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Human BST2 Primary Antibody for SDS - ABIN667927
Schubert, Zhai, Sandrin, Eckert, Garcia-Maya, Saul, Sundquist, Steiner, Hill: Structural and functional studies on the extracellular domain of BST2/tetherin in reduced and oxidized conformations. in Proceedings of the National Academy of Sciences of the United States of America 2010
Show all 2 references for ABIN667927
The cytoplasmic domain of HIV-1 Vpu contributes to the physical interaction with, and functional antagonism of chimpanzee BST-2.
the detected relationship between BST2 expression and viral load as well as with MX1 (show MX1 Proteins) indicate a common regulation by the interferon (show IFNA Proteins) response and suggest rather limited influence of BST2 in vivo on the simian immunodeficiency virus infection outcome
Data suggest that rhesus macaque tetherin and Simian immunodeficiency virus Nef undergo physical interaction leading to removal of tetherin from plasma membrane by clathrin-mediated endocytosis.
A 5-amino-acid sequence in the rhesus BST-2 cytoplasmic domain accounts for the interaction with Vpu and for rhesus BST-2 antagonism by HIV-1 Vpu.
Simian immunodeficiency virus infection results in rapid upregulation of BST-2 on peripheral blood lymphocytes.
Indirect immunofluorescence assay and western blot analysis showed that the MAb was specifically reacted with the overexpressed porcine BST-2 protein in Vero cells. The specific MAb of porcine BST-2 provides a valuable tool for further studies of BST-2 to restrict virus infection
This antibody only reacted with porcine BST-2 protein and not with human, monkey, or mouse BST-2 protein
PRRSV counteract the antiviral functions of IFITM1 (show IFITM1 Proteins) and Tetherin by the interaction of the Nsp3 (show SH2D3C Proteins) with IFITM1 (show IFITM1 Proteins) and the E protein with Tetherin.
The BST2 had antiviral activity against vesicular stomatitis virus, avian influenza virus and Porcine reproductive and respiratory syndrome virus.
In this study, we addressed this question by analysing sLex expression together with two glycoproteins (BST-2 and LGALS3BP (show LGALS3BP Proteins)).Concomitant high expression of BST-2 with sLex defined a sub-group of patients with ER-negative tumours displaying higher risks of liver and brain metastasis and a 3-fold decreased survival rate
Studies demonstrate that the interaction Bst-2 and MT1-MMP (show MMP14 Proteins), actually happens and the cytoplasmic tails, both the N-terminal domain of Bst-2 and the C-terminal domain of MT1-MMP (show MMP14 Proteins), play crucial roles in the interaction. The interaction between Bst-2 and MT1-MMP (show MMP14 Proteins) is important in MT1-MMP (show MMP14 Proteins) regulating the tetherin activity of Bst-2 and also in Bst-2 regulating the activity of the MT1 (show MT1A Proteins)-MP/proMMP2/MMP2 (show MMP2 Proteins) pathway.
BST-2 and HIV-2 Env (show ERVW-1 Proteins) proteins interact through their ectodomain but residues involved are not clearly defined. In this study, we demonstrated the importance of the asparagine residue at position 659 in the HIV-2 gp36 (show PDPN Proteins) ectodomain for the anti-tetherin function. This study also demonstrated the involvement of the HIV-2 Env (show ERVW-1 Proteins) cytoplasmic tail in this antagonistic role.
results herein demonstrated that IMB-LA could specifically inhibit the degradation of BST-2 induced by Vpu, and impair HIV-1 replication in a BST-2 dependent manner
BST-2 inhibits the the release of Hepatitis B virus particles. [review]
Data suggest that ATP1B3 is binding partner of BST-2 and regulates stability of BST-2; ATP1B3 is co-factor that accelerates BST-2 degradation and reduces BST-2-mediated restriction of HIV-1 replication/tropism and NFkappaB activation.
Combining these results suggests an important role for the Ebola virus glycoprotein glycan cap and membrane spanning domain in tetherin antagonism.
BST2 showed significantly elevated plasma levels and overexpression of BST2 in CRC (show CALR Proteins) tissues that correlated with poor survival of colorectal cancer patients.
Human parainfluenza virus type 2 V protein antagonizes tetherin by binding it and reducing its presence at the cell surface.
studies suggest that Vpu hijacks the FLNa (show FLNA Proteins) function in the modulation of tetherin to neutralize the antiviral factor tetherin.
Bone marrow stromal antigen 2-mediated dendritic cell activation as a critical mechanism for how Tetherin influenced retrovirus cell-mediated immune responses that subsequently inhibited retrovirus replication in vivo.
BST-2 does not have a role in modulating Influenza A Virus in the mouse model of infection
Although Bst2 prevented Measles virus (MV) release from nonneuronal cells, its deletion had no effect on viral pathogenesis in MV-challenged mice.
BST-2 contributes to the emergence of neoplasia and malignant progression of breast cancer. BST-2 enhances cancer cell adhesion, anchorage-independency, migration, and invasion.
BST-2 protects lymphoid tissues from Chikungunya virus (CHIKV) infection and regulates CHIKV-induced inflammatory response by the host.
TLR4 (show TLR4 Proteins) and PI3K effects on BST-2 induction are at the level of transcription.
Tetherin acts as a modulator of the cell-mediated immune response against retrovirus infection in vivo.
These findings suggest that BST2 antagonism by Vpu is critical for efficient early viral expansion and dissemination during acute infection and as such is likely to confer HIV-1 increased transmission fitness.
These data suggest that overexpression of BST-2 in carcinoma tissues could not be attributed to interferons but to a yet to be determined factor that upregulates BST-2 once oncogenesis is initiated.
Taken together, our results indicate that BST-2 is an important factor in the invasiveness and motility of tamoxifen-resistant breast cancer cells, and that its expression and activity are regulated by activated STAT3 (show STAT3 Proteins).
Bone marrow stromal cells are involved in the growth and development of B-cells. The specific function of the protein encoded by the bone marrow stromal cell antigen 2 is undetermined\; however, this protein may play a role in pre-B-cell growth and in rheumatoid arthritis.
bone marrow stromal antigen 2
, bone marrow stromal cell antigen 2
, HM1.24 antigen
, DAMP-1 protein homolog
, protein DAMP-1