Search results for "Recombinant Fusion Protein"

showing 10 items of 260 documents

Cloning and characterization of CSP37, a novel gene encoding a putative membrane protein of Candida albicans.

1997

In the course of an analysis of the functions and assembly of the cell wall of Candida albicans, we have cloned and characterized a gene, which we designated CSP37 (cell surface protein), encoding a 37-kDa polypeptide which is a membrane-associated protein. The gene was isolated by immunological screening of a DNA library constructed from mycelial cells with a polyclonal serum raised against cell walls of this morphology. Analysis of the nucleotide sequence of a corresponding genomic DNA fragment revealed a single open reading frame which encodes a predicted protein of 321 amino acids with no significant homology to others in the databases. Disruption of the CSP37 gene by the method describ…

Vesicle-associated membrane protein 8HeterozygoteRecombinant Fusion ProteinsMutantGenes FungalMolecular Sequence DataBiologyMicrobiologyRetinoblastoma-like protein 1Fungal ProteinsMiceHSPA2SNAP23Candida albicansEscherichia coliAnimalsAmino Acid SequenceCloning MolecularDNA FungalMolecular BiologyGeneHSPA9Mice Inbred BALB CBase SequenceHomozygoteMembrane ProteinsSequence Analysis DNABlotting NorthernMolecular biologyPhenotypeAKT1S1Gene DeletionResearch ArticleJournal of bacteriology
researchProduct

Polar accumulation of the metabolic sensory histidine kinases DcuS and CitA in Escherichia coli

2008

Signal transduction in prokaryotes is frequently accomplished by two-component regulatory systems in which a histidine protein kinase is the sensory component. Many of these sensory kinases control metabolic processes that do not show an obvious requirement for inhomogeneous distribution within bacterial cells. Here, the sensory kinases DcuS and CitA, two histidine kinases of Escherichia coli, were investigated. Both are membrane-integral and involved in the regulation of carboxylate metabolism. The two-component sensors were fused with yellow fluorescent protein (YFP) and live images of immobilized cells were obtained by confocal laser fluorescence microscopy. The fluorescence of the fusio…

Yellow fluorescent proteinbiologyKinaseEscherichia coli ProteinsRecombinant Fusion ProteinsCell PolarityMicrobiologyFusion proteinLuminescent ProteinsProtein TransportBacterial ProteinsBiochemistryCytoplasmEscherichia colibiology.proteinSignal transductionCell fractionationProtein kinase AProtein KinasesHistidineMicrobiology
researchProduct

In vivo and in vitro sensitivity of blastic plasmacytoid dendritic cell neoplasm to SL-401, an interleukin-3 receptor targeted biologic agent.

2015

International audience; Blastic plasmacytoid dendritic cell neoplasm is an aggressive malignancy derived from plasmacytoid dendritic cells. There is currently no accepted standard of care for treating this neoplasm, and therapeutic strategies have never been prospectively evaluated. Since blastic plasmacytoid dendritic cell neoplasm cells express high levels of interleukin-3 receptor α chain (IL3-Rα or CD123), antitumor effects of the interleukin-3 receptor-targeted drug SL-401 against blastic plasmacytoid dendritic cell neoplasm were evaluated in vitro and in vivo. The cytotoxicity of SL-401 was assessed in patient-derived blastic plasmacytoid dendritic cell neoplasm cell lines (CAL-1 and …

[SDV.MHEP.HEM] Life Sciences [q-bio]/Human health and pathology/HematologyMalePathology[SDV]Life Sciences [q-bio]ApoptosisMice SCIDMice0302 clinical medicineMice Inbred NODhemic and lymphatic diseasesTumor Cells CulturedMedicineCytotoxic T cellNeoplasm[ SDV.MHEP.HEM ] Life Sciences [q-bio]/Human health and pathology/HematologyCytotoxicityAged 80 and overmedicine.diagnostic_test[SDV.MHEP.HEM]Life Sciences [q-bio]/Human health and pathology/HematologyHematologyArticlesMiddle AgedFlow Cytometry3. Good health[SDV] Life Sciences [q-bio]030220 oncology & carcinogenesisHematologic NeoplasmsFemaleAdultmedicine.medical_specialtyRecombinant Fusion ProteinsBlotting WesternInterleukin-3 Receptor alpha Subunit[SDV.CAN]Life Sciences [q-bio]/Cancer[SDV.BC]Life Sciences [q-bio]/Cellular BiologyIn Vitro TechniquesFlow cytometry03 medical and health sciences[SDV.CAN] Life Sciences [q-bio]/CancerBiomarkers TumorAnimalsHumans[SDV.BC] Life Sciences [q-bio]/Cellular BiologyAgedCell ProliferationMyeloproliferative Disordersbusiness.industryCell growthDendritic Cellsmedicine.diseaseXenograft Model Antitumor Assaysstomatognathic diseasesCell cultureApoptosisCancer researchInterleukin-3 receptorbusiness030215 immunologyPlasmacytomaHaematologica
researchProduct

Expression and purification of polyhistidine-tagged firefly luciferase in insect cells

2001

The coleopteran firefly, Photinus pyralis, luciferase was produced in lepidopteran Trichoplusia ni insect cells using a baculovirus expression vector. The recombinant protein was equipped with a polyhistidine affinity tag at the carboxyl terminus and purified by immobilized metal-ion affinity chromatography in combination with an expanded bed adsorption system. This approach enabled an efficient, one-step purification protocol of a genetically modified luciferase with properties similar to those of the authentic counterpart. According to light emission measurements, the final yield of highly purified protein was 23 mg l−1 of cell culture. In addition, no specific interaction of interfering …

aviationRecombinant Fusion ProteinsBioengineeringMothsProtein EngineeringApplied Microbiology and Biotechnologychemistry.chemical_compoundAffinity chromatographyPhotinus pyralisAnimalsLuciferaseHistidinePolyhistidine-tagLuciferasesbiologyExpanded bed adsorptionGeneral Medicinebiology.organism_classificationFusion proteinMolecular biologyColeopteraaviation.aircraft_modelchemistryBiochemistryLight emissionLampyridaePeptidesBiotechnologyJournal of Biotechnology
researchProduct

Production, crystallization and preliminary X-ray analysis of the human integrin alpha1 I domain.

1999

Integrin α1β1 is one of the main collagen receptors in many cell types. A fast large-scale production, purification and crystallization method for the integrin α1 I domain is reported here. The α1 I domain was crystallized using the vapour-diffusion method with a reservoir solution containing a mixture of PEG 4000, sodium acetate, glycerol and Tris–HCl buffer. The crystals beong to the C2 space group, with unit-cell parameters a = 74.5, b = 81.9, c = 37.3 Å, α = γ = 90.0, β = 90.8°. The crystals diffract to 2.0 Å and a 94.2% complete data set to 2.2 Å has been collected from a single crystal with an R merge of 5.8%.

biologyProtein ConformationRecombinant Fusion ProteinsIntegrinIntegrin alpha1General MedicineCrystallography X-Raylaw.inventionCollagen receptorchemistry.chemical_compoundCrystallographychemistryStructural BiologylawAntigens CDDomain (ring theory)PEG ratioGlycerolbiology.proteinHumansCrystallizationCrystallizationSingle crystalSodium acetateActa crystallographica. Section D, Biological crystallography
researchProduct

Peptide–Membrane Interactions Monitored by Fluorescence Lifetime Imaging: A Study Case of Transportan 10

2021

The interest on detailed analysis of peptide-membrane interactions is of great interest in both fundamental and applied sciences as these may relate to both functional and pathogenic events. Such interactions are highly dynamic and spatially heterogeneous, making the investigation of the associated phenomena highly complex. The specific properties of membranes and peptide structural details, together with environmental conditions, may determine different events at the membrane interface, which will drive the fate of the peptide-membrane system. Here, we use an experimental approach based on the combination of spectroscopy and fluorescence microscopy methods to characterize the interactions …

chemistry.chemical_classificationFluorescence-lifetime imaging microscopyChemistryRecombinant Fusion ProteinsSpectrum AnalysisGalaninWasp VenomsPeptideSurfaces and InterfacesCondensed Matter PhysicsFluorescenceArticleMembraneMicroscopy FluorescenceAmphiphileElectrochemistryFluorescence microscopeHigh spatial resolutionBiophysicsPeptide−Membrane Interactions FLIM Transportan 10 PhasorGeneral Materials SciencePeptidesSpectroscopySpectroscopyLangmuir
researchProduct

Integrin-mediated Cell Adhesion to Type I Collagen Fibrils

2004

In the integrin family, the collagen receptors form a structurally and functionally distinct subgroup. Two members of this subgroup, α1β1 and α2β1 integrins, are known to bind to monomeric form of type I collagen. However, in tissues type I collagen monomers are organized into large fibrils immediately after they are released from cells. Here, we studied collagen fibril recognition by integrins. By an immunoelectron microscopy method we showed that integrin α2I domain is able to bind to classical D-banded type I collagen fibrils. However, according to the solid phase binding assay, the collagen fibril formation appeared to reduce integrin α1I and α2I domain avidity to collagen and to lower …

fibrilsIntegrinsintegrinRecombinant Fusion ProteinsImmunoelectron microscopyIntegrinCHO Cellsmacromolecular substancesIn Vitro TechniquesFibrilBiochemistryCollagen Type IIntegrin alpha1beta1Collagen receptorCricetinaeCell AdhesionAnimalsHumansMicroscopy ImmunoelectronCell adhesionMolecular BiologybiologyChemistryFibrillogenesisCell BiologycollagensCell biologyCollagen type I alpha 1Biochemistrybiology.proteinCattleIntegrin alpha2beta1Type I collagenJournal of Biological Chemistry
researchProduct

Hydrophobin (HFBI): a potential fusion partner for one-step purification of recombinant proteins from insect cells

2008

Hydrophobins play an important role in binding and assembly of fungal surface structures as well as in medium-air interactions. These, hydrophobic properties provide interesting possibilities when purification of macromolecules is concerned. In aqueous micellar two-phase systems, based on surfactants, the water soluble hydrophobins are concentrated inside micellar structures and, thus, distributed to defined aqueous phases. This, one-step purification is attractive particularly when large-scale production of recombinant proteins is concerned. In the present study the hydrophobin HFBI of Trichoderma reesei was expressed as an N-terminal fusion with chicken avidin in baculovirus infected inse…

hydrophobinaqueous micellar two-phase system (AMTPS)HydrophobinRecombinant Fusion ProteinsBlotting Westernfluorescence scanning microscopy (FSM)SpodopteraMicellesurfactantslaw.inventionFungal ProteinsPulmonary surfactantlawprotein purificationProtein purificationAnimalsMicellesTrichoderma reeseiTrichodermaMicroscopy Confocalbiologytechnology industry and agricultureAvidinbiology.organism_classificationBiochemistryCytoplasmRecombinant DNAbiology.proteinBaculoviridaeBiotechnologyAvidinProtein Expression and Purification
researchProduct

Activation of a murine autoreactive B cell by immunization with human recombinant autoantigen La/SS-B: Characterization of the autoepitope

1995

Immunization of Balb/c mice with a homogeneously purified recombinant human La/SS-B protein resulted in activation of an autoreactive B cell secreting a novel monoclonal anti-La antibody termed La4B6. La4B6 reacted with La protein from a variety of sources including human, bovine, rat and mouse. ATP blocked the binding of La4B6 to recombinant La protein. The human epitope was identified as consisting of the amino acid sequence SKGRRFKGKGKGN, which includes the proposed ATP-binding site of the La protein. In the human and bovine La protein, the epitope exists as a continuous amino acid sequence. In rat and mouse the epitope was found to consist of the amino acid sequence SKG interrupted by a…

medicine.drug_classRecombinant Fusion ProteinsImmunologyMolecular Sequence DataAutoimmunityBiologyMonoclonal antibodyAutoantigensPC12 CellsEpitopelaw.inventionCell LineMiceAdenosine TriphosphatelawmedicineImmunology and AllergyAnimalsHumansElméleti orvostudományokAmino Acid SequenceGeneralLiterature_REFERENCE(e.g.dictionariesencyclopediasglossaries)Peptide sequencechemistry.chemical_classificationB-LymphocytesMicroscopy ConfocalLinear epitopeOrvostudományok3T3 CellsMolecular biologyAmino acidRatschemistryMicroscopy FluorescenceRibonucleoproteinsRecombinant DNAbiology.proteinCattleImmunizationAntibodyEpitope MappingGene DeletionConformational epitope
researchProduct

Domains of the E1 Protein of Human Papillomavirus Type 33 Involved in Binding to the E2 Protein

1996

Papillomavirus E1 and E2 proteins are essential for the initiation of viral DNA replication. We have now analyzed the interaction of E1 and E2 of human papillomavirus type 33, which is associated with cervical carcinoma. When synthesized in insect cells using the baculovirus expression system, the E1 and E2 proteins interacted efficiently at 4 degree. A monoclonal antibody recognizing E1 amino acids 584--600 inhibited the binding of E2 and vice versa, indicating that these amino acids are involved in E2 binding. To confirm this result, a mutational analysis of E1 was performed. The E2 binding activity of E1 deletion and point mutant proteins was assayed using glutathione S-transferase E1 fu…

medicine.drug_classRecombinant Fusion ProteinsMolecular Sequence DataContext (language use)BiologySpodopteraMonoclonal antibodyAntibodies ViralCell Linechemistry.chemical_compoundMiceVirologymedicineTumor Cells CulturedAnimalsHumansPoint MutationPapillomaviridaeDNA PrimersGlutathione TransferaseSequence Deletionchemistry.chemical_classificationMice Inbred BALB CBase SequencePoint mutationTemperatureAntibodies MonoclonalGlutathioneOncogene Proteins ViralFusion proteinMolecular biologyIn vitroAmino acidchemistryEpitope MappingBinding domainProtein BindingVirology
researchProduct