Analytical Data
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Gene name
cspA
- Application
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Alternative Names
cspA;cspS;Cold shock Protein CspA
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Species
Human
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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
P0A9X9
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Expression Region
1-70aa
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AA Sequence
MSGKMTGIVKWFNADKGFGFITPDDGSKDVFVHFSAIQNDGYKSLDEGQKVSFTIESGAKGPAAGNVTSL
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Molecular Weight
7.4 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
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Protein Description
CspA, a cold shock protein found in *Escherichia coli*, plays a crucial role in bacterial adaptation to low-temperature environments by promoting mRNA stability and translation. Its ability to regulate gene expression in response to temperature fluctuations makes it a key target for research in bacterial physiology and stress responses. Given its significant role in cold shock responses, CspA has attracted attention for applications in biotechnology and synthetic biology, where enhancing microbial survival and productivity under varying temperature conditions is paramount. The recombinant production of CspA allows for detailed biochemical characterization and functional studies, enabling researchers to elucidate its mechanisms of action, interactions with nucleic acids, and potential applications in industrial processes. Moreover, understanding CspA's structure-function relationships can provide insights into the evolutionary adaptations of bacteria in extreme environments. As microbial applications in biotechnology increase, the importance of proteins like CspA in enhancing stress resilience is becoming clearer, highlighting the necessity for further studies on its recombinant forms and functional properties. This research not only contributes to fundamental microbiological knowledge but also paves the way for innovative strategies in bioprocess optimization and development of cold-active biocatalysts.











