DEC-205, A 205-KDA PROTEIN ABUNDANT ON MOUSE DENDRITIC CELLS AND THYMIC EPITHELIUM THAT IS DETECTED BY THE MONOCLONAL-ANTIBODY NLDC-145 - PURIFICATION, CHARACTERIZATION, AND N-TERMINAL AMINO-ACID-SEQUENCE
DEC-205, A 205-KDA PROTEIN ABUNDANT ON MOUSE DENDRITIC CELLS AND THYMIC EPITHELIUM THAT IS DETECTED BY THE MONOCLONAL-ANTIBODY NLDC-145 - PURIFICATION, CHARACTERIZATION, AND N-TERMINAL AMINO-ACID-SEQUENCE
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DOI：
10.1006/cimm.1995.1218
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发表时间：
1995-10-15
影响因子：
4.3
通讯作者：
STEINMAN, RM
中科院分区：
文献类型：
--
作者：
SWIGGARD, WJ;MIRZA, A;STEINMAN, RM
单克隆抗体NLDC-145检测小鼠树突状细胞（dc）和胸腺上皮细胞高水平表达的抗原。本文报道了该抗原的纯化和生化特性。NLDC-145单抗检测到的抗原是一种完整的膜糖蛋白，免疫沉淀和Western blotting检测到的表观分子质量为205 kDa。等电点pH为7.5，碳水化合物约占总质量的7kda。凝集素印迹和FACE分析显示非均质双链n -链聚糖。未检测到o链聚糖。n端序列分析表明，该抗原是一种新蛋白，针对合成的n端肽段或整个纯化蛋白制备的多克隆抗体与NLDC-145识别的205-kDa蛋白结合。鉴于其在树突状和胸腺上皮细胞中大量表达，以及修订后的分子质量，我们将其称为DEC-205。(C) 1995学术出版社，Inc。
The monoclonal antibody NLDC-145 detects an antigen expressed at high levels by mouse dendritic cells (DCs) and thymic epithelial cells. Here we report on the purification and biochemical characterization of this antigen. The antigen detected by the NLDC-145 mAb is an integral membrane glycoprotein, with an apparent molecular mass of 205 kDa by immunoprecipitation and Western blotting. The isoelectric point is pH 7.5, and carbohydrates comprise about 7 kDa of the total mass. Lectin blotting and FACE analysis revealed heterogeneous biantennary N-linked glycans. O-linked glycans were not detected. N-terminal sequence analysis revealed that the antigen is a novel protein, Polyclonal antibodies prepared either to a synthetic N-terminal peptide or to whole purified protein bind the same 205-kDa protein recognized by NLDC-145. We refer to the protein as DEC-205, in view of its abundant expression by dendritic and thymic epithelial cells, and the revised molecular mass. (C) 1995 Academic Press, Inc.