6533b7cefe1ef96bd12572c0
RESEARCH PRODUCT
Monoclonal anti-fosB antibody specific for predetermined, nonstructural region of the fosB protein.
J. SteinbergsL. JackevicaI. GusarsA. TsimanisM. SallbergK. Kilcevskasubject
Leucine zippermedicine.drug_classImmunologyMolecular Sequence DataEnzyme-Linked Immunosorbent AssayMonoclonal antibodyEpitopeMiceAntibody SpecificityGeneticsmedicineAnimalsHumansAmino Acid SequencePeptide sequencebiologyProtein primary structureDrug Resistance MicrobialMolecular biologyPeptide FragmentsEpitope mappingbiology.proteinAntibodyProto-Oncogene Proteins c-fosEpitope MappingFOSBdescription
Comparison of the primary structures and theoretical prediction of the potential antigenic determinant of the deduced Fos proteins reveals the presence of a nonstructural and hydrophilic region juxtaposed to the leucine zipper and nonconserved among the Fos protein family. To develop monoclonal anti-peptide antibodies capable of distinguishing all Fos-proteins, synthetic peptides specific for the mentioned predicted region were synthesized manually by the "tea-bag" method. Immunization of Balb/c mice with fosB-related synthetic peptide BSA gave rise to mouse hybridoma cell line K21 (IgG1, kappa) secreting highly specific antibodies against corresponding human fosB protein. Fine mapping of the MAb K21 indicated that the minimal epitope essential for the recognition is the sequence GPGPLAE.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 1997-06-01 | Hybridoma |