Analytical Data
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Gene name
ssbF
- Application
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Alternative Names
ssbF；ssb；ssf；Plasmid-derived single-stranded DNA-binding Protein
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Species
E.coli
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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
P18310
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Expression Region
2-179aa
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AA Sequence
AVRGINKVILVGRLGKDPEVRYIPNGGAVANLQVATSESWRDKQTGEMREQTEWHRVVLFGKLAEVAGECLRKGAQVYIEGQLRTRSWEDNGITRYVTEILVKTTGTMQMLVRAAGAQTQPEEGQQFSGQPQPEPQAEAGTKKGGAKTKGRGRKAAQPEPQPQPPEGDDYGFSDDIPF
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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
ssbF, or single-stranded binding protein F, plays a crucial role in DNA replication and repair processes in prokaryotic organisms. It is primarily involved in stabilizing single-stranded DNA intermediates during these processes, thereby preventing the formation of secondary structures that can impede replication and repair mechanisms. The interest in ssbF reconstituted proteins stems from its potential applications in biotechnology and synthetic biology, where engineered proteins can enhance DNA manipulation techniques. Understanding the structural dynamics and binding mechanisms of ssbF is essential for elucidating its function and interactions with other molecular partners during the cell cycle. Furthermore, research into ssbF can provide insights into the evolutionary variations of DNA-binding proteins, as it exhibits unique characteristics compared to its eukaryotic counterparts. Investigating the reconstitution of ssbF proteins not only contributes to our fundamental knowledge of molecular biology but also opens avenues for developing innovative tools for genetic engineering, therapeutic interventions, and even in the creation of biosensors. The study of ssbF is thus a vital component of ongoing research aimed at deciphering the complexities of nucleic acid metabolism and its applications in medical and technological fields.
