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Characterization of Antisera Directed Against follistatin/activin-binding Protein Peptides

S Saito, K Sugino, K Yamanouchi, K Kogawa, K Titani, K Shiota, M Takahashi, H Sugino

Endocrinol Jpn. 1991 Aug;38(4):377-82.

PMID: 1802678

Abstract:

An attempt was made to develop immunologic probes directed against follistatin/activin-binding protein (ABP), for use in investigating the distribution of ABP in various tissues. Five oligopeptides corresponding to different regions of the predicted ABP amino acid sequence (peptides 1-12, 28-43, 123-134, 270-281 and 300-315) were synthesized chemically, and coupled to Limulus polyphemus hemolymph hemocyanin. The peptide-hemocyanin conjugates were then used to immunize rabbits, and the immunoresponses were monitored by enzyme-linked immunosorbent assay. Reactivity of the antipeptide antisera with ABP was determined by SDS-polyacrylamide gel electrophoresis and immunoblotting analysis. All of the peptides produced immune responses. The antiserum to peptide 123-134 recognized all forms of ABP, whereas the antiserum to peptide 300-315 reacted specifically and sensitively with the long forms of ABP. These two antisera exhibited only a limited cross-reaction with other proteins or none at all. Therefore, they will be useful for studying the distribution of ABP in various tissues.

Chemicals Related in the Paper:

Catalog Number Product Name Structure CAS Number Price
AP9013723-A Hemocyanin from Limulus polyphemus hemolymph Hemocyanin from Limulus polyphemus hemolymph 9013-72-3 Price
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