Analytical Data
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Gene name
fis
- Application
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Species
Salmonella typhi
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Source
Yeast
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Tag
C- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P0A6R7
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Expression Region
1-98aa
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Molecular Weight
12.7 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
The study of FIS (Factor for Inversion Stimulation) recombinant proteins has gained significant attention in molecular biology and genetic research due to their essential role in the regulation of genomic architecture and function. FIS is a key DNA-binding protein found in bacteria, particularly Escherichia coli, which plays a critical role in the transcriptional regulation of various genes, particularly those involved in the cellular response to environmental changes. By promoting DNA bending and facilitating interactions between distant regulatory elements, FIS influences the accessibility of DNA to the transcription machinery. This makes it an important factor in processes such as DNA replication, recombination, and the formation of higher-order DNA structures. Understanding the molecular mechanisms underlying FIS function not only sheds light on bacterial adaptability and survival but also has broader implications for biotechnology and synthetic biology. The ability to produce FIS as a recombinant protein allows researchers to conduct detailed structural and functional analyses, paving the way for novel therapeutic strategies and the development of engineered organisms with tailored genetic circuits. As a result, ongoing research into FIS and its recombinant forms continues to reveal insights into cellular regulation and the complexities of genetic control mechanisms, making it a vital area of investigation in the fields of microbiology and genetic engineering.
