Monoclonal antibodies reacting with the mucin-specific lectin from Sambucus sieboldiana (SSA-M).
Monoclonal antibodies (MAbs) were prepared against the mucin-specific lectin from Sambucus sieboldiana (SSA-M). The majority of MAbs reacted with both free SSA-M and SSA-M bound to porcine mucin. However, MAbs SS16, SS18, and SS19 did not react with mucin-bound lectin, suggesting that these MAbs may react at or near the lectin binding site. Some MAbs also showed reactivity with lectins other than SSA-M (e.g. ConA, Pisum sativum, and Saphora japonica lectins) suggesting possible sequence homology between SSA-M and other lectins. These MAbs should be useful reagents for immunoaffinity purification of SSA-M, characterizing SSA-M structure and binding, and metabolic studies on mucins.
Devine
P L
PL
University of Queensland, Department of Obstetrics and Gynaecology, Royal Brisbane Hospital, Herston, Australia.
Quin
R J
RJ
Harada
H
H
D000818:Animals; D000911:Antibodies, Monoclonal / Q000276:immunology*; D002240:Carbohydrate Sequence; D003429:Cross Reactions; D004797:Enzyme-Linked Immunosorbent Assay; D005260:Female; D007132:Immunoglobulin Isotypes / Q000276:immunology; D037102:Lectins / Q000276:immunology*; D051379:Mice; D008807:Mice, Inbred BALB C; D008969:Molecular Sequence Data; D037121:Plant Lectins; D054788:Ribosome Inactivating Proteins
D000911:Antibodies, Monoclonal; D007132:Immunoglobulin Isotypes; D037102:Lectins; D037121:Plant Lectins; C050600:Sambucus nigra lectins; D054788:Ribosome Inactivating Proteins