A monoclonal antibody against a synthetic fragment of bombyxin (4K-prothoracicotropic hormone) from the silkmoth, Bombyx mori: characterization and immunohistochemistry.
Monoclonal antibodies were produced by immunizing mice with a synthetic decapeptide corresponding to the N-terminal portion of the A-chain of bombyxin, a peptide from Bombyx mori which activates the prothoracic glands of the saturniid moth, Samia cynthia ricini, and was previously called 4K-PTTH. We obtained a hybridoma clone secreting an antibody that recognized specifically bombyxin after treatments for disulfide-bond reduction but did not when untreated. Immunoblotting studies demonstrated the presence of highly heterogeneous immunoreactive components in Bombyx brain homogenates. Immunohistochemistry using this antibody indicated that bombyxin was produced by four pairs of mid-dorsal neurosecretory cells of the brain and transferred to and released from the corpora allata of Bombyx.
Mizoguchi
A
A
Ishizaki
H
H
Nagasawa
H
H
Kataoka
H
H
Isogai
A
A
Tamura
S
S
Suzuki
A
A
Fujino
M
M
Kitada
C
C
D000818:Animals; D000911:Antibodies, Monoclonal; D012831:Bombyx; D001923:Brain Chemistry; D003335:Corpora Allata / Q000032:analysis; D004797:Enzyme-Linked Immunosorbent Assay; D006651:Histocytochemistry; D007163:Immunosorbent Techniques; D007301:Insect Hormones / Q000276:immunology*; D007814:Larva / Q000032:analysis; D008970:Molecular Weight; D010446:Peptide Fragments / Q000276:immunology*
D000911:Antibodies, Monoclonal; D007301:Insect Hormones; D010446:Peptide Fragments; C009089:prothoracicotropic hormone