potential implications in various fields, including cancer biology, neurodegeneration, and aging. Abnormal regulation of HSF1 has been linked to various diseases, making it a target for therapeutic intervention. The recombination of HSF1 allows for the study of its structure-function relationship, enabling scientists to explore how specific domains influence its transcriptional activity and interaction with other cellular proteins. Furthermore, recombinant HSF1 can be utilized in biotechnological applications, such as the production of HSPs in microbial systems, enhancing the yield of protein-based therapeutics. Understanding the precise mechanisms of HSF1 activation and its interactions with co-chaperones and other regulatory proteins is crucial for developing strategies to modulate its activity, providing a promising avenue for therapeutic development in stress-related diseases.
