Analytical Data
-
Gene name
sso7d
- Application
-
Alternative Names
sso7d;sso7d-1;DNA-binding Protein 7d
-
Species
E.coli
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P39476
-
Expression Region
2-64aa
-
AA Sequence
ATVKFKYKGEEKEVDISKIKKVWRVGKMISFTYDEGGGKTGRGAVSEKDAPKELLQMLEKQKK
-
Molecular Weight
9.1 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 Sso7d, a small, thermostable protein derived from the archaeon Sulfolobus solfataricus, has garnered significant interest in the fields of molecular biology and biochemistry due to its unique structural and functional properties. This protein, which consists of only 70 amino acids, exhibits remarkable thermal stability, allowing it to retain its functional integrity even at elevated temperatures. Sso7d's compact structure and robust nature make it an excellent model for exploring protein folding dynamics and stability mechanisms. Furthermore, Sso7d has been shown to possess DNA-binding capabilities, raising its potential application in biotechnology, particularly in the fields of gene editing and molecular diagnostics. As researchers investigate the molecular basis of its interaction with DNA, Sso7d promises to enhance our understanding of protein-DNA recognition processes and contribute to the development of innovative tools for genetic manipulation. Additionally, its simple structure allows for the engineering of variants with tailored functionalities, thus opening avenues for its utilization in therapeutic and industrial applications. Overall, Sso7d represents a fascinating subject of study, bridging basic research in protein science with practical applications in biotechnology.











