Analytical Data
-
Gene name
SBSN
- Application
-
Species
Human
-
Source
E. coli
-
Tag
N-His
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q6UWP8
-
Expression Region
Gly434~Pro590
-
Molecular Weight
22kDa
-
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
SBSN (Skin-Binding Serum Protein) is a protein that has garnered interest in various fields of biological research, particularly due to its essential role in skin biology and its potential implications in drug delivery and tissue engineering. It is primarily expressed in the skin and is involved in processes such as cellular adhesion, wound healing, and skin barrier formation. Recent studies have highlighted the importance of SBSN in the maintenance of skin integrity and its involvement in pathological conditions like skin diseases and cancers. The ability to recombinantly express and purify SBSN has opened new avenues for research, enabling scientists to study its structural and functional properties in detail. This approach not only facilitates a better understanding of the protein's biological roles but also allows for the exploration of its applications in therapeutic contexts, where recombinant SBSN could be used to enhance healing or serve as a scaffold in regenerative medicine. Overall, the investigation into recombinant SBSN serves as a promising step toward harnessing this protein's potential in both fundamental research and practical biomedical applications.
