CD317 (BST2, PDCA-1) Monoclonal Antibody (26F8), Functional Grade, eBioscience™, Invitrogen™

Description

Description: This 26F8 monoclonal antibody reacts with human CD317 (also known as BST2 and tetherin). CD317 is a 30-36-kDa type II transmembrane protein expressed on B cells and bone marrow stromal cells. Although reports have indicated that CD317 mRNA is detectable in activated T cells, protein expression in primary T cells and macrophages is undetectable. Moreover, certain T cell lines, such as Jurkat, do not express detectable levels of CD317 protein. CD317 has been associated with pre-B cell growth and the terminal differentiation of plasma B cells. More recently, this molecule has been reported to prevent HIV-1 virion release from the surface of infected cells, leading to reuptake and degradation of the virus. This activity is inhibited by the HIV-1 accessory protein Vpu. CD317 has been identified as the ligand for the ILT7 receptor. Applications Reported: This 26F8 antibody has been reported for use in flow cytometric analysis and functional assays. The 26F8 clone has been reported to block the binding of CD317 to the ILT7 receptor. Applications Tested: This 26F8 antibody has been tested by flow cytometric analysis on MCF7 cells. This can be used at less than or equal to 0.125 μg per test. A test is defined as the amount (μg) of antibody that will stain a cell sample in a final volume of 100 μL. Cell number should be determined empirically but can range from 10^5 to 10^8 cells/test.

BST2 (CD317, HM1.24 antigen, DAMP-2, tetherin) is an integral membrane protein that is involved in the development and growth of B-cells. The surface expression of BST2 on fibroblast cell lines facilitated the stromal cell-dependent growth of DW34, a pre-B-cell line. BST2 is highly expressed during B-cell development, from pro-B precursors to plasma cells, T-cells, monocytes, NK cells and DCs (at protein level), and myeloma cells. Research studies have shown that BST2 also functions as an inhibitor of retrovirus release from human cells whose activity is antagonized by the HIV-1 accessory protein, Vpu. While BST2 causes retention of virions on cell surfaces or endocytosis into BST2-positive compartments, its depletion abolished the viral requirement for Vpu for virus release, an activity that may represent a potential therapeutic strategy for the treatment of HIV/AIDS. Another disease associated with BST2 dysfunction is stomatitis.