Analytical Data
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Gene name
HSF2
- Application
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Alternative Names
HSF2；HSTF2；Heat shock factor Protein 2
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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
Q03933
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Expression Region
411-536aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMSENKGLETTKNNVVQPVSEEGRKSKSKPD KQLIQYTAFPLLAFLDGNPASSVEQASTTASSEVLSSVDKPIEVDELLDS SLDPEPTQSKLVRLEPLTEA EASEATLFYLCELAPAPLDSDMPLLDS
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Molecular Weight
16 kDa
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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
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Protein Description
HSF2, or Heat Shock Factor 2, is a crucial regulatory protein that plays a significant role in cellular responses to stress, particularly in the context of heat shock and other stressors. Research on HSF2 has gained prominence due to its involvement in the regulation of heat shock protein (HSP) genes, which are essential for protein folding, protection from aggregation, and recovery from cellular stress. Unlike its well-studied counterpart HSF1, which has been extensively characterized in various stress responses, HSF2's specific contributions to cellular adaptation and development remain less understood. Investigating the recombinant protein production of HSF2 is vital to elucidate its functional mechanisms, post-translational modifications, and interactions with other cellular factors. Additionally, insights gleaned from HSF2 studies may have significant implications for understanding stress-related diseases, aging, and neurodegenerative conditions. As researchers harness recombinant DNA technology to produce HSF2 in model organisms or expression systems, such as bacteria or yeast, this work opens avenues for high-throughput screening and drug development targeting the heat shock response. Overall, the study of HSF2 and its recombinant protein forms enhances our understanding of the molecular underpinnings of stress responses and their physiological relevance in health and disease.
