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Human BST2 ELISA Kit for Sandwich ELISA - ABIN811640
Fang, Kao, Chi, Liang, Liu, Hseuh, Liao, Yen, Yu, Chang: Overexpression of BST2 is associated with nodal metastasis and poorer prognosis in oral cavity cancer. in The Laryngoscope 2014
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 ELISA Kits) indicate a common regulation by the interferon (show IFNA ELISA Kits) 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 and Tetherin by the interaction of the Nsp3 (show SH2D3C ELISA Kits) with IFITM1 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.
Thus, efficient human immunodeficiency virus type 1 release from infected cells seems to play an important role in the spread of the virus in the human population and requires a fully functional Vpu protein that counteracts human tetherin.
BST-2 restricts influenza A virus release and is countered by the viral M2 protein.
IL8 (show IL8 ELISA Kits) might play an important role in the enhancement of BST2 and be involved in HBsAg eradication.
Antagonism of BST-2 is a conserved function of the env glycoprotein of primary HIV-2 isolates.
These data present the first example of an HIV-1 group O Vpu that efficiently antagonizes human tetherin and suggest that counteraction by O-Nefs may be suboptimal.
This is in contrast to the pandemic HIV-1 group M-specified BST2 countermeasure Vpu.
The authors show that while the conserved transmembrane-proximal Vpu hinge region residues have no intrinsic activity on the cellular distribution of Vpu in the absence of BST2, they regulate the ability of Vpu to bind to BST2 and, consequently, govern both BST2-dependent trafficking properties of the protein as well as its co-localization with BST2.
In this study, we addressed this question by analysing sLex expression together with two glycoproteins (BST-2 and LGALS3BP (show LGALS3BP ELISA Kits)).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 ELISA Kits), actually happens and the cytoplasmic tails, both the N-terminal domain of Bst-2 and the C-terminal domain of MT1-MMP (show MMP14 ELISA Kits), play crucial roles in the interaction. The interaction between Bst-2 and MT1-MMP (show MMP14 ELISA Kits) is important in MT1-MMP (show MMP14 ELISA Kits) regulating the tetherin activity of Bst-2 and also in Bst-2 regulating the activity of the MT1 (show MT1A ELISA Kits)-MP/proMMP2/MMP2 (show MMP2 ELISA Kits) pathway.
BST-2 and HIV-2 Env 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 ectodomain for the anti-tetherin function. This study also demonstrated the involvement of the HIV-2 Env cytoplasmic tail in this antagonistic role.
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 ELISA Kits) 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 ELISA Kits).
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