Recombinant Human BST2 Protein, His

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.