Search results for " Monoclonal"

showing 10 items of 807 documents

Identification and characterization of a monoclonal antibody to the membrane fatty acid binding protein

1992

A monoclonal antibody to the rat liver membrane fatty acid binding protein (MFABP) was prepared by immunizing mice with purified MFABP isolated from solubilized rat liver plasma membrane proteins by oleate-agarose affinity chromatography technique. The monoclonal antibody K15/6 identified a single 40 kDa protein in rat liver plasma membranes with pI values of 8.5, 8.8 and 9.0, which is identical to the authentic MFABP, but clearly distinct from rat mitochondrial GOT. The antibody K15/6 selectively inhibited cellular influx as well as membrane binding of fatty acids, but not of cholesterol or vitamin E. The same antibody was used in immunofluorescence, ELISA and Western blot analysis to dete…

medicine.drug_classBlotting WesternImmunoblottingBiophysicsFluorescent Antibody TechniqueEnzyme-Linked Immunosorbent AssayNerve Tissue ProteinsFatty Acid-Binding ProteinsMonoclonal antibodyBiochemistryFatty acid-binding proteinCell LineMiceEndocrinologyAffinity chromatographymedicineAnimalsHumanschemistry.chemical_classificationMice Inbred BALB CbiologyMembrane transport proteinTumor Suppressor ProteinsBinding proteinCell MembraneFatty AcidsAntibodies MonoclonalFatty acidMolecular biologyNeoplasm ProteinsRatsLiverchemistryMembrane proteinBiochemistrybiology.proteinElectrophoresis Polyacrylamide GelAntibodyCarrier ProteinsFatty Acid-Binding Protein 7Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism
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Liver cell damage caused by monoclonal antibody against an organ-specific membrane antigen in vivo and in vitro

1987

Summary Monoclonal antibodies have been raised against different antigenic determinants of normal rabbit hepatocytes. One antibody (2D3) recognized a liver-specific 43 kDa protein displayed exclusively on the basolateral portion of the hepatocellular membrane. Purified monoclonal antibodies were injected intravenously into rabits. Following the injection of antibody 2D3, a dose-dependent increase of liver enzyme activities in sera was observed. Within 8 h, marked morphological alterations of the hepatocytes, including multiple cell necroses, could be demonstrated by light and electron microscopy. When isolated vital rabbit hepatocytes in culture were used as targets, cytotoxic effects of th…

medicine.drug_classCellBiologyMonoclonal antibodyAutoimmune DiseasesAntigenIn vivomedicineAnimalsCytotoxic T cellHepatitisHepatologyLiver DiseasesAntibodies MonoclonalMembrane ProteinsProteinsmedicine.diseaseVirologyMolecular biologyIn vitromedicine.anatomical_structureLiverOrgan SpecificityAntigens Surfacebiology.proteinRabbitsAntibodyJournal of Hepatology
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Analysis of liver-specific protein LSP using murine monoclonal antibodies.

1987

. We describe twenty murine monoclonal antibodies directed against different antigenic determinants of human and rabbit liver-specific protein LSP. Among them, nine were directed against liver-specific epitopes as judged from immunohistological studies. Immunoelectronmicroscopy revealed that seven of these monoclonals recognized membrane determinants differing in staining of distinct areas of the hepatocellular surface. Eleven antibodies were directed against intracellular structures. Western blot analysis showed that the epitopes detected were displayed on either single or multiple protein bands with apparent molecular weights between 24 000 and 60 000. Further differences were observed wi…

medicine.drug_classClinical BiochemistryMonoclonal antibodyBiochemistryEpitopeEpitopesMiceWestern blotAntigenmedicineAnimalsHumansbiologymedicine.diagnostic_testMolecular massAntibodies MonoclonalMembrane ProteinsProteinsGeneral MedicineMolecular biologyImmunohistochemistryStainingLiverAntigens Surfacebiology.proteinRabbitsAntibodyIntracellularEuropean journal of clinical investigation
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Monoclonal antibodies against components of the classical pathway of complement.

1989

Activation of the classical pathway of complement involves several binding and enzymatic cleavage processes. Binding and enzymatic activation results in the appearance of new structures in the individual components. This report describes the different activation steps for C1q, C1r, C1s, C4 and C2 and summarizes monoclonal antibodies reported so far which recognize either conserved epitopes or activation-dependent epitopes with particular emphasis on neoepitopes occurring during the activation cascade.

medicine.drug_classComplement Activating EnzymesImmunologyComplement C3-C5 ConvertasesComplement C3-C5 ConvertasesMonoclonal antibodyEpitopeClassical complement pathwayEpitopesComplement C1medicineComplement Pathway ClassicalComplement C1qComplement ActivationComplement component 2biologyChemistryComplement C1qAntibodies MonoclonalComplement C4HematologyComplement System ProteinsComplement C2Complement systemBiochemistrybiology.proteinAntibodyComplement and inflammation
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The C-terminal antibody binding domain ofCandida albicansmp58 represents a protective epitope during candidiasis

2003

The 58-kDa surface mannoprotein of Candida albicans (mp58) elicits strong antibody responses during infection. Epitope mapping with sera from patients with candidiasis and control individuals indicated the presence of multiple IgG-reactive continuous epitopes on the protein, expanding both the amino- and carboxy-terminal domains and several internal regions. These immunoreactive regions were similar to the ones previously identified using sera from immunized animals. Two of the epitopic regions (including the C-terminal domain) showed increased reactivity with antibodies present in sera from patients with candidiasis as compared to control individuals. Patients who survived the infection di…

medicine.drug_classEnzyme-Linked Immunosorbent AssayMonoclonal antibodyMicrobiologyEpitopeImmunoglobulin GFungal ProteinsEpitopesMiceCandida albicansGeneticsmedicineAnimalsAmino Acid SequenceCandida albicansMolecular BiologyMice Inbred BALB CMembrane GlycoproteinsbiologyCandidiasisAntibodies Monoclonalbiology.organism_classificationDisseminated CandidiasisVirologyCorpus albicansProtein Structure TertiaryEpitope mappingbiology.proteinFemaleAntibodyEpitope MappingFEMS Microbiology Letters
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Rationally designed haptens for highly sensitive monoclonal antibody-based immunoanalysis of fenhexamid.

2018

Immunochemical methods have been consolidated during the last few years as complementary analytical strategies for chemical contaminant and residue determination. However, generation of suitable immunoreagents for small organic molecules demands adequate hapten design. In this study, fenhexamid was considered as a model compound and novel haptens were designed and synthesized in order to evaluate the influence of the linker tethering site on antibody binding properties and immunoassay parameters. Haptens were conceived with the spacer arm at different positions, while the more antigenic aromatic moiety was kept free. The synthesis of these functionalized compounds was accomplished by total …

medicine.drug_classEnzyme-Linked Immunosorbent AssayTandem mass spectrometryQuechersMonoclonal antibody01 natural sciencesBiochemistryAnalytical ChemistryLimit of DetectionElectrochemistrymedicineEnvironmental ChemistrySpectroscopyDetection limitResidue (complex analysis)Chromatographymedicine.diagnostic_test010405 organic chemistryChemistry010401 analytical chemistryAntibodies MonoclonalRepeatabilityAmides0104 chemical sciencesFungicides IndustrialImmunoassayHaptenHaptensThe Analyst
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Evaluation of a novel monoclonal antibody against tumor-associated MUC1 for diagnosis and prognosis of breast cancer

2019

There is still a great unmet medical need concerning diagnosis and treatment of breast cancer which could be addressed by utilizing specific molecular targets. Tumor-associated MUC1 is expressed on over 90 % of all breast cancer entities and differs strongly from its physiological form on epithelial cells, therefore presenting a unique target for breast cancer diagnosis and antibody-mediated immune therapy. Utilizing an anti-tumor vaccine based on a synthetically prepared glycopeptide, we generated a monoclonal antibody (mAb) GGSK-1/30, selectively recognizing human tumor-associated MUC1. This antibody targets exclusively tumor-associated MUC1 in the absence of any binding to MUC1 on health…

medicine.drug_classEstrogen receptorMUC1Breast NeoplasmsMice TransgenicDeferoxamineMonoclonal antibody89Zr03 medical and health sciences0302 clinical medicineBreast cancerIn vivoCell Line TumorBiomarkers TumormedicineAnimalsHumansTissue Distributionskin and connective tissue diseasesMUC1Triple-negative breast cancermAbRadioisotopesMice Inbred BALB Cbiologybusiness.industryMucin-1breast cancer diagnosisAntibodies MonoclonalCancerGeneral MedicinePrognosismedicine.diseaseImmunohistochemistryMice Inbred C57BLPositron-Emission Tomographybiology.proteinCancer researchFemale030211 gastroenterology & hepatologyZirconiumAntibodybusinessResearch PaperInternational Journal of Medical Sciences
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Generation of anti-azoxystrobin monoclonal antibodies from regioisomeric haptens functionalized at selected sites and development of indirect competi…

2012

Azoxystrobin is a modern strobilurin fungicide used around the world to combat prime diseases affecting highly valuable crops. Accordingly, residues of this chemical are frequently found in food, even though mostly under maximum tolerated levels. We herein describe the development of an indirect competitive immunoassay for the determination of azoxystrobin residues. A panel of monoclonal antibodies displaying subnanomolar affinity to azoxystrobin was generated using, as immunizing haptens in mice, four functionalized derivatives carrying the same spacer arm located at different rationally chosen positions. This collection of antibodies was thoroughly characterized with homologous and hetero…

medicine.drug_classFungicidePolysorbatesEnzyme-Linked Immunosorbent AssayFood ContaminationMonoclonal antibodyBiochemistryFood safetyAnalytical ChemistryMicechemistry.chemical_compoundLimit of DetectionVegetablesmedicineAnimalsEnvironmental ChemistrySpectroscopyMice Inbred BALB CHybridomasChromatographybiologymedicine.diagnostic_testChemistryAntibodies MonoclonalStrobilurinsFungicides IndustrialCompetitive ELISAFungicideSite heterologyPyrimidinesAzoxystrobinFruitImmunoassayStrobilurinSolventsbiology.proteinMethacrylatesLandsteiner's principleFemaleAntibodyHaptensHaptenConjugateAnalytica Chimica Acta
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C1q-bearing immune complexes detected by a monoclonal antibody to human C1q in rheumatoid arthritis sera and synovial fluids

1991

Using a monoclonal antibody directed against the C-chain of human C1q, we detected C1q-bearing immune complexes (IC) in sera and synovial fluids of rheumatoid arthritis (RA) patients. In a sandwich-ELISA, C1q-bearing IC were captured by the solid-phase monoclonal antibody and then detected with peroxidase-labeled F(ab')2-antibodies to either human IgG or IgM. The results of this assay were compared to an ELISA-modification of the C1q-solid-phase binding assay (C1q-SPBA). C1q-bearing IC were detected in 81.1% of RA-sera and the 65.2% of RA-synovial fluids. IgG as well as IgM was present in 72.6% of the sera and 70% of the synovial fluids which were positive in both assays. Most RA sera that …

medicine.drug_classImmunologyEnzyme-Linked Immunosorbent Assaychemical and pharmacologic phenomenaAntigen-Antibody ComplexMonoclonal antibodyComplement Hemolytic Activity AssayArthritis RheumatoidImmunoglobulin Fab FragmentsClassical complement pathwayImmune systemRheumatologyimmune system diseasesOsteoarthritisSynovial FluidmedicineHumansImmunology and AllergySynovial fluidskin and connective tissue diseasesbiologybusiness.industryComplement C1qAntibodies Monoclonalmedicine.diseaseImmune complexImmunoglobulin MImmunoglobulin GRheumatoid arthritisMonoclonalImmunologybiology.proteinAntibodybusinessRheumatology International
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Fab fragments from a monoclonal antibody against a germ tube mannoprotein block the yeast-to-mycelium transition in Candida albicans.

1990

Fab fragments prepared from the immunoglobulin G monoclonal antibody (MAb) 4C12, which reacts with a determinant expressed on the hyphal extension of germ tubes of Candida albicans, inhibited germ tube formation, but intact MAb 4C12 did not. Indirect immunofluorescence showed a punctate binding pattern on cells incubated with Fab fragments but a confluent binding on cells incubated with intact MAb 4C12.

medicine.drug_classImmunologyGerm tubeFluorescent Antibody TechniqueMonoclonal antibodyMicrobiologyImmunoglobulin GMicrobiologyImmunoglobulin Fab FragmentsCell WallCandida albicansmedicineAscitic FluidHumansCandida albicansMyceliumMembrane GlycoproteinsbiologyImmunoglobulin Fab FragmentsAntibodies Monoclonalbiology.organism_classificationMolecular biologyYeastInfectious DiseasesMicroscopy FluorescenceImmunoglobulin Gbiology.proteinParasitologyAntibodyResearch ArticleInfection and immunity
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