Analytical Data
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Gene name
ssbF
- Application
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Alternative Names
Helix-destabilizing protein
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Species
Escherichia coli
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P18310
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Expression Region
2-179aa
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Molecular Weight
35.5 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
The research on the SsbF recombinant protein is primarily driven by its critical role in the biogenesis and stability of various cellular proteins within bacteria. SsbF, a member of the SSB (Single-Stranded DNA Binding) protein family, is essential for maintaining the integrity of single-stranded DNA during processes such as DNA replication, repair, and recombination. Its function is particularly vital in organisms exposed to stressful conditions that can lead to DNA damage. Studies have indicated that SsbF not only protects DNA but also assists in the proper folding of newly synthesized proteins, linking DNA metabolism with protein homeostasis. Understanding the structure and function of SsbF can reveal insights into the molecular mechanisms of bacterial resilience and adaptation, with potential implications for antibiotic development and biotechnology applications. By employing recombinant DNA technology, researchers can produce SsbF in vitro, facilitating extensive biochemical and structural analyses that enhance our understanding of its mechanisms of action. This knowledge may pave the way for novel strategies to manipulate bacterial genetic processes or improve protein production systems in industrial applications. Moreover, exploring the evolutionary conservation of SsbF across different species can provide broader insights into the fundamental aspects of DNA-protein interactions, further underscoring its significance in microbiology and molecular biology research.
