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KMID : 0578319950050020134
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Molecules and Cells
1995 Volume.5 No. 2 p.134 ~ p.139
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Production and Characterization of Monoclonal Antibodies against Heat Shock Protein 70
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Kang, Ho Sung
Park, Young Chul/Han, Song Il/Kim, Young Hee/Moon, Dae Yeon/Lee, Chu/Kim, Byeong Gee
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Abstract
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Heat shock protein 70 (hsp70, also known as hsp72/hsp73) is known to function as a molecular chaperone that regulates in vivo folding and assembly of proteins. However, its exact action mechanism remains to be elucidated. In this study, in order to facilitate the characterization of hsp70 function, monoclonal antibodies against hsp70 and Bip/grp78 were produced by the murine hybridoma technique. For the production of MAb´s, hsp70 and Bip/grp78 were purified from human placenta by DEAE-cellulose ion exchange and ATP-agarose affinity chromatography and immunized into Balb/c mice and then the spleen cells from the mice were fused with NSI myeloma cells. The hybridoma cells were screened by enzyme-linked immunosorbent assay and subcloned by limiting dilution and successively in semi-solid agnrose. Here we report the production of 16 positive monoclonal hfbridoma cells which all recognized inducible hsp72 as well as constitutively expressed hsp73. Most of the monoclonal antibodies showed the crossreactiyities with hsp70 from human, rabbit, mouse, chick, plant, frog, fish and Drosopihla but not with that from E. coli.
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