Analytical Data
-
Gene name
SHISA5
- Application
-
Alternative Names
SHISA5; SCOTIN; PSEC0133; Protein shisa-5; Putative NF-kappa-B-activating protein 120; Scotin
-
Species
Human
-
Source
E. coli
-
Tag
GST-tag at N-terminal
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q8N114
-
Expression Region
1-137 aa
-
AA Sequence
MGFGATLAVGLTIFVLSVVTIIICFTCSCCCLYKTCRRPRPVVTTTTSTTVVHAPYPQPPSVPPSYPGPSYQGYHTMPPQPGMPAAPYPMQYPPPYPAQPMGPPAYHETLAGGAAAPYPASQPPYNPAYMDAPKAAL
-
Molecular Weight
40.81 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
SHISA5 is a member of the Shisa protein family, which is known to play crucial roles in various cellular processes, particularly in the regulation of signal transduction pathways involving receptor localization and function. Research into SHISA5 has garnered attention due to its involvement in several physiological and pathological conditions, including cell proliferation, differentiation, and potential implications in cancer biology. It has been observed that SHISA5 interacts with various receptor complexes, modulating their activity and stability, which may influence cellular responses to external stimuli. The intricate regulatory mechanisms mediated by SHISA5 highlight its importance in maintaining cellular homeostasis and ensuring proper signaling. Studying the recombinant expression of SHISA5 protein allows for a better understanding of its structural and functional characteristics, thereby providing insights into its roles in health and disease. Furthermore, this research may contribute to the development of targeted therapies that exploit SHISA5's regulatory functions, presenting potential avenues for intervention in diseases where these pathways are disrupted. As such, investigating SHISA5 at the molecular level is not only essential for fundamental biological knowledge but also for its potential translational applications in medicine.
