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一种新型单克隆抗体1B3.1与VLA-1分子的一个新表位结合。

A novel monoclonal antibody, 1B3.1, binds to a new epitope of the VLA-1 molecule.

作者信息

Bank I, Hemler M, Brenner M B, Cohen D, Levy V, Belko J, Crouse C, Chess L

机构信息

Department of Internal Medicine and Oncology, Chaim Sheba Medical Center Tel Hashomer, Israel.

出版信息

Cell Immunol. 1989 Sep;122(2):416-23. doi: 10.1016/0008-8749(89)90088-9.

Abstract

A monoclonal antibody, 1B3.1, was raised against a cloned IL-2-dependent T cell line that expresses the T gamma delta T cell receptor. MoAb 1B3.1 reacted with long-term cultured T cell lines of both T gamma delta and T alpha beta lineage, and with in vivo-stimulated T cells, derived from synovial fluid, but not with resting or short-term activated T cells, B cells, or macrophages. Immunoprecipitation of the 1B3.1 target antigens showed that 1B3.1 recognizes a 200/110 kDa molecule that is identical to the VLA-1 heterodimer precipitated by MoAb TS2/7. 1B3.1, however, binds to an epitope of VLA-1 that is distinct from the TS2/7 binding site. This new MoAb could be useful in further studies of the functions of VLA-1, and of the cells that express this molecule.

摘要

制备了一种针对表达Tγδ T细胞受体的克隆化IL-2依赖型T细胞系的单克隆抗体1B3.1。单克隆抗体1B3.1与Tγδ和Tαβ谱系的长期培养T细胞系以及源自滑液的体内刺激T细胞发生反应,但不与静息或短期活化的T细胞、B细胞或巨噬细胞发生反应。对1B3.1靶抗原的免疫沉淀显示,1B3.1识别一种200/110 kDa的分子,该分子与单克隆抗体TS2/7沉淀的VLA-1异二聚体相同。然而,1B3.1与VLA-1的一个表位结合,该表位与TS2/7结合位点不同。这种新的单克隆抗体可能有助于进一步研究VLA-1的功能以及表达该分子的细胞。

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