Analytical Data
-
Gene name
BST2
- Application
-
Alternative Names
CD317; Tetherin; HM1.24 antigen
-
Species
Human
-
Source
E. coli
-
Tag
N-His
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q10589
-
Expression Region
Asn49~Ser161
-
Molecular Weight
18kDa
-
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
BST-2, also known as bone marrow stromal antigen 1 (BSA1) or tetherin, is a type II transmembrane protein that plays a critical role in the host immune response against viral infections. It was initially discovered for its ability to restrict the release of enveloped viruses, such as HIV, from infected cells, effectively tethering them to the cellular membrane. This pioneering discovery highlighted the protein's importance in the innate immune defense, intriguingly positioning it as a potential therapeutic target for antiviral strategies. Moreover, BST-2's expression is regulated by various cytokines and can be modulated by different pathogens, including certain viruses that exploit it for their replication. Research into BST-2 has expanded to explore its diverse roles beyond antiviral responses, revealing associations with cancer metastasis and immune regulation. Understanding the molecular mechanisms underlying BST-2 function and its interactions with viral components has become a significant area of interest, as it could lead to novel approaches for enhancing immune responses or developing antiviral therapies. As such, BST-2 recombinant proteins are increasingly utilized in basic and applied research to dissect its mechanisms of action and assess its potential as a biomarker or therapeutic target in various disease contexts, paving the way for innovative strategies in both virology and oncology.
