Analytical Data
-
Gene name
cspA
- Application
-
Alternative Names
7.4 kDa cold shock protein CS7.4
-
Species
Salmonella enteritidis
-
Source
E. coli
-
Tag
N- His & C- Myc
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P0A9Y5
-
Expression Region
2-70aa
-
Molecular Weight
14.7 kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
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.
-
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.
-
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 the cspA gene, which encodes a cold shock protein in bacteria, has garnered significant attention due to its essential role in stress response mechanisms and its potential applications in biotechnology. cspA is known to be rapidly induced upon temperature downshift, facilitating the adaptation of bacteria to cold environments by stabilizing mRNA and preventing its degradation, thereby enhancing protein synthesis during stress. This gene has been particularly studied in *Escherichia coli*, where its expression is tightly regulated and contributes to the organism's survival under low-temperature conditions. Understanding the structure and function of cspA and its recombinant protein can provide insights into its mechanism of action and its interactions with other cellular components. Additionally, cspA's ability to function as a chaperone suggests its usefulness in the industrial production of protein therapeutics, where it could help to improve yield and solubility of target proteins. Furthermore, the manipulation of cspA expression in microbial hosts could lead to enhanced resilience in bioprocesses, thereby making it a valuable target for genetic engineering efforts aimed at improving microbial performance under various environmental stresses.
