Analytical Data
-
Gene name
RNASEK
- Application
-
Alternative Names
RNase K (RNase kappa)
-
Species
Human
-
Source
E. coli
-
Tag
N- His
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q6P5S7
-
Expression Region
1-137aa
-
Molecular Weight
21.5 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
RNASEK, or Ribonuclease K, is a member of the ribonuclease family that has garnered attention due to its potential therapeutic applications and its role in various biological processes. The enzyme is involved in the degradation of RNA, an essential process for cellular regulation and maintenance. Its unique properties, including a high affinity for RNA and the ability to exhibit antimicrobial activity, make RNASEK a compelling subject of research in both basic and applied sciences. Studies have indicated that RNASEK may play a crucial role in modulating immune responses and reducing inflammation, which paves the way for its exploration in treating diseases such as cancer and viral infections. Additionally, the recombinant production of RNASEK allows for detailed investigations into its structure-function relationships, enzymatic mechanisms, and interactions with nucleic acids. This recombinant approach provides a platform for exploring the enzyme’s stability, specificity, and potential as a therapeutic agent. As researchers continue to uncover the regulatory functions of RNASEK in cellular contexts, its implications in biotechnology and medicine become increasingly significant, highlighting the importance of understanding this protein in both fundamental and applied research. The ongoing exploration of RNASEK not only deepens our understanding of ribonuclease enzymes but also opens new avenues for innovative treatments in various diseases, establishing RNASEK as a valuable target for future research and development.
