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Bone marrow stromal cells are involved in the growth and development of B-cells. Additionally we are shipping BST2 Antibodies (173) and BST2 Kits (8) and many more products for this protein.
Showing 10 out of 17 products:
Human BST2 Protein expressed in Escherichia coli (E. coli) - 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.
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.
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.
Using viral tethering, amino acid level insights into the function of BST-2 were identified.
BST-2 restricts Hepatitis B virus production at intracellular multivesicular bodies.
results shed light on the interaction between HIV-2 Env (show ERVW-1 Proteins) and tetherin, suggesting a physical interaction that maps to the ectodomains of both proteins and indicating a strong selection pressure to maintain an anti-tetherin activity in the HIV-2 Env (show ERVW-1 Proteins)
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).
BST-2 is a useful receptor to target with antigen, given its broad expression pattern and ability to access both MHCI and MHCII presentation pathways with relative efficiency.
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