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Bone marrow stromal cell antigen 2 (BST2) is a dual-anchored transmembrane glycoprotein encoded by the BST2 gene, composed of extracellular coiled-coil domain, single transmembrane segment and cytoplasmic immune signaling tail, and acts as a core scaffold subunit mediating membrane tethering and immune receptor complex assembly. BST2 is widely expressed across stromal, epithelial and myeloid cell populations, serving as a molecular platform linking viral particle confinement and downstream innate immune kinase recruitment upon pathogen stimulation.
BST2 exerts its biological effects through membrane cross-linking and receptor co-assembly at cell surface bilayers, a mechanism that stabilizes extracellular vesicle and virion anchoring and modulates intracellular antiviral signal cascade activation efficiency. Unlike ligand-specific immune receptors, BST2 cannot independently initiate full immune signal cascades and relies on membrane oligomerization to sustain complete signal output; it recruits cytoplasmic signal mediators to assembled membrane complexes, uncoupling extracellular pathogen retention from intracellular immune transcription factor activation and maintaining persistent tissue antiviral response signals. This dual regulatory mode adjusts the magnitude of local immune responses after pathogen exposure, fine-tuning resident immune cell activation and cytokine secretion levels, while sustained abnormal BST2-mediated membrane signaling drives imbalanced antiviral surveillance and inflammatory tissue lesions. BST2 participates in key physiological and pathological processes including viral particle restriction, innate immune priming, stromal tissue homeostasis and chronic infectious inflammatory disorders. Dysregulation of BST2 expression or membrane oligomerization capacity is closely associated with compromised anti-pathogen defense and dysregulated inflammatory responses, making BST2 a crucial research target for antiviral immune signaling, stromal cell biology and infectious disease research.
Fig. 1 Domain architecture and crystal structure of human BST2, marking intracellular signaling motifs, disulfide bond sites, N-glycosylation residues and coiled-coil dimerization interface.1
The biological functions of BST2 are focused on membrane oligomerization, cross-talked innate immune signal propagation and stromal tissue immune balance:
Creative Biolabs offers high-purity BST2 proteins through optimized heterologous expression systems, including full-length BST2 and isolated extracellular coiled-coil domain variants with modified glycosylation status. These products retain native conformational characteristics and membrane oligomer binding activity, suitable for antiviral immune signaling research, membrane complex interaction detection, and small molecule immune modulator screening for infectious disorder research. All BST2 proteins undergo strict quality control, including purity analysis and biological activity validation to preserve core receptor function.
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Creative Biolabs provides custom-engineered BST2 stable cell lines, including overexpressing and knockdown models in stromal and myeloid cell models. These cell lines are optimized for studying BST2-mediated membrane oligomer assembly mechanisms, antiviral signal cascade dynamics, and immune modulator sensitivity. Each cell line undergoes stringent validation, including stable expression detection and functional integrity verification.
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High-specificity recombinant antibodies targeting BST2 are developed via advanced antibody engineering technologies, with no cross-reactivity with other membrane scaffold subunits. These antibodies are validated for multiple applications, including immunofluorescence for BST2 membrane localization, Western blot for expression analysis, and co-immunoprecipitation for BST2-membrane complex research, enabling precise analysis of BST2 expression, subcellular localization and functional regulation.
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Beyond catalog products, Creative Biolabs offers specialized custom services for BST2 research:
BST2 is a dual-anchored membrane scaffold protein that forms surface homo-oligomers to retain extracellular viral particles, modulate pathogen-induced immune signal amplitude, balance stromal tissue immune response dynamics, and mediate innate immune activation upon microbial stimulation.
BST2 is a core regulator of membrane viral restriction and stromal innate immune homeostasis, and its dysregulation is associated with weakened antiviral defense and chronic inflammatory lesions. It is a critical target for antiviral membrane protein and infectious disease research.
No, all BST2 products and services are strictly for research use only, not intended for clinical diagnosis or treatment.
Offerings include BST2 proteins (full-length, extracellular coiled-coil domain variants), specific recombinant antibodies, and custom stable stromal cell lines, supporting antiviral and inflammatory research.
BST2 proteins are validated by membrane oligomer binding assays and antiviral signal regulation verification to ensure native regulatory function in innate immune research.