Analytical Data
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Gene name
hup1
- Application
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Alternative Names
HSl
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Species
Streptomyces lividans
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Source
E. coli
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Tag
N- GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P0A3H6
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Expression Region
1-93aa
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Molecular Weight
36.9 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
Hup1 is a protein that has garnered significant interest due to its involvement in various biological processes within microorganisms, particularly in response to environmental stresses. This protein, known for its role as a transcription factor, modulates gene expression in response to changes in nutrient availability and other external stimuli. Research into Hup1 has been motivated by its potential applications in biotechnology and medicine, including improving microbial fermentation processes and understanding stress responses in cells. Additionally, the study of Hup1 may provide insights into broader regulatory mechanisms in eukaryotic organisms. As researchers delve deeper into the structural and functional aspects of Hup1, there is growing interest in its recombinant forms, which can be produced using recombinant DNA technology. This has opened up new avenues for studying the protein's functions in more controlled environments, leading to potential innovations in genetic engineering and synthetic biology. The ongoing exploration of Hup1 and its recombinant counterparts holds promise for enhancing agricultural productivity, developing new therapeutic strategies, and understanding fundamental biological principles.
