Analytical Data
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Gene name
HSFY1
- Application
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Alternative Names
HSFY1; Heat shock transcription factor 2-like protein; Heat shock transcription factor; HSF2 like; HSF2-like; HSF2L; HSFY; HSFY1_HUMAN; HSFY2; Y-linked
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q96LI6
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Expression Region
1-401aa
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AA Sequence
MAHVSSETQDVSPKDELTASEASTRSPLCEHTFPGDSDLRSMIEEHAFQVLSQGSLLESPSYTVCVSEPDKDDDFLSLNFPRKLWKIVESDQFKSISWDENGTCIVINEELFKKEILETKAPYRIFQTDAIKSFVRQLNLYGFSKIQQNFQRSAFLATFLSEEKESSVLSKLKFYYNPNFKRGYPQLLVRVKRRIGVKNASPISTLFNEDFNKKHFRAGANMENHNSALAAEASEESLFSASKNLNMPLTRESSVRQIIANSSVPIRSGFPPPSPSTSVGPSEQIATDQHAILNQLTTIHMHSHSTYMQARGHIVNFITTTTSQYHIISPLQNGYFGLTVEPSAVPTRYPLVSVNEAPYRNMLPAGNPWLQMPTIADRSAAPHSRLALQPSPLDKYHPNYN
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Molecular Weight
71.5 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
Related Products
Protein Description
HSFY1, or Heat Shock Factor Y1, plays a crucial role in the heat shock response of various organisms, particularly in the regulation of gene expression under stress conditions. Initially identified in plants, HSFY1 is significant for its ability to activate heat shock proteins (HSPs), which function as molecular chaperones to protect cells from damage due to elevated temperatures and other stressors. The study of HSFY1 has gained attention due to its potential applications in agricultural biotechnology; by enhancing the expression of this protein, researchers aim to improve stress resilience in crops, leading to better yield and survival under challenging environmental conditions. Understanding the structure and function of the HSFY1 recombinant protein is vital for unraveling its mechanisms of action and could pave the way for biotechnological advancements. Furthermore, exploring HSFY1 in various model organisms can shed light on conserved stress response pathways, emphasizing its evolutionary significance. As climate change intensifies and leads to more frequent extreme weather events, investigating HSFY1 and its associated pathways becomes increasingly relevant in the quest to develop crops that can withstand such adversities. In summary, research on HSFY1 recombinant protein is essential not only for advancing our fundamental understanding of stress biology but also for translating this knowledge into practical solutions for improving agricultural resilience in a changing environment.
