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Antibodies to different peptides in osteopontin reveal complexities in the various secreted forms
Author(s) -
Kon Shigeyuki,
Maeda Masahiro,
Segawa Tatsuya,
Hagiwara Yoshiaki,
Horikoshi Yuko,
Chikuma Shunsuke,
Tanaka Kumiko,
Rashid Mohammod Mizanur,
Inobe Manabu,
Chambers Ann F.,
Uede Toshimitsu
Publication year - 2000
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/(sici)1097-4644(20000601)77:3<487::aid-jcb13>3.0.co;2-8
Subject(s) - osteopontin , antibody , computational biology , chemistry , biology , immunology
We have generated synthetic peptides corresponding to various portions of human osteopontin (OPN) and have immunized rabbits and mice with these peptides to generate polyclonal and monoclonal antibodies specific to human OPN. We then generated six distinct sandwich enzyme‐linked immunoabsorbent assay (ELISA) systems by using different pairs of polyclonal and monoclonal antibodies against human OPN. These systems allowed us to detect not only various isoforms and truncated forms of recombinant OPN, but also the glycosylated form of native urinary OPN. Most importantly, tumor‐derived OPN was differentially detected by the six ELISA systems. The ELISA systems that we have developed will be useful for clarifying the functional roles for OPN in vivo in various physiologic and pathologic conditions. J. Cell. Biochem. 77:487–498, 200. © 2000 Wiley‐Liss, Inc.