Imai K, Wilson B S, Bigotti A, Natali P G, Ferrone S
J Natl Cancer Inst. 1982 May;68(5):761-9.
The IgG2a monoclonal antibody (MoAb) 376.96S, secreted by a hybridoma derived from a mouse immunized with cultured human melanoma cells COLO 38, reacts with a single 94,000-dalton glycoprotein that is peripherally associated with the plasma cell membrane of cultured melanoma cells. Indirect immunofluorescence analysis with cryostat thin sections of human tissues showed that this antigen is absent from a large variety of normal tissues but is readily detectable on melanomas, nevi, and several different carcinomas. The MoAb 376.96S binds with cultured melanoma and carcinoma cell lines to a similar extent and can mediate both complement-dependent and cell-dependent lysis of these cells. The 94,000-dalton glycoprotein detected by MoAb 376.96S is distinct in its tissue distribution, antigenicity, and molecular profile from several structures previously identified with monoclonal antibodies that have similar molecular weights.
用培养的人黑色素瘤细胞COLO 38免疫小鼠获得的杂交瘤分泌的IgG2a单克隆抗体（MoAb）376.96S，与一种单一的94,000道尔顿糖蛋白发生反应，该糖蛋白与培养的黑色素瘤细胞的浆细胞膜外周相关。对人体组织冰冻切片进行的间接免疫荧光分析表明，在多种正常组织中不存在这种抗原，但在黑色素瘤、痣和几种不同的癌组织中很容易检测到。MoAb 376.96S与培养的黑色素瘤和癌细胞系的结合程度相似，并且可以介导这些细胞的补体依赖性和细胞依赖性裂解。MoAb 376.96S检测到的94,000道尔顿糖蛋白在组织分布、抗原性和分子特征方面与先前用分子量相似的单克隆抗体鉴定的几种结构不同。
