AnatomyOrganismsDiseasesChemicals and DrugsAnalytical, Diagnostic and Therapeutic Techniques and EquipmentPhenomena and ProcessesInformation Science
Recombinant Fusion ProteinsMolecular Sequence DataAmino Acid SequenceRecombinant ProteinsCloning, MolecularEscherichia coliBase SequenceVaccines, SyntheticImmunotoxinsMembrane FusionEpitopesViral Fusion ProteinsCell FusionGenetic VectorsDNA, ComplementaryImmunoconjugatesCell LineProtein BindingSequence Homology, Amino AcidGlutathione TransferaseAntibodies, MonoclonalEnzyme-Linked Immunosorbent AssayGene ExpressionPlasmidsDNA PrimersMice, Inbred BALB CBlotting, WesternBinding SitesImmunoblottingElectrophoresis, Polyacrylamide GelBacterial ProteinsProtozoan ProteinsAntibody SpecificityImmunoglobulin GHepatocyte Nuclear Factor 3-betaDiphtheria ToxinMembrane GlycoproteinsAntigens, BacterialTumor Cells, CulturedPolymerase Chain ReactionAntibodies, BacterialAutoantibodiesOncogene Proteins, FusionKineticsMolecular WeightRabbitsCattleGene FusionSpinal FusionT-LymphocytesADP Ribose TransferasesProtein Structure, TertiaryTransfectionDNA, RecombinantGreen Fluorescent ProteinsPeptide FragmentsMembrane Fusion ProteinsCells, CulturedLuminescent ProteinsBacterial ToxinsMutationCricetinaeMaltose-Binding ProteinsMembrane ProteinsBaculoviridaeViral Envelope Proteinsbeta-GalactosidaseRecombination, GeneticCarrier ProteinsCercopithecus aethiopsViral ProteinsOncogene FusionMutagenesis, Site-DirectedProtein EngineeringCHO CellsCell MembraneHeLa CellsSpodopteraDNA-Binding ProteinsTranscription FactorsCOS CellsPeptidesVirus InternalizationTranscription, GeneticProtein ConformationRNA, MessengerImmunoglobulin Fc FragmentsRestriction MappingSubstrate SpecificitySaccharomyces cerevisiaeTranslocation, GeneticPichiaMicroscopy, FluorescenceGenes, BacterialDNAMice, Inbred C57BLSequence DeletionVesicular Transport ProteinsAquaporin 1Models, MolecularAntibodies, ViralProtein TransportGiant CellsVero Cells
Recombinant Fusion Proteins: Recombinant proteins produced by the GENETIC TRANSLATION of fused genes formed by the combination of NUCLEIC ACID REGULATORY SEQUENCES of one or more genes with the protein coding sequences of one or more genes.Molecular Sequence Data: Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.Amino Acid Sequence: The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.Recombinant Proteins: Proteins prepared by recombinant DNA technology.Cloning, Molecular: The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.Escherichia coli: A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.Base Sequence: The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.Vaccines, Synthetic: Small synthetic peptides that mimic surface antigens of pathogens and are immunogenic, or vaccines manufactured with the aid of recombinant DNA techniques. The latter vaccines may also be whole viruses whose nucleic acids have been modified.Immunotoxins: Semisynthetic conjugates of various toxic molecules, including RADIOACTIVE ISOTOPES and bacterial or plant toxins, with specific immune substances such as IMMUNOGLOBULINS; MONOCLONAL ANTIBODIES; and ANTIGENS. The antitumor or antiviral immune substance carries the toxin to the tumor or infected cell where the toxin exerts its poisonous effect.Membrane Fusion: The adherence and merging of cell membranes, intracellular membranes, or artificial membranes to each other or to viruses, parasites, or interstitial particles through a variety of chemical and physical processes.Epitopes: Sites on an antigen that interact with specific antibodies.Viral Fusion Proteins: Proteins, usually glycoproteins, found in the viral envelopes of a variety of viruses. They promote cell membrane fusion and thereby may function in the uptake of the virus by cells.Cell Fusion: Fusion of somatic cells in vitro or in vivo, which results in somatic cell hybridization.Genetic Vectors: DNA molecules capable of autonomous replication within a host cell and into which other DNA sequences can be inserted and thus amplified. Many are derived from PLASMIDS; BACTERIOPHAGES; or VIRUSES. They are used for transporting foreign genes into recipient cells. Genetic vectors possess a functional replicator site and contain GENETIC MARKERS to facilitate their selective recognition.DNA, Complementary: Single-stranded complementary DNA synthesized from an RNA template by the action of RNA-dependent DNA polymerase. cDNA (i.e., complementary DNA, not circular DNA, not C-DNA) is used in a variety of molecular cloning experiments as well as serving as a specific hybridization probe.Immunoconjugates: Combinations of diagnostic or therapeutic substances linked with specific immune substances such as IMMUNOGLOBULINS; MONOCLONAL ANTIBODIES; or ANTIGENS. Often the diagnostic or therapeutic substance is a radionuclide. These conjugates are useful tools for specific targeting of DRUGS and RADIOISOTOPES in the CHEMOTHERAPY and RADIOIMMUNOTHERAPY of certain cancers.Cell Line: Established cell cultures that have the potential to propagate indefinitely.Protein Binding: The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.Sequence Homology, Amino Acid: The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.Glutathione Transferase: A transferase that catalyzes the addition of aliphatic, aromatic, or heterocyclic FREE RADICALS as well as EPOXIDES and arene oxides to GLUTATHIONE. Addition takes place at the SULFUR. It also catalyzes the reduction of polyol nitrate by glutathione to polyol and nitrite.Antibodies, Monoclonal: Antibodies produced by a single clone of cells.Enzyme-Linked Immunosorbent Assay: An immunoassay utilizing an antibody labeled with an enzyme marker such as horseradish peroxidase. While either the enzyme or the antibody is bound to an immunosorbent substrate, they both retain their biologic activity; the change in enzyme activity as a result of the enzyme-antibody-antigen reaction is proportional to the concentration of the antigen and can be measured spectrophotometrically or with the naked eye. Many variations of the method have been developed.Gene Expression: The phenotypic manifestation of a gene or genes by the processes of GENETIC TRANSCRIPTION and GENETIC TRANSLATION.Plasmids: Extrachromosomal, usually CIRCULAR DNA molecules that are self-replicating and transferable from one organism to another. They are found in a variety of bacterial, archaeal, fungal, algal, and plant species. They are used in GENETIC ENGINEERING as CLONING VECTORS.DNA Primers: Short sequences (generally about 10 base pairs) of DNA that are complementary to sequences of messenger RNA and allow reverse transcriptases to start copying the adjacent sequences of mRNA. Primers are used extensively in genetic and molecular biology techniques.Mice, Inbred BALB CBlotting, Western: Identification of proteins or peptides that have been electrophoretically separated by blot transferring from the electrophoresis gel to strips of nitrocellulose paper, followed by labeling with antibody probes.Binding Sites: The parts of a macromolecule that directly participate in its specific combination with another molecule.Immunoblotting: Immunologic method used for detecting or quantifying immunoreactive substances. The substance is identified by first immobilizing it by blotting onto a membrane and then tagging it with labeled antibodies.Electrophoresis, Polyacrylamide Gel: Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.Bacterial Proteins: Proteins found in any species of bacterium.Protozoan Proteins: Proteins found in any species of protozoan.Antibody Specificity: The property of antibodies which enables them to react with some ANTIGENIC DETERMINANTS and not with others. Specificity is dependent on chemical composition, physical forces, and molecular structure at the binding site.Immunoglobulin G: The major immunoglobulin isotype class in normal human serum. There are several isotype subclasses of IgG, for example, IgG1, IgG2A, and IgG2B.Hepatocyte Nuclear Factor 3-beta: A forkhead transcription factor that regulates expression of metabolic GENES and is involved in EMBRYONIC DEVELOPMENT. Mutations in HNF-3beta have been associated with CONGENITAL HYPERINSULINISM.Diphtheria Toxin: An ADP-ribosylating polypeptide produced by CORYNEBACTERIUM DIPHTHERIAE that causes the signs and symptoms of DIPHTHERIA. It can be broken into two unequal domains: the smaller, catalytic A domain is the lethal moiety and contains MONO(ADP-RIBOSE) TRANSFERASES which transfers ADP RIBOSE to PEPTIDE ELONGATION FACTOR 2 thereby inhibiting protein synthesis; and the larger B domain that is needed for entry into cells.Membrane Glycoproteins: Glycoproteins found on the membrane or surface of cells.Antigens, Bacterial: Substances elaborated by bacteria that have antigenic activity.Tumor Cells, Cultured: Cells grown in vitro from neoplastic tissue. If they can be established as a TUMOR CELL LINE, they can be propagated in cell culture indefinitely.Polymerase Chain Reaction: In vitro method for producing large amounts of specific DNA or RNA fragments of defined length and sequence from small amounts of short oligonucleotide flanking sequences (primers). The essential steps include thermal denaturation of the double-stranded target molecules, annealing of the primers to their complementary sequences, and extension of the annealed primers by enzymatic synthesis with DNA polymerase. The reaction is efficient, specific, and extremely sensitive. Uses for the reaction include disease diagnosis, detection of difficult-to-isolate pathogens, mutation analysis, genetic testing, DNA sequencing, and analyzing evolutionary relationships.Antibodies, Bacterial: Immunoglobulins produced in a response to BACTERIAL ANTIGENS.Autoantibodies: Antibodies that react with self-antigens (AUTOANTIGENS) of the organism that produced them.Oncogene Proteins, Fusion: The GENETIC TRANSLATION products of the fusion between an ONCOGENE and another gene. The latter may be of viral or cellular origin.Kinetics: The rate dynamics in chemical or physical systems.Molecular Weight: The sum of the weight of all the atoms in a molecule.Rabbits: The species Oryctolagus cuniculus, in the family Leporidae, order LAGOMORPHA. Rabbits are born in burrows, furless, and with eyes and ears closed. In contrast with HARES, rabbits have 22 chromosome pairs.Cattle: Domesticated bovine animals of the genus Bos, usually kept on a farm or ranch and used for the production of meat or dairy products or for heavy labor.Gene Fusion: The GENETIC RECOMBINATION of the parts of two or more GENES resulting in a gene with different or additional regulatory regions, or a new chimeric gene product. ONCOGENE FUSION includes an ONCOGENE as at least one of the fusion partners and such gene fusions are often detected in neoplastic cells and are transcribed into ONCOGENE FUSION PROTEINS. ARTIFICIAL GENE FUSION is carried out in vitro by RECOMBINANT DNA technology.Spinal Fusion: Operative immobilization or ankylosis of two or more vertebrae by fusion of the vertebral bodies with a short bone graft or often with diskectomy or laminectomy. (From Blauvelt & Nelson, A Manual of Orthopaedic Terminology, 5th ed, p236; Dorland, 28th ed)T-Lymphocytes: Lymphocytes responsible for cell-mediated immunity. Two types have been identified - cytotoxic (T-LYMPHOCYTES, CYTOTOXIC) and helper T-lymphocytes (T-LYMPHOCYTES, HELPER-INDUCER). They are formed when lymphocytes circulate through the THYMUS GLAND and differentiate to thymocytes. When exposed to an antigen, they divide rapidly and produce large numbers of new T cells sensitized to that antigen.ADP Ribose Transferases: Enzymes that transfer the ADP-RIBOSE group of NAD or NADP to proteins or other small molecules. Transfer of ADP-ribose to water (i.e., hydrolysis) is catalyzed by the NADASES. The mono(ADP-ribose)transferases transfer a single ADP-ribose. POLY(ADP-RIBOSE) POLYMERASES transfer multiple units of ADP-ribose to protein targets, building POLY ADENOSINE DIPHOSPHATE RIBOSE in linear or branched chains.Protein Structure, Tertiary: The level of protein structure in which combinations of secondary protein structures (alpha helices, beta sheets, loop regions, and motifs) pack together to form folded shapes called domains. Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure. Small proteins usually consist of only one domain but larger proteins may contain a number of domains connected by segments of polypeptide chain which lack regular secondary structure.Transfection: The uptake of naked or purified DNA by CELLS, usually meaning the process as it occurs in eukaryotic cells. It is analogous to bacterial transformation (TRANSFORMATION, BACTERIAL) and both are routinely employed in GENE TRANSFER TECHNIQUES.DNA, Recombinant: Biologically active DNA which has been formed by the in vitro joining of segments of DNA from different sources. It includes the recombination joint or edge of a heteroduplex region where two recombining DNA molecules are connected.Green Fluorescent Proteins: Protein analogs and derivatives of the Aequorea victoria green fluorescent protein that emit light (FLUORESCENCE) when excited with ULTRAVIOLET RAYS. They are used in REPORTER GENES in doing GENETIC TECHNIQUES. Numerous mutants have been made to emit other colors or be sensitive to pH.Peptide Fragments: Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques.Membrane Fusion Proteins: Proteins that catalyze MEMBRANE FUSION.Cells, Cultured: Cells propagated in vitro in special media conducive to their growth. Cultured cells are used to study developmental, morphologic, metabolic, physiologic, and genetic processes, among others.Luminescent Proteins: Proteins which are involved in the phenomenon of light emission in living systems. Included are the "enzymatic" and "non-enzymatic" types of system with or without the presence of oxygen or co-factors.Bacterial Toxins: Toxic substances formed in or elaborated by bacteria; they are usually proteins with high molecular weight and antigenicity; some are used as antibiotics and some to skin test for the presence of or susceptibility to certain diseases.Mutation: Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.Cricetinae: A subfamily in the family MURIDAE, comprising the hamsters. Four of the more common genera are Cricetus, CRICETULUS; MESOCRICETUS; and PHODOPUS.Maltose-Binding Proteins: Periplasmic proteins that bind MALTOSE and maltodextrin. They take part in the maltose transport system of BACTERIA.Membrane Proteins: Proteins which are found in membranes including cellular and intracellular membranes. They consist of two types, peripheral and integral proteins. They include most membrane-associated enzymes, antigenic proteins, transport proteins, and drug, hormone, and lectin receptors.Baculoviridae: Family of INSECT VIRUSES containing two subfamilies: Eubaculovirinae (occluded baculoviruses) and Nudibaculovirinae (nonoccluded baculoviruses). The Eubaculovirinae, which contain polyhedron-shaped inclusion bodies, have two genera: NUCLEOPOLYHEDROVIRUS and GRANULOVIRUS. Baculovirus vectors are used for expression of foreign genes in insects.Viral Envelope Proteins: Layers of protein which surround the capsid in animal viruses with tubular nucleocapsids. The envelope consists of an inner layer of lipids and virus specified proteins also called membrane or matrix proteins. The outer layer consists of one or more types of morphological subunits called peplomers which project from the viral envelope; this layer always consists of glycoproteins.beta-Galactosidase: A group of enzymes that catalyzes the hydrolysis of terminal, non-reducing beta-D-galactose residues in beta-galactosides. Deficiency of beta-Galactosidase A1 may cause GANGLIOSIDOSIS, GM1.Recombination, Genetic: Production of new arrangements of DNA by various mechanisms such as assortment and segregation, CROSSING OVER; GENE CONVERSION; GENETIC TRANSFORMATION; GENETIC CONJUGATION; GENETIC TRANSDUCTION; or mixed infection of viruses.Carrier Proteins: Transport proteins that carry specific substances in the blood or across cell membranes.Cercopithecus aethiops: A species of CERCOPITHECUS containing three subspecies: C. tantalus, C. pygerythrus, and C. sabeus. They are found in the forests and savannah of Africa. The African green monkey (C. pygerythrus) is the natural host of SIMIAN IMMUNODEFICIENCY VIRUS and is used in AIDS research.Viral Proteins: Proteins found in any species of virus.Oncogene Fusion: The GENETIC RECOMBINATION of the parts of two or more GENES, including an ONCOGENE as at least one of the fusion partners. Such gene fusions are often detected in neoplastic cells and are transcribed into ONCOGENE FUSION PROTEINS.Mutagenesis, Site-Directed: Genetically engineered MUTAGENESIS at a specific site in the DNA molecule that introduces a base substitution, or an insertion or deletion.Protein Engineering: Procedures by which protein structure and function are changed or created in vitro by altering existing or synthesizing new structural genes that direct the synthesis of proteins with sought-after properties. Such procedures may include the design of MOLECULAR MODELS of proteins using COMPUTER GRAPHICS or other molecular modeling techniques; site-specific mutagenesis (MUTAGENESIS, SITE-SPECIFIC) of existing genes; and DIRECTED MOLECULAR EVOLUTION techniques to create new genes.CHO Cells: CELL LINE derived from the ovary of the Chinese hamster, Cricetulus griseus (CRICETULUS). The species is a favorite for cytogenetic studies because of its small chromosome number. The cell line has provided model systems for the study of genetic alterations in cultured mammalian cells.Cell Membrane: The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.HeLa Cells: The first continuously cultured human malignant CELL LINE, derived from the cervical carcinoma of Henrietta Lacks. These cells are used for VIRUS CULTIVATION and antitumor drug screening assays.Spodoptera: A genus of owlet moths of the family Noctuidae. These insects are used in molecular biology studies during all stages of their life cycle.DNA-Binding Proteins: Proteins which bind to DNA. The family includes proteins which bind to both double- and single-stranded DNA and also includes specific DNA binding proteins in serum which can be used as markers for malignant diseases.Transcription Factors: Endogenous substances, usually proteins, which are effective in the initiation, stimulation, or termination of the genetic transcription process.COS Cells: CELL LINES derived from the CV-1 cell line by transformation with a replication origin defective mutant of SV40 VIRUS, which codes for wild type large T antigen (ANTIGENS, POLYOMAVIRUS TRANSFORMING). They are used for transfection and cloning. (The CV-1 cell line was derived from the kidney of an adult male African green monkey (CERCOPITHECUS AETHIOPS).)Peptides: Members of the class of compounds composed of AMINO ACIDS joined together by peptide bonds between adjacent amino acids into linear, branched or cyclical structures. OLIGOPEPTIDES are composed of approximately 2-12 amino acids. Polypeptides are composed of approximately 13 or more amino acids. PROTEINS are linear polypeptides that are normally synthesized on RIBOSOMES.Virus Internalization: The entering of cells by viruses following VIRUS ATTACHMENT. This is achieved by ENDOCYTOSIS, by direct MEMBRANE FUSION of the viral membrane with the CELL MEMBRANE, or by translocation of the whole virus across the cell membrane.Transcription, Genetic: The biosynthesis of RNA carried out on a template of DNA. The biosynthesis of DNA from an RNA template is called REVERSE TRANSCRIPTION.Protein Conformation: The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).RNA, Messenger: RNA sequences that serve as templates for protein synthesis. Bacterial mRNAs are generally primary transcripts in that they do not require post-transcriptional processing. Eukaryotic mRNA is synthesized in the nucleus and must be exported to the cytoplasm for translation. Most eukaryotic mRNAs have a sequence of polyadenylic acid at the 3' end, referred to as the poly(A) tail. The function of this tail is not known for certain, but it may play a role in the export of mature mRNA from the nucleus as well as in helping stabilize some mRNA molecules by retarding their degradation in the cytoplasm.Immunoglobulin Fc Fragments: Crystallizable fragments composed of the carboxy-terminal halves of both IMMUNOGLOBULIN HEAVY CHAINS linked to each other by disulfide bonds. Fc fragments contain the carboxy-terminal parts of the heavy chain constant regions that are responsible for the effector functions of an immunoglobulin (COMPLEMENT fixation, binding to the cell membrane via FC RECEPTORS, and placental transport). This fragment can be obtained by digestion of immunoglobulins with the proteolytic enzyme PAPAIN.Restriction Mapping: Use of restriction endonucleases to analyze and generate a physical map of genomes, genes, or other segments of DNA.Substrate Specificity: A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.Saccharomyces cerevisiae: A species of the genus SACCHAROMYCES, family Saccharomycetaceae, order Saccharomycetales, known as "baker's" or "brewer's" yeast. The dried form is used as a dietary supplement.Translocation, Genetic: A type of chromosome aberration characterized by CHROMOSOME BREAKAGE and transfer of the broken-off portion to another location, often to a different chromosome.Pichia: Yeast-like ascomycetous fungi of the family Saccharomycetaceae, order SACCHAROMYCETALES isolated from exuded tree sap.Microscopy, Fluorescence: Microscopy of specimens stained with fluorescent dye (usually fluorescein isothiocyanate) or of naturally fluorescent materials, which emit light when exposed to ultraviolet or blue light. Immunofluorescence microscopy utilizes antibodies that are labeled with fluorescent dye.Genes, Bacterial: The functional hereditary units of BACTERIA.DNA: A deoxyribonucleotide polymer that is the primary genetic material of all cells. Eukaryotic and prokaryotic organisms normally contain DNA in a double-stranded state, yet several important biological processes transiently involve single-stranded regions. DNA, which consists of a polysugar-phosphate backbone possessing projections of purines (adenine and guanine) and pyrimidines (thymine and cytosine), forms a double helix that is held together by hydrogen bonds between these purines and pyrimidines (adenine to thymine and guanine to cytosine).Mice, Inbred C57BLSequence Deletion: Deletion of sequences of nucleic acids from the genetic material of an individual.Vesicular Transport Proteins: A broad category of proteins involved in the formation, transport and dissolution of TRANSPORT VESICLES. They play a role in the intracellular transport of molecules contained within membrane vesicles. Vesicular transport proteins are distinguished from MEMBRANE TRANSPORT PROTEINS, which move molecules across membranes, by the mode in which the molecules are transported.Aquaporin 1: Aquaporin 1 forms a water-specific channel that is constitutively expressed at the PLASMA MEMBRANE of ERYTHROCYTES and KIDNEY TUBULES, PROXIMAL. It provides these cells with a high permeability to WATER. In humans polymorphisms of this protein result in the Colton blood group antigen.Models, Molecular: Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.Antibodies, Viral: Immunoglobulins produced in response to VIRAL ANTIGENS.Protein Transport: The process of moving proteins from one cellular compartment (including extracellular) to another by various sorting and transport mechanisms such as gated transport, protein translocation, and vesicular transport.Giant Cells: Multinucleated masses produced by the fusion of many cells; often associated with viral infections. In AIDS, they are induced when the envelope glycoprotein of the HIV virus binds to the CD4 antigen of uninfected neighboring T4 cells. The resulting syncytium leads to cell death and thus may account for the cytopathic effect of the virus.Vero Cells: A CELL LINE derived from the kidney of the African green (vervet) monkey, (CERCOPITHECUS AETHIOPS) used primarily in virus replication studies and plaque assays.

VEGF is required for growth and survival in neonatal mice. (1/41883)

We employed two independent approaches to inactivate the angiogenic protein VEGF in newborn mice: inducible, Cre-loxP- mediated gene targeting, or administration of mFlt(1-3)-IgG, a soluble VEGF receptor chimeric protein. Partial inhibition of VEGF achieved by inducible gene targeting resulted in increased mortality, stunted body growth and impaired organ development, most notably of the liver. Administration of mFlt(1-3)-IgG, which achieves a higher degree of VEGF inhibition, resulted in nearly complete growth arrest and lethality. Ultrastructural analysis documented alterations in endothelial and other cell types. Histological and biochemical changes consistent with liver and renal failure were observed. Endothelial cells isolated from the liver of mFlt(1-3)-IgG-treated neonates demonstrated an increased apoptotic index, indicating that VEGF is required not only for proliferation but also for survival of endothelial cells. However, such treatment resulted in less significant alterations as the animal matured, and the dependence on VEGF was eventually lost some time after the fourth postnatal week. Administration of mFlt(1-3)-IgG to juvenile mice failed to induce apoptosis in liver endothelial cells. Thus, VEGF is essential for growth and survival in early postnatal life. However, in the fully developed animal, VEGF is likely to be involved primarily in active angiogenesis processes such as corpus luteum development.  (+info)

Cell polarization: chemotaxis gets CRACKing. (2/41883)

An early stage in the establishment of cell polarity during chemotaxis of Dictyostelium dicoideum has been identified by a recent study; the new results also show that the development of cell polarity does not rely upon cytoskeletal rearrangement, and may use a spatial sensing mechanism.  (+info)

Deletion analysis of the Drosophila Inscuteable protein reveals domains for cortical localization and asymmetric localization. (3/41883)

The Drosophila Inscuteable protein acts as a key regulator of asymmetric cell division during the development of the nervous system [1] [2]. In neuroblasts, Inscuteable localizes into an apical cortical crescent during late interphase and most of mitosis. During mitosis, Inscuteable is required for the correct apical-basal orientation of the mitotic spindle and for the asymmetric segregation of the proteins Numb [3] [4] [5], Prospero [5] [6] [7] and Miranda [8] [9] into the basal daughter cell. When Inscuteable is ectopically expressed in epidermal cells, which normally orient their mitotic spindle parallel to the embryo surface, these cells reorient their mitotic spindle and divide perpendicularly to the surface [1]. Like the Inscuteable protein, the inscuteable RNA is asymmetrically localized [10]. We show here that inscuteable RNA localization is not required for Inscuteable protein localization. We found that a central 364 amino acid domain - the Inscuteable asymmetry domain - was necessary and sufficient for Inscuteable localization and function. Within this domain, a separate 100 amino acid region was required for asymmetric localization along the cortex, whereas a 158 amino acid region directed localization to the cell cortex. The same 158 amino acid fragment could localize asymmetrically when coexpressed with the full-length protein, however, and could bind to Inscuteable in vitro, suggesting that this domain may be involved in the self-association of Inscuteable in vivo.  (+info)

Bcl-2 regulates amplification of caspase activation by cytochrome c. (4/41883)

Caspases, a family of specific proteases, have central roles in apoptosis [1]. Caspase activation in response to diverse apoptotic stimuli involves the relocalisation of cytochrome c from mitochondria to the cytoplasm where it stimulates the proteolytic processing of caspase precursors. Cytochrome c release is controlled by members of the Bcl-2 family of apoptosis regulators [2] [3]. The anti-apoptotic members Bcl-2 and Bcl-xL may also control caspase activation independently of cytochrome c relocalisation or may inhibit a positive feedback mechanism [4] [5] [6] [7]. Here, we investigate the role of Bcl-2 family proteins in the regulation of caspase activation using a model cell-free system. We found that Bcl-2 and Bcl-xL set a threshold in the amount of cytochrome c required to activate caspases, even in soluble extracts lacking mitochondria. Addition of dATP (which stimulates the procaspase-processing factor Apaf-1 [8] [9]) overcame inhibition of caspase activation by Bcl-2, but did not prevent the control of cytochrome c release from mitochondria by Bcl-2. Cytochrome c release was accelerated by active caspase-3 and this positive feedback was negatively regulated by Bcl-2. These results provide evidence for a mechanism to amplify caspase activation that is suppressed at several distinct steps by Bcl-2, even after cytochrome c is released from mitochondria.  (+info)

Plasma membrane recruitment of RalGDS is critical for Ras-dependent Ral activation. (5/41883)

In COS cells, Ral GDP dissociation stimulator (RalGDS)-induced Ral activation was stimulated by RasG12V or a Rap1/Ras chimera in which the N-terminal region of Rap1 was ligated to the C-terminal region of Ras but not by Rap1G12V or a Ras/Rap1 chimera in which the N-terminal region of Ras was ligated to the C-terminal region of Rap1, although RalGDS interacted with these small GTP-binding proteins. When RasG12V, Ral and the Rap1/Ras chimera were individually expressed in NIH3T3 cells, they localized to the plasma membrane. Rap1Q63E and the Ras/Rap1 chimera were detected in the perinuclear region. When RalGDS was expressed alone, it was abundant in the cytoplasm. When coexpressed with RasG12V or the Rap1/Ras chimera, RalGDS was detected at the plasma membrane, whereas when coexpressed with Rap1Q63E or the Ras/Rap1 chimera, RalGDS was observed in the perinuclear region. RalGDS which was targeted to the plasma membrane by the addition of Ras farnesylation site (RalGDS-CAAX) activated Ral in the absence of RasG12V. Although RalGDS did not stimulate the dissociation of GDP from Ral in the absence of the GTP-bound form of Ras in a reconstitution assay using the liposomes, RalGDS-CAAX could stimulate it without Ras. RasG12V activated Raf-1 when they were coexpressed in Sf9 cells, whereas RasG12V did not affect the RalGDS activity. These results indicate that Ras recruits RalGDS to the plasma membrane and that the translocated RalGDS induces the activation of Ral, but that Rap1 does not activate Ral due to distinct subcellular localization.  (+info)

B-MYB transactivates its own promoter through SP1-binding sites. (6/41883)

B-MYB is an ubiquitous protein required for mammalian cell growth. In this report we show that B-MYB transactivates its own promoter through a 120 bp segment proximal to the transcription start site. The B-MYB-responsive element does not contain myb-binding sites and gel-shift analysis shows that SP1, but not B-MYB, protein contained in SAOS2 cell extracts binds to the 120 bp B-myb promoter fragment. B-MYB-dependent transactivation is cooperatively increased in the presence of SP1, but not SP3 overexpression. When the SP1 elements of the B-myb promoter are transferred in front of a heterologous promoter, an increased response to B-MYB results. In contrast, c-MYB, the prototype member of the Myb family, is not able to activate the luciferase construct containing the SP1 elements. With the use of an SP1-GAL4 fusion protein, we have determined that the cooperative activation occurs through the domain A of SP1. These observations suggest that B-MYB functions as a coactivator of SP1, and that diverse combinations of myb and SP1 sites may dictate the responsiveness of myb-target genes to the various members of the myb family.  (+info)

A single membrane-embedded negative charge is critical for recognizing positively charged drugs by the Escherichia coli multidrug resistance protein MdfA. (7/41883)

The nature of the broad substrate specificity phenomenon, as manifested by multidrug resistance proteins, is not yet understood. In the Escherichia coli multidrug transporter, MdfA, the hydrophobicity profile and PhoA fusion analysis have so far identified only one membrane-embedded charged amino acid residue (E26). In order to determine whether this negatively charged residue may play a role in multidrug recognition, we evaluated the expression and function of MdfA constructs mutated at this position. Replacing E26 with the positively charged residue lysine abolished the multidrug resistance activity against positively charged drugs, but retained chloramphenicol efflux and resistance. In contrast, when the negative charge was preserved in a mutant with aspartate instead of E26, chloramphenicol recognition and transport were drastically inhibited; however, the mutant exhibited almost wild-type multidrug resistance activity against lipophilic cations. These results suggest that although the negative charge at position 26 is not essential for active transport, it dictates the multidrug resistance character of MdfA. We show that such a negative charge is also found in other drug resistance transporters, and its possible significance regarding multidrug resistance is discussed.  (+info)

Assembly requirements of PU.1-Pip (IRF-4) activator complexes: inhibiting function in vivo using fused dimers. (8/41883)

Gene expression in higher eukaryotes appears to be regulated by specific combinations of transcription factors binding to regulatory sequences. The Ets factor PU.1 and the IRF protein Pip (IRF-4) represent a pair of interacting transcription factors implicated in regulating B cell-specific gene expression. Pip is recruited to its binding site on DNA by phosphorylated PU.1. PU.1-Pip interaction is shown to be template directed and involves two distinct protein-protein interaction surfaces: (i) the ets and IRF DNA-binding domains; and (ii) the phosphorylated PEST region of PU.1 and a lysine-requiring putative alpha-helix in Pip. Thus, a coordinated set of protein-protein and protein-DNA contacts are essential for PU.1-Pip ternary complex assembly. To analyze the function of these factors in vivo, we engineered chimeric repressors containing the ets and IRF DNA-binding domains connected by a flexible POU domain linker. When stably expressed, the wild-type fused dimer strongly repressed the expression of a rearranged immunoglobulin lambda gene, thereby establishing the functional importance of PU.1-Pip complexes in B cell gene expression. Comparative analysis of the wild-type dimer with a series of mutant dimers distinguished a gene regulated by PU.1 and Pip from one regulated by PU.1 alone. This strategy should prove generally useful in analyzing the function of interacting transcription factors in vivo, and for identifying novel genes regulated by such complexes.  (+info)

Studying the role of rhBAFF and BAFF R Fc fusion protein on lymphocytes and platelets in patients with immune thrombocytopenia ...Studying the role of rhBAFF and BAFF R Fc fusion protein on lymphocytes and platelets in patients with immune thrombocytopenia ...
Thesis, English, Studying the role of rhBAFF and BAFF R Fc fusion protein on lymphocytes and platelets in patients with immune thrombocytopenia for Nouran Mohamed Nabil Momen
High level transient production of recombinant antibodies and antibody fusion proteins in HEK293 cells | BMC Biotechnology |...High level transient production of recombinant antibodies and antibody fusion proteins in HEK293 cells | BMC Biotechnology |...
The demand of monospecific high affinity binding reagents, particularly monoclonal antibodies, has been steadily increasing over the last years. Enhanced throughput of antibody generation has been addressed by optimizing in vitro selection using phage display which moved the major bottleneck to the production and purification of recombinant antibodies in an end-user friendly format. Single chain (sc)Fv antibody fragments require additional tags for detection and are not as suitable as immunoglobulins (Ig)G in many immunoassays. In contrast, the bivalent scFv-Fc antibody format shares many properties with IgG and has a very high application compatibility. In this study transient expression of scFv-Fc antibodies in human embryonic kidney (HEK) 293 cells was optimized. Production levels of 10-20 mg/L scFv-Fc antibody were achieved in adherent HEK293T cells. Employment of HEK293-6E suspension cells expressing a truncated variant of the Epstein Barr virus (EBV) nuclear antigen (EBNA) 1 in combination with
Chimeric human fcgamma-allergen fusion proteins in the prevention of allergy, NC DOCKS (North Carolina Digital Online...Chimeric human fcgamma-allergen fusion proteins in the prevention of allergy, NC DOCKS (North Carolina Digital Online...
Abstract: Allergic responses are strongly associated with Th2-type immune responses, and modulation of the skewed Th2 response toward a more balanced response is the major goal of allergen immunotherapy (IT) in allergic disorders. To achieve this goal, several approaches have been tested. The authors previously showed that a human immunoglobulin (Ig) Fcg-Fce fusion protein (GE2) that directly cross-links FceRI and FcgRIIb on human mast cells and basophils was able to inhibit degranulation, and they reasoned that human gamma-allergen fusion protein would achieve a similar inhibitory effect in an allergen-specific fashion while preserving the immunogenicity of the allergen component. Therefore, the authors constructed and developed a human-cat chimeric fusion protein composed of the human Fcg1 and the cat allergen Fel d1 (Felis domesticus) for cat allergen-specific IT. This article summarizes the therapeutic features and potential of this novel fusion protein for allergic IT.. Chimeric human ...
Phase I study of bintrafusp alfa, a bifunctional fusion protein targeting TGF-β and PD-L1, in patients with pretreated biliary...Phase I study of bintrafusp alfa, a bifunctional fusion protein targeting TGF-β and PD-L1, in patients with pretreated biliary...
Phase I study of bintrafusp alfa, a bifunctional fusion protein targeting TGF-β and PD-L1, in patients with pretreated biliary tract cancer ...
A Yeast Platform for the Production of Single-Chain Antibody-Green Fluorescent Protein Fusions | Applied and Environmental...A Yeast Platform for the Production of Single-Chain Antibody-Green Fluorescent Protein Fusions | Applied and Environmental...
The goals of this study were to build a yeast platform for the secretion of a variety of scFv/scTCR GFP fusion proteins and to understand the effects that fusion protein construction can have on intracellular fusion protein processing. A large collection of 27 GFP fusion proteins having scFv/scTCR fusion partners representative of a wide range of secretion fitnesses was analyzed. It was discovered that the fusion secretion levels were governed by scFv/scTCR secretion fitness, rather than by GFP, linker length, or fusion orientation. In addition, type III fusions were the most fluorescent with the least amount of observed degradation, and therefore, they represent the recommended construct for secretion of GFP fusions from yeast. Finally, fusion to GFP clearly affected the intracellular processing of the scFv/scTCR, and in particular helped promote the exit of mature protein from the cell. Finally, large amounts of fully active fusion protein accumulated inside the cell as a result of secretory ...
Levicept Starts First-in-Human Phase I Trial of LEVI-04, A Novel Fusion Protein Therapy for Chronic Pain | Neuigkeiten | Gilde...Levicept Starts First-in-Human Phase I Trial of LEVI-04, A Novel Fusion Protein Therapy for Chronic Pain | Neuigkeiten | Gilde...
Sandwich, UK -- Levicept Ltd., an asset-centric biotechnology company focused on the development of LEVI-04, a first-in-class treatment for chronic pain indications,…
fusion protein expressionfusion protein expression
Dear netters, I am a PhD student in Japan. I am facing some problems in expressing my fusion proteins (both GST-fusions and His-tag fusions) in soluble fractions; therefore I decided to use the TNT-coupled recticulocyte system to synthesis the desired proteins. I need to use these fusion proteins for the following assay: (i) protein interaction - pull down assay (ii) in-vitro kinase assay My questions are: (i) how to purify the translated product from the TNT- coupled recticulocyte system? (ii) Are there any references for the above assays (pull down assay & in-vitro kinase assay) using both in-vitro translated fusion proteins? Your help are kindly appreciated. Thank you. sincerely, YK ...
Production of anti-breast cancer monoclonal antibodies using a glutathione-S-transferase-MUC1 bacterial fusion protein. ...Production of anti-breast cancer monoclonal antibodies using a glutathione-S-transferase-MUC1 bacterial fusion protein. ...
Two murine Mabs VA1(IgG1) and VA2(IgG1) were produced against a bacterial fusion protein comprising glutathione S-transferase and five tandem repeats of the MUC1 protein. Using the immunoperoxidase staining technique, VA1 detected 46/53 and VA2 detected 48/53 breast cancers and both also reacted wit...
Patent US6242570 - Production and use of recombinant protein multimers with increased ... - Google PatentsPatent US6242570 - Production and use of recombinant protein multimers with increased ... - Google Patents
The invention relates to novel recombinant fusion proteins comprising two or more erythropoietin molecules. The fusion proteins can be linked by a peptide linker. The fusion proteins can be used, for example, to treat or prevent anemia in a mammal. Also disclosed are nucleotide sequences encoding the fusion proteins vectors comprising the nucleic acid sequences of the fusion proteins and host cells transfected with the vectors.
flag-vector-info | China-Mainland | Sigma-Aldrichflag-vector-info | China-Mainland | Sigma-Aldrich
The FLAG Expression System is an established way to express, purify and detect recombinant fusion proteins. FLAG and 3xFLAG have proven utility in numerous applications such as Western blotting, immunocytochemistry, immunoprecipitation, flow cytometry, protein purification, and in the study of protein-protein interactions, cell ultrastructure and protein localization. These small hydrophilic tags facilitate superior detection and purification of recombinant fusion proteins when using our highly specific and sensitive ANTI-FLAG® antibodies. Ideal epitope tags are small, hydrophilic and cleavable.. The FLAG expression system utilizes a short, hydrophilic 8-amino acid peptide that is fused to the recombinant protein of interest. Because of its hydrophilic nature, the FLAG peptide is likely to be located on the surface of the fusion protein. As a result, the FLAG peptide is easily accessible for cleavage by enterokinase (Ek) and for detection with antibodies. In addition, because of the small size ...
Purification tags/Protein tag|UCBMSH.ORGPurification tags/Protein tag|UCBMSH.ORG
Purification tags/Protein tag,Protein tags are peptide sequences genetically grafted onto a recombinant protein. Often these tags are removable by chemical agents or by enzymatic means, such as proteolysis or intein splicing. Tags are attached to proteins for various purposes.
Dr. Roland Strong - Institute for Protein DesignDr. Roland Strong - Institute for Protein Design
Website: http://labs.fhcrc.org/strong/. Tailoring immunotargeting and immunomodulatory reagents for the treatment of cancer. This project builds on two ongoing efforts: (1) to specifically elicit, customize and weaponize antibodies to target solid tumors induced by viruses and (2) to translate immunomodulators that target T cell co-receptor signaling pathways from canine to human patients for managing the sequelae of treatments for hematopoietic tumors. Antibodies are clinically-relevant reagents for treating various diseases, though often require chemical conjugation to generate useful diagnostics or therapeutics. We are developing novel antibody fusion proteins, adding functional modules that enable simple, plug-and-play, non-covalent incorporation of a variety of adducts. We are also developing improved versions of MHC proteins as immunogens to efficiently elicit antibodies specific for virally-infected cells. Computational refinement of initial designs is required to fully realize these ...
DTGM Fusion Protein in Treating Patients With Recurrent or Refractory Acute Myeloid LeukemiaDTGM Fusion Protein in Treating Patients With Recurrent or Refractory Acute Myeloid Leukemia
RATIONALE: DTGM fusion protein may be able to locate cancer cells and stop them from growing. PURPOSE: Phase I/II trial to study the effectivenes
how to purify fusion proteins on a large scale? - Protein and Proteomicshow to purify fusion proteins on a large scale? - Protein and Proteomics
i want to understand also how to determine which OD to start my IPTG induction in? and when to say its time to stop when OD reaches 2 ...
Degradation of GST fusion proteins - Molecular BiologyDegradation of GST fusion proteins - Molecular Biology
I clone GST fusion proteins with pGEX 4T-3 vector, I check for inserts in minipreps (OK), grow bacteria, induce them, and run lysates on SDS-PAGE. What happens is that the expressed proteins are of GST size, probably degraded. Has anyone got that kind of results before? I checked DNA, its OK, no stop codons at the ligation site.. ...
Monoclonal antibody against GST fusion proteinMonoclonal antibody against GST fusion protein
I am attemptting to make a monoclonal antibody aganist a GST fusion protein ( 34 kDa). I am wondering if anybody outthere can tell me how much purified antigen I need to use for each immunization, and how much antigen I have to use for coding the plates for screening. Thank you, Qiang ...
Chimerigen LaboratoriesChimerigen Laboratories
Since many years Chimerigen Laboratories, LLC (Chimerigen) develops, manufactures and markets high quality and leading edge proteins for biomedical and immunology research. One of Chimerigens specialty is the production of unique immunoglobulin based chimeric fusion proteins using advanced cellular and molecular biological techniques.
SMART: B41 domain annotationSMART: B41 domain annotation
The ERM proteins, ezrin, radixin, and moesin, are involved in the actin filament/plasma membrane interaction as cross-linkers. CD44 has been identified as one of the major membrane binding partners for ERM proteins. To examine the CD44/ERM protein interaction in vitro, we produced mouse ezrin, radixin, moesin, and the glutathione-S-transferase (GST)/CD44 cytoplasmic domain fusion protein (GST-CD44cyt) by means of recombinant baculovirus infection, and constructed an in vitro assay for the binding between ERM proteins and the cytoplasmic domain of CD44. In this system, ERM proteins bound to GST-CD44cyt with high affinity (Kd of moesin was 9.3 +/- 1.6nM) at a low ionic strength, but with low affinity at a physiological ionic strength. However, in the presence of phosphoinositides (phosphatidylinositol [PI], phosphatidylinositol 4-monophosphate [4-PIP], and phosphatidylinositol 4.5-bisphosphate [4,5-PIP2]), ERM proteins bound with a relatively high affinity to GST-CD44cyt even at a physiological ...
Recombinant Human VISTA/B7-H5/PD-1H Fc Chimera Protein, CF 7126-B7-050: R&D SystemsRecombinant Human VISTA/B7-H5/PD-1H Fc Chimera Protein, CF 7126-B7-050: R&D Systems
Human VISTA / B7-H5 / PD-1H protein (7126-B7) is manufactured by R&D Systems, over 95% purity. Reproducible results in bioactivity assays. Learn More...
Recombinant Human Vasorin/SLIT-like 2 Fc Chimera Protein, CF 10139-VN-050: R&D SystemsRecombinant Human Vasorin/SLIT-like 2 Fc Chimera Protein, CF 10139-VN-050: R&D Systems
Human Vasorin / SLIT-like 2 protein (10139-VN) is manufactured by R&D Systems, over 95% purity. Reproducible results in bioactivity assays. Learn More...
Protein Therapy Alternative to ChemotherapyProtein Therapy Alternative to Chemotherapy
new growths elsewhere in the body, a process known as metastasis that can cause cancer to spread with deadly effect, the findings showed. "This is a very promising therapy that appears to be effective and non-toxic in pre-clinical experiments," said co-researcher Amato Giaccia, a professor at the Stanford University in the US. "It could open up a new approach to cancer treatment," Giaccia added. Today doctors try to slow or stop metastasis with chemotherapy, but these treatments are unfortunately not very effective and have severe side effects. The researchers sought to stop metastasis by preventing two proteins - Axl and Gas6 - from interacting to initiate the spread of cancer. Axl proteins stand like bristles on the surface of cancer cells, poised to receive bio-chemical signals from Gas6 proteins. When two Gas6 proteins link with two Axls, the signals that are generated enable cancer cells to leave the original tumor site, migrate to other parts of the body and form new cancer nodules ...
Protein therapy development for RDEBProtein therapy development for RDEB
In a preclinical study, researchers at the University of Southern California evaluated whether human Collagen 7 that had been produced in the lab, when applied to mouse skin, could restore the missing protein in the skin and enhance wound healing.. They found that the Collagen 7 applied to the surface of the mouse skin was incorporated stably at the newly formed junction between the dermis and epidermis of healed wounds. It accelerated wound closure by increasing the formation of new epithelium (skin). It also led to reduced scarring and had other positive impacts. ...
Gentaur Molecular :Clemente Associates Inc \ FUSION PROTEIN TAGS Anti FLAG M1 \ flgm1250Gentaur Molecular :Clemente Associates Inc \ FUSION PROTEIN TAGS Anti FLAG M1 \ flgm1250
Gentaur molecular products has all kinds of products like :search , Clemente Associates Inc \ FUSION PROTEIN TAGS Anti FLAG M1 \ flgm1250 for more molecular products just contact us
Studying the role of the fusion protein MLL-AF4 in leukemogenesis with the help of siRNAs [Elektronische Ressource] / von Maria...Studying the role of the fusion protein MLL-AF4 in leukemogenesis with the help of siRNAs [Elektronische Ressource] / von Maria...
Studying the role of the fusion protein MLL-AF4 in leukemogenesis with the help of siRNAs [Elektronische Ressource] / von Maria Thomas (geb. Arkhipova) : Studying the role of the fusion protein MLL-AF4 in leukemogenesis with the help of siRNAs der Fakultät für Biologie der Eberhard Karls Universität Tübingen zur Erlangung des Grades eines Doktors der Naturwissenschaften von Maria Thomas (geb. Arkhipova) aus Pushchino (Russland) vorgelegte D i s s e r t a t i o n 2007 Tag der mündlichen Prüfung: 11.10
CGEN-15001T (partnered) - CompugenCGEN-15001T (partnered) - Compugen
CGEN-15001T is a novel B7/CD28-like immune checkpoint target candidate discovered by Compugen.. Studies testing the immune function of CGEN-15001T, as a membrane bound protein or using a recombinant fusion protein containing the extracellular domain of CGEN-15001T, showed it is capable of inhibiting T cell activation, promoting a Th1 to Th2 shift, and potentially inducing immune tolerance. CGEN-15001T is expressed in subpopulations of immune cells, mainly macrophages, in both tumor and normal tissue samples.. In August 2013, Compugen signed a research and discovery collaboration and license agreement with Bayer HealthCare for the development and commercialization of antibody-based therapeutics for cancer immunotherapy against CGEN-15001T. After achieving all preclinical stage milestones, this program was transferred to Bayer for further development. To date, preclinical activities are on track, and pivotal toxicity studies and GMP clinical trial material production are ongoing.. ...
Fooling the Virus: A Fusion Protein as Virus-Specific TherapeuticFooling the Virus: A Fusion Protein as Virus-Specific Therapeutic
Fooling the Virus: The Fusion protein as Virus-Specific Therapeutic An ACE2 A fusion protein of ACE2 with an Immunogenic Component Project ID : 47-2020-10877
mRNA processingmRNA processing
USP39 Polyclonal Antibody (CAB9582)OverviewTitle:USP39 Polyclonal Antibody (CAB9582)Size:100µLCode:CAB9582Host Species:RabbitPurification:Affinity purificationIsotype:IgGBackgroundN/AImmunogen InformationImmunogen:Recombinant fusion protein containing a ...
Anti-Ran antibody (ab11693) | AbcamAnti-Ran antibody (ab11693) | Abcam
Rabbit polyclonal Ran antibody validated for WB, ICC/IF. Referenced in 2 publications. Immunogen corresponding to recombinant fusion protein
Anti-Livin antibody [88C570] (ab11983) | AbcamAnti-Livin antibody [88C570] (ab11983) | Abcam
Mouse monoclonal Livin antibody [88C570] validated for WB, Flow Cyt and tested in Human. Immunogen corresponding to recombinant fusion protein
A Phase 1b Study of Repeated Doses of Autologous CLL B Cells Transduced to Express Chimeric CD154 (ISF35) in Combination With...A Phase 1b Study of Repeated Doses of Autologous CLL B Cells Transduced to Express Chimeric CD154 (ISF35) in Combination With...
The study is a Phase 1b open label, non-randomized, single institution clinical trial that is designed to evaluate the safety and tolerability of three repeat
RBB 001 - AdisInsightRBB 001 - AdisInsight
RBB 001, a recombinant fusion protein, is a targeted cytoprotectant in development with Rubicon Biotechnology for the treatment of myocardial or cerebral
How Fusion Proteins Cause LeukemiaHow Fusion Proteins Cause Leukemia
Many leukemias begin when a large piece of one chromosome becomes loose and reattaches to another chromosome. This can produce fusion proteins that shut down DNA repair gens and activate genes that help the cells proliferate.
C9orf125 Fusion Protein Ag14695 | ProteintechC9orf125 Fusion Protein Ag14695 | Proteintech
C9orf125 human Fusion Protein GST from Proteintech. Produced in E.coli-derived, PET28a, with high quality purity. Cat.No. Ag14695
P27; KIP1 Fusion Protein Ag2280 | ProteintechP27; KIP1 Fusion Protein Ag2280 | Proteintech
P27; KIP1 human Fusion Protein GST from Proteintech. Produced in E.coli-derived, PET28a, with high quality purity. Cat.No. Ag2280
Osteocrin Protein Human Recombinant | OSTN Antigen | ProSpecOsteocrin Protein Human Recombinant | OSTN Antigen | ProSpec
The recombinant Human Osteocrin is produced with N-terminal fusion of His Tag. The Human Osteocrin His-Tagged Fusion Protein is 13.6 kDa.
In vivo degradation of GFP and a GFP-HipB hybrid.GFP an | Open-iIn vivo degradation of GFP and a GFP-HipB hybrid.GFP an | Open-i
In vivo degradation of GFP and a GFP-HipB hybrid.GFP and GFP with C-terminal fusion to the C terminus of HipB were expressed from a pBRlacitac promoter in BW251
Labeling Proteins in vitro (S9147) | NEBLabeling Proteins in vitro (S9147) | NEB
Protocol Add 2 µl of the substrate stock solution to 18 µl of protein sample containing a SNAP-tag fusion protein in an appropriate buffer (see notes)
Chimeric fusion proteins - Diphtheria toxin-based<...Chimeric fusion proteins - Diphtheria toxin-based<...
TY - JOUR. T1 - Chimeric fusion proteins - Diphtheria toxin-based. AU - Frankel, A. E.. AU - Powell, B. L.. AU - Vallera, D. A.. AU - Neville D.M., Jr. PY - 2001. Y1 - 2001. N2 - Most cancer patients receive chemotherapy drugs that target DNA or the cell division apparatus. Many of these patients develop multidrug-resistant tumor cells, thus, novel methods to overcome drug resistance are needed. One approach is to target tumor cell protein synthesis. Peptide toxins, which catalytically inactivate protein synthesis, have been re-engineered to selectively bind and intoxicate tumor cells. Diphtheria toxin (DT), a member of the class of peptide toxins, has been subjected to structural and genetic analysis and protein engineering for several decades. In this review, we will examine the structure, function, synthesis and pharmacology of anticancer DT conjugates.. AB - Most cancer patients receive chemotherapy drugs that target DNA or the cell division apparatus. Many of these patients develop ...
Functional comparisons of different tumour necrosis factor receptor/IgG fusion proteins. - Nuffield Department of Orthopaedics,...Functional comparisons of different tumour necrosis factor receptor/IgG fusion proteins. - Nuffield Department of Orthopaedics,...
Nine different IgG fusion proteins and one non-fusion protein, all containing sequences from the extracellular domain of either of two human TNF receptors, were compared for their ability to bind and inhibit human TNF-alpha or TNF-beta. The fusion proteins differed with respect to TNF receptor type (p55 or p75 TNF receptor), receptor valency (one, two or four receptor domains per molecule), the presence or absence of a CH1 domain in the IgG constant region, and the proportion of the extracellular domain included in the construct. In vitro TNF binding assays and cytotoxicity assays indicated that, of the constructs that bound TNF, the greatest difference in affinity and neutralizing capability was between monovalent and bivalent receptor constructs. Differences were also noted between tetravalent and bivalent versions of p55 fusion proteins, as well as between a p75 fusion protein comprising the complete extracellular domain and one lacking the C-terminal 53 amino acids of the extracellular domain. p55
Linkers in transferrin fusion proteins: effects on pharmacokinetics and pharmacodynamics :: University of Southern California...Linkers in transferrin fusion proteins: effects on pharmacokinetics and pharmacodynamics :: University of Southern California...
Recombinant fusion proteins have become an important class of biomolecules since the invention of recombinant DNA technology. As an indispensable component of recombinant fusion proteins, linkers have shown increasing importance in the construction of stable, bioactive fusion proteins. In the development of recombinant transferrin (Tf)-fusion proteins for protein drug oral delivery, various linkers have been designed to improve the biological activity, or to achieve desired pharmacokinetic and pharmacodynamic properties. ❧ The Introduction in this dissertation first reviewed the mechanism for Tf receptor-mediated protein drug oral delivery, as well as the recombinant Tf-fusion proteins that have been constructed previously in our lab. It also covers the current knowledge of fusion protein linkers and summarizes examples for their applications. The basic function of linkers is to covalently join the functional domains in the fusion proteins. However, linkers can offer many other advantages for ...
Linkers in transferrin fusion proteins: effects on pharmacokinetics and pharmacodynamics :: University of Southern California...Linkers in transferrin fusion proteins: effects on pharmacokinetics and pharmacodynamics :: University of Southern California...
Recombinant fusion proteins have become an important class of biomolecules since the invention of recombinant DNA technology. As an indispensable component of recombinant fusion proteins, linkers have shown increasing importance in the construction of stable, bioactive fusion proteins. In the development of recombinant transferrin (Tf)-fusion proteins for protein drug oral delivery, various linkers have been designed to improve the biological activity, or to achieve desired pharmacokinetic and pharmacodynamic properties. ❧ The Introduction in this dissertation first reviewed the mechanism for Tf receptor-mediated protein drug oral delivery, as well as the recombinant Tf-fusion proteins that have been constructed previously in our lab. It also covers the current knowledge of fusion protein linkers and summarizes examples for their applications. The basic function of linkers is to covalently join the functional domains in the fusion proteins. However, linkers can offer many other advantages for ...
Effect of SBDs position in fusion proteins on activity and binding properties<...Effect of SBD's position in fusion proteins on activity and binding properties<...
TY - JOUR. T1 - Effect of SBDs position in fusion proteins on activity and binding properties. AU - Ji, Q.. AU - Vincken, J.P.. AU - Raemakers, C.J.J.M.. AU - Suurs, L.C.J.M.. AU - Visser, R.G.F.. PY - 2005. Y1 - 2005. M3 - Comment/Letter to the editor. VL - 28. SP - 1. EP - 5. JO - Journal of Nanjing Normal university: Natural Science Edition. JF - Journal of Nanjing Normal university: Natural Science Edition. SN - 1001-4616. IS - 1. ER - ...
Expression of Human Globular Adiponectin-Glucagon-Like Peptide-1 Analog Fusion Protein and Its Assay of Glucose-Lowering Effect...Expression of Human Globular Adiponectin-Glucagon-Like Peptide-1 Analog Fusion Protein and Its Assay of Glucose-Lowering Effect...
In the present study, we developed, for the first time, a successful protocol for expression human gAd-GLP-1-A fusion protein from Escherichia coli strain BL21 (DE3). Plasmid vector PET28a was used to express this fusion protein. This vector can produce an N-terminal His-tagged protein. His-tag is often used for protein purification [11]. The affinity of the His-tag for metal ions allows the fusion product to be quickly separated from the bulk of other bacterial proteins by using metal chelate affinity chromatography [11]. Because N-terminal His-tag may influence the function of protein, we designed an enterokinase cleavage site at the 5 terminus of the gene of the gAd-GLP-1-A fusion protein, which was used to remove the His-tag [9]. In our study, most of the His-tagged fusion protein expressed from BL21 (DE3) was present in inclusion body. In order to recover its function, the fusion protein in inclusion body was refolded in urea gradient refolding buffer. And then, the refolded protein was ...
Heart attack: New protein therapy may improve recovery | LifesaversHeart attack: New protein therapy may improve recovery | Lifesavers
New preclinical research in animal models finds that infusing a specific protein into scar tissue after a heart attack improves and speeds up the recovery of the heart. According to the American Heart Association (AHA), around 605,000 people in the United States have a new heart attack each year, and approximately 200,000 experience a recurrent attack.. Reperfusion, which is a technique that frees up the flow of oxygen to the hearts tissue, is a common form of treatment after a heart attack. However, up to one-quarter of people who undergo reperfusion develop heart failure within a year.. So, researchers led by James Chong - an associate professor at the University of Sydney in Australia - have explored an alternative treatment that targets the scar tissue that forms after a heart attack.. Chong and colleagues evaluated the therapeutic potential of a protein therapy called recombinant human platelet-derived growth factor-AB (rhPDGF-AB).. As its name suggests, rhPDGF-AB is a recombinant growth ...
Expression In Bacteria Of Beta-Galactosidase Fusion Proteins Carrying Antigenic Determinants Of The 2 X-Gene Products Of Bovine...Expression In Bacteria Of Beta-Galactosidase Fusion Proteins Carrying Antigenic Determinants Of The 2 X-Gene Products Of Bovine...
Expression In Bacteria Of Beta-Galactosidase Fusion Proteins Carrying Antigenic Determinants Of The 2 X-Gene Products Of Bovine Leukemia- ...
Global Spinal Fusion Systems Market Executive Summary and Analysis by Top Players 2020-2025 : Medtronic, Johnson & Johnson,...Global Spinal Fusion Systems Market Executive Summary and Analysis by Top Players 2020-2025 : Medtronic, Johnson & Johnson,...
The global Spinal Fusion Systems Market report offers precise analytical information about the Spinal Fusion Systems market. The market experts and proficient analysts generate the information based on the past and current situation of Spinal Fusion Systems market, various factors affecting the growth trajectory, global sales, demand, total revenue generated, and capitalization of the market. Moreover, the report delivers a summarized assessment of the impact of federal policies and regulations on market operations. It also comprises detailed information pertaining to the Spinal Fusion Systems markets current dynamics. The global Spinal Fusion Systems market acts as a huge platform that offers several opportunities for many reputed firms, organizations, manufacturers, vendors, and suppliers Medtronic, Johnson & Johnson, Zimmer Biomet, Benvenue Medical, SeaSpine Holdings Corporation, Alphatec, Orthofix, Stryker to compete with each other to become one of the globally and regionally leading ...
The Synovial Sarcoma-Associated SS18-SSX2 Fusion Protein Induces Epigenetic Gene (De)Regulation.The Synovial Sarcoma-Associated SS18-SSX2 Fusion Protein Induces Epigenetic Gene (De)Regulation.
Fusion of the SS18 and either one of the SSX genes is a hallmark of human synovial sarcoma. The SS18 and SSX genes encode nuclear proteins that exhibit opposite transcriptional activities. The SS18 protein functions as a transcriptional coactivator and is associated with the SWI/SNF complex, whereas the SSX proteins function as transcriptional corepressors and are associated with the polycomb complex. The domains involved in these opposite transcriptional activities are retained in the SS18-SSX fusion proteins. Here, we set out to determine the direct transcriptional consequences of conditional SS18-SSX2 fusion protein expression using complementary DNA microarray-based profiling. By doing so, we identified several clusters of SS18-SSX2-responsive genes, including a group of genes involved in cholesterol synthesis, which is a general characteristic of malignancy. In addition, we identified a group of SS18-SSX2-responsive genes known to be specifically deregulated in primary synovial sarcomas, ...
PPT - Detection of Protein-Protein Interactions Using the GST Fusion Protein Pull-down Technique PowerPoint Presentation - ID...PPT - Detection of Protein-Protein Interactions Using the GST Fusion Protein Pull-down Technique PowerPoint Presentation - ID...
Detection of Protein-Protein Interactions Using the GST Fusion Protein Pull-down Technique. Bacterially expressed glutathione S-transferase (GST)-fused proteins are used as probes to perform direct measure of protein-protein interactions and for affinity purification. Slideshow 6521621 by...
US Patent # 9,566,353. Fluorescent fusion polypeptides and methods of use - Patents.comUS Patent # 9,566,353. Fluorescent fusion polypeptides and methods of use - Patents.com
Embodiments of the present invention provide for the facile generation of a stable recombinant fusion polypeptides with intrinsic fluorescent properties. The recombinant antibodies may be suitable fo
Selective Chemokine Receptor-Targeted Depletion of Pathological Cells as A Therapeutic Strategy for Inflammatory, Allergic and...Selective Chemokine Receptor-Targeted Depletion of Pathological Cells as A Therapeutic Strategy for Inflammatory, Allergic and...
Title: Selective Chemokine Receptor-Targeted Depletion of Pathological Cells as A Therapeutic Strategy for Inflammatory, Allergic and Autoimmune Diseases. VOLUME: 3 ISSUE: 3. Author(s):John R. McDonald. Affiliation:Osprey Pharmaceuticals Limited, 7150 Frederick, Banting, d, St. Laurent, QC H4S 2A1, Canada.. Keywords:Chemokine, fusion protein, monoclonal antibody, immunotoxin, allergic, autoimmune, inflammation, cancer, bispecific antibodies, ribosome inactivating protein. Abstract: Targeting cell surface antigens or receptors with lytic monoclonal antibodies and specific ligand-directed fusion proteins in order to eliminate cancer cells has been in development for at least forty years. More recently, leukocyte populations known to drive a host of allergic, autoimmune and inflammatory diseases have been targeted. For fusion protein constructs, a number of different classes of cellular toxins have been fused to a variety of ligands such as monoclonal antibodies, growth factors and cytokines. ...
Patent US7601814 - Reducing the immunogenicity of fusion proteins - Google PatentsPatent US7601814 - Reducing the immunogenicity of fusion proteins - Google Patents
Disclosed are compositions and methods for producing fusion proteins with reduced immunogenicity. Fusion proteins of the invention include a junction region having an amino acid change that reduces the ability of a junctional epitope to bind to MHC Class II, thereby reducing its interaction with a T-cell receptor. Methods of the invention involve analyzing, changing, or modifying one or more amino acids in the junction region of a fusion protein in order to identify a T-cell epitope and reduce its ability to interact with a T cell receptor. Compositions and methods of the invention are useful in therapy.
KEGG PATHWAY: ko05221KEGG PATHWAY: ko05221
Acute myeloid leukemia (AML) is a disease that is characterized by uncontrolled proliferation of clonal neoplastic cells and accumulation in the bone marrow of blasts with an impaired differentiation program. AML accounts for approximately 80% of all adult leukemias and remains the most common cause of leukemia death. Two major types of genetic events have been described that are crucial for leukemic transformation. A proposed necessary first event is disordered cell growth and upregulation of cell survival genes. The most common of these activating events were observed in the RTK Flt3, in N-Ras and K-Ras, in Kit, and sporadically in other RTKs. Alterations in myeloid transcription factors governing hematopoietic differentiation provide second necessary event for leukemogenesis. Transcription factor fusion proteins such as AML-ETO, PML-RARalpha or PLZF-RARalpha block myeloid cell differentiation by repressing target genes. In other cases, the transcription factors themselves are mutated ...
Transfection of the different EGFP fusion constructs to | Open-iTransfection of the different EGFP fusion constructs to | Open-i
Transfection of the different EGFP fusion constructs to IMR-90 fibroblasts. A) The wild-type SAP30L concentrates in small dense bodies in the nuclei. B) The nuc
Potency-matched dual cytokine-antibody fusion proteins for cancer therapy - Zurich Open Repository and ArchivePotency-matched dual cytokine-antibody fusion proteins for cancer therapy - Zurich Open Repository and Archive
A novel biopharmaceutical, consisting of the F8 mAb (specific to a splice isoform of fibronectin) simultaneously fused to both TNF and IL2, was found to react with the majority of solid tumors and hematologic malignancies in mouse and man, but not with healthy adult tissues. The product selectively localized to neoplastic lesions in vivo, as evidenced by quantitative biodistribution studies using radioiodinated protein preparations. When the potency of the cytokine payloads was matched by a single-point mutation, the resulting fusion protein (IL2-F8-TNFmut) eradicated soft-tissue sarcomas in immunocompetent mice, which did not respond to individual antibody-cytokine fusion proteins or by standard doxorubicin treatment. Durable complete responses were also observed in mice bearing CT26, C1498, and F9 tumors. The simultaneous delivery of multiple proinflammatory payloads to the cancer site conferred protective immunity against subsequent tumor challenges. A fully human homolog of IL2-F8-TNFmut, ...
AT2 Receptors - Pharmacogenetics of BCR/ABL InhibitorsAT2 Receptors - Pharmacogenetics of BCR/ABL Inhibitors
A recombinant fusion proteins (BBG2Na) comprising the central conserved website of the respiratory syncytial computer virus subgroup A (RSV-A) (Long) G protein (residues 130 to 230) and an albumin binding website of streptococcal protein G was shown previously to protect mouse top (URT) and lower (LRT) respiratory tracts against intranasal RSV challenge (U. of the implicated epitopes in the context of the whole computer virus. However, Pepscan analyses of RSV-seropositive human being sera revealed that from the murine B-cell defensive epitopes (protectopes) that mapped towards the central conserved domains had been recognized in guy. Should these murine protectopes end up being implicated in individual LRT security also, their clustering throughout the highly conserved cysteine noose region shall possess important implications for the introduction of RSV vaccines. Respiratory syncytial trojan (RSV) is an associate Rabbit polyclonal to PPAN. from the genus as well as the family members had been ...
Favipiravir - Pharmacogenetics of BCR/ABL InhibitorsFavipiravir - Pharmacogenetics of BCR/ABL Inhibitors
A recombinant fusion proteins (BBG2Na) comprising the central conserved website of the respiratory syncytial computer virus subgroup A (RSV-A) (Long) G protein (residues 130 to 230) and an albumin binding website of streptococcal protein G was shown previously to protect mouse top (URT) and lower (LRT) respiratory tracts against intranasal RSV challenge (U. of the implicated epitopes in the context of the whole computer virus. However, Pepscan analyses of RSV-seropositive human being sera revealed that from the murine B-cell defensive epitopes (protectopes) that mapped towards the central conserved domains had been recognized in guy. Should these murine protectopes end up being implicated in individual LRT security also, their clustering throughout the highly conserved cysteine noose region shall possess important implications for the introduction of RSV vaccines. Respiratory syncytial trojan (RSV) is an associate Rabbit polyclonal to PPAN. from the genus as well as the family members had been ...
Pharmacokinetics and safety in rhesus monkeys of a monoclonal antibody-GDNF fusion protein for targeted blood-brain barrier...Pharmacokinetics and safety in rhesus monkeys of a monoclonal antibody-GDNF fusion protein for targeted blood-brain barrier...
A no-observable-adverse-effect level is established in the Rhesus monkey for the acute administration of the HIRMAb-GDNF fusion protein. The fusion protein targeting the insulin receptor has a PK profile similar to a classical small molecule.
Pick1 monoclonal antibody, clone GB5 (ATTO 633) - (MAB11625) - Products - AbnovaPick1 monoclonal antibody, clone GB5 (ATTO 633) - (MAB11625) - Products - Abnova
Mouse monoclonal antibody raised against partial synthetic protein of Pick1. Recombinant fusion protein corresponding to amino acids 101-130 of rat Pick1. (MAB11625) - Products - Abnova
TFAP2C monoclonal antibody, clone AP2g 6E4/4 - (MAB7289) - Products - AbnovaTFAP2C monoclonal antibody, clone AP2g 6E4/4 - (MAB7289) - Products - Abnova
Mouse monoclonal antibody raised against recombinant TFAP2C. Recombinant fusion protein corresponding to TFAP2C. (MAB7289) - Products - Abnova
Sepax Technologies, Inc.Sepax Technologies, Inc.
Zenix SEC-300 (3 µm, 300 Å) column delivers baseline separation of Fc fusion protein, its oligomer, and impurity. With the addition of arginine, the hydrophobic interaction between Fc fusion protein and column resin is minimized. ...
Chromatography Archives - Page 6 of 10 - BioProcess InternationalBioProcess International | Page 6Chromatography Archives - Page 6 of 10 - BioProcess InternationalBioProcess International | Page 6
Protein A affinity chromatography is traditionally used as the capture step for monoclonal antibodies (MAbs) (1,2,3). It yields high purity because only the fragment-crystallizable (Fc) region of an antibody (IgG1 or IgG2) or Fc-containing fusion protein can bind to the protein A ligand. The resulting specificity provides substantial reduction in impurities such as host cell proteins (HCPs) and DNA (4,5,6,7,8). The dynamic binding capacity of protein A chromatography resins is generally ≤40 g/L and depends highly on residence time because…. ...
May 2009 Archives - BioProcess InternationalBioProcess InternationalMay 2009 Archives - BioProcess InternationalBioProcess International
Protein A affinity chromatography is traditionally used as the capture step for monoclonal antibodies (MAbs) (1,2,3). It yields high purity because only the fragment-crystallizable (Fc) region of an antibody (IgG1 or IgG2) or Fc-containing fusion protein can bind to the protein A ligand. The resulting specificity provides substantial reduction in impurities such as host cell proteins (HCPs) and DNA (4,5,6,7,8). The dynamic binding capacity of protein A chromatography resins is generally ≤40 g/L and depends highly on residence time because…. ...
HaloLink Resin for Protein Pull-Down and AnalysisHaloLink Resin for Protein Pull-Down and Analysis
In this article we analyze protein:protein interactions and enzyme activity for several fusion proteins, and show that HaloTag fusion proteins bound to HaloLink Resin maintain function.
Plus itPlus it
Studies using PKC regulatory/catalytic domain chimeras have underscored the complexity of PKC functions in relation to its structural domains. In previous reports, we and others showed that certain features of isozyme-specific PKC functions could be attributed to the catalytic domain only. These include the PKC-δ-mediated PMA-induced macrophage differentiation of 32D cells (14), the tumorigenicity of PKC-ε-overexpressing NIH 3T3 cells (15), the PKC-βII-mediated growth promotion in K-562 cells (26), and the protection of PKC-δ from down-regulation induced by bryostatin 1 in NIH 3T3 cells (17). However, in some cases, both the regulatory and the catalytic domains contribute to the isoform-specific effects (15, 18, 27). Further mapping of the structural domains beyond the catalytic and regulatory regions is essential to clearly determine the function of each structural domain and to understand how individual domains interact with each other to regulate PKC function.. Previous studies on the ...
Fusion ProteinsFusion Proteins
Caltag Medsystems supply a wide range of fusion proteins for cancer research, neurobiology, metabolism, apoptosis, cell biology, immunology, infectious diseases
Recombinant Human ACVR1, Fc-tagged, Biotinylated ACVR1-526H - Creative BioMartRecombinant Human ACVR1, Fc-tagged, Biotinylated ACVR1-526H - Creative BioMart
The recombinant human ACVR1-Fc fusion protein is expressed as a 331amino acid protein consisting of Met21 - Glu123 region of ACVR1 (UniProt accession #Q04771) and a C-terminal Fc fusion from human IgG1, which exists as a dimer under non-reducing condition.
Raw fusion protein powder review 2020 from official source | Pictures revealed!Raw fusion protein powder review 2020 from official source | Pictures revealed!
Raw fusion protein powder experience: You have to avoid these #errors, then #successes are already possible after 17 days ✚ the big test here
ReP USP - Detalhe do registro: Use of pex and pgex bacterial heterologous protein expression systems for recombinant...ReP USP - Detalhe do registro: Use of pex and pgex bacterial heterologous protein expression systems for recombinant...
POMPEIA, C; ORTIS, F; ARMELIN, M C S. Use of pex and pgex bacterial heterologous protein expression systems for recombinant oncoprotein production and antisera generation. Biotechnology and Applied Biochemistry, San Diego, v. 25, p. 207-15, 1997 ...
Optimal expression of fusion proteins in mammalian cells | AgilentOptimal expression of fusion proteins in mammalian cells | Agilent
Get epitope-tagging technology which can provide you a powerful means to functionally analyze your protein of interest without the need for an antibody specific to each new protein under study. pCMV-3Tag vectors have three copies of the epitope tag in a variety of configurations to prove a stronger signal in immmunological assays.
A novel melittin-MhIL-2 fusion protein inhibits the growth of human ovarian cancer SKOV3 cells in vitro and in vivo tumor...A novel melittin-MhIL-2 fusion protein inhibits the growth of human ovarian cancer SKOV3 cells in vitro and in vivo tumor...
Sigma-Aldrich offers abstracts and full-text articles by [Mingjun Liu, Jinbao Zong, Zimin Liu, Ling Li, Xu Zheng, Bin Wang, Guirong Sun].
Analysis of the Targeting Properties of Fc Chimeric Proteins and Antibodies in Mice In Vivo - Current ProtocolsAnalysis of the Targeting Properties of Fc Chimeric Proteins and Antibodies in Mice In Vivo - Current Protocols
This unit includes protocols for the analysis of the targeting properties of Fc chimeric proteins and antibodies in mice in vivo
ATCC ® 87059™ATCC ® 87059™
ATCC ® 87059™ Designation: pETGEXCT TypeStrain=False Application: encodes removable tag for protein isolation expression vector vector permitting RNA synthesis in vitro vector permitting construction of fusion proteins
PLGLB2PLGLB2
TopoTargetTopoTarget
BiopharmaceuticalBiopharmaceutical
HaloTagHaloTag
EtanerceptEtanercept
FLAG-tagFLAG-tag
TROVE2TROVE2
TEV proteaseTEV protease
Factor IXFactor IX
Sporosarcina ureaeSporosarcina ureae
ImmunotoxinImmunotoxin
Nuclear-inclusion-a endopeptidaseNuclear-inclusion-a endopeptidase
BelimumabBelimumab
AtaciceptAtacicept
Biological therapy for inflammatory bowel diseaseBiological therapy for inflammatory bowel disease
CD4 immunoadhesinCD4 immunoadhesin
Human metapneumovirusHuman metapneumovirus
AlbinterferonAlbinterferon
MorpheeinMorpheein
BDH1BDH1
BatroxobinBatroxobin
Ruth Sonntag NussenzweigRuth Sonntag Nussenzweig
LuspaterceptLuspatercept
IMP321IMP321
Transmembrane activator and CAML interactorTransmembrane activator and CAML interactor
Index of HIV/AIDS-related articlesIndex of HIV/AIDS-related articles
Tumor necrosis factor alphaTumor necrosis factor alpha
InfluenzaInfluenza
Lasker AwardLasker Award
Interleukin 15Interleukin 15
Beta cellBeta cell
Green fluorescent proteinGreen fluorescent protein
TransgenesisTransgenesis
ImmunocontraceptionImmunocontraception
Cell-penetrating peptideCell-penetrating peptide
Contrast-enhanced ultrasoundContrast-enhanced ultrasound
Blue-white screenBlue-white screen
Concanavalina A, a enciclopedia libreConcanavalina A, a enciclopedia libre
InfliximabInfliximab
Affinity chromatographyAffinity chromatography
Arabidopsis thalianaArabidopsis thaliana
DNADNA
ThrombinThrombin
Spinal fusionSpinal fusion
IRGsIRGs
Immunosuppressive drugImmunosuppressive drug
Genetic engineeringGenetic engineering
Microbial geneticsMicrobial genetics
Polymerase chain reactionPolymerase chain reaction
Gag-onc fusion proteinGag-onc fusion protein
Chromosomal crossoverChromosomal crossover
Spinal muscular atrophySpinal muscular atrophy
真菌 - 维基百科，自由的百科全书真菌 - 维基百科，自由的百科全书
Transforming growth factor, beta 3Transforming growth factor, beta 3
Dihydrofolate reductaseDihydrofolate reductase
AnatomyOrganismsDiseasesChemicals and DrugsAnalytical, Diagnostic and Therapeutic Techniques and EquipmentPhenomena and ProcessesInformation Science
Recombinant Fusion ProteinsMolecular Sequence DataAmino Acid SequenceRecombinant ProteinsCloning, MolecularEscherichia coliBase SequenceVaccines, SyntheticImmunotoxinsMembrane FusionEpitopesViral Fusion ProteinsCell FusionGenetic VectorsDNA, ComplementaryImmunoconjugatesCell LineProtein BindingSequence Homology, Amino AcidGlutathione TransferaseAntibodies, MonoclonalEnzyme-Linked Immunosorbent AssayGene ExpressionPlasmidsDNA PrimersMice, Inbred BALB CBlotting, WesternBinding SitesImmunoblottingElectrophoresis, Polyacrylamide GelBacterial ProteinsProtozoan ProteinsAntibody SpecificityImmunoglobulin GHepatocyte Nuclear Factor 3-betaDiphtheria ToxinMembrane GlycoproteinsAntigens, BacterialTumor Cells, CulturedPolymerase Chain ReactionAntibodies, BacterialAutoantibodiesOncogene Proteins, FusionKineticsMolecular WeightRabbitsCattleGene FusionSpinal FusionT-LymphocytesADP Ribose TransferasesProtein Structure, TertiaryTransfectionDNA, RecombinantGreen Fluorescent ProteinsPeptide FragmentsMembrane Fusion ProteinsCells, CulturedLuminescent ProteinsBacterial ToxinsMutationCricetinaeMaltose-Binding ProteinsMembrane ProteinsBaculoviridaeViral Envelope Proteinsbeta-GalactosidaseRecombination, GeneticCarrier ProteinsCercopithecus aethiopsViral ProteinsOncogene FusionMutagenesis, Site-DirectedProtein EngineeringCHO CellsCell MembraneHeLa CellsSpodopteraDNA-Binding ProteinsTranscription FactorsCOS CellsPeptidesVirus InternalizationTranscription, GeneticProtein ConformationRNA, MessengerImmunoglobulin Fc FragmentsRestriction MappingSubstrate SpecificitySaccharomyces cerevisiaeTranslocation, GeneticPichiaMicroscopy, FluorescenceGenes, BacterialDNAMice, Inbred C57BLSequence DeletionVesicular Transport ProteinsAquaporin 1Models, MolecularAntibodies, ViralProtein TransportGiant CellsVero Cells
Recombinant human ADRB1 Gly389 + GsaL fusion protein (ab90784) ProtocolsRecombinant human ADRB1 Gly389 + GsaL fusion protein (ab90784) Protocols
High level transient production of recombinant antibodies and antibody fusion proteins in HEK293 cells | BMC Biotechnology |...High level transient production of recombinant antibodies and antibody fusion proteins in HEK293 cells | BMC Biotechnology |...
Patent US6242570 - Production and use of recombinant protein multimers with increased ... - Google PatentsPatent US6242570 - Production and use of recombinant protein multimers with increased ... - Google Patents
Factor IX (Recombinant [Fc Fusion Protein]) Information - Drugs.comFactor IX (Recombinant [Fc Fusion Protein]) Information - Drugs.com
Factor IX (Recombinant), albumin fusion protein Monograph for Professionals - Drugs.comFactor IX (Recombinant), albumin fusion protein Monograph for Professionals - Drugs.com
Factor IX (Recombinant [Fc Fusion Protein]) | Memorial Sloan Kettering Cancer CenterFactor IX (Recombinant [Fc Fusion Protein]) | Memorial Sloan Kettering Cancer Center
Recombinant human ADRB2 + GsaL fusion protein (ab90837)Recombinant human ADRB2 + GsaL fusion protein (ab90837)
Factor IX (Recombinant [Fc Fusion Protein]): Pediatric Medication | Memorial Sloan Kettering Cancer CenterFactor IX (Recombinant [Fc Fusion Protein]): Pediatric Medication | Memorial Sloan Kettering Cancer Center
Factor Ix Fc Fusion Protein Recombinant (Intravenous Route) Description and Brand Names - Mayo ClinicFactor Ix Fc Fusion Protein Recombinant (Intravenous Route) Description and Brand Names - Mayo Clinic
Recombinant Fusion Proteins | Harvard Catalyst Profiles | Harvard CatalystRecombinant Fusion Proteins | Harvard Catalyst Profiles | Harvard Catalyst
Eloctate (Antihemophilic Factor (Recombinant), Fc Fusion Protein for Intravenous Infusion): Side Effects, Interactions, Warning...Eloctate (Antihemophilic Factor (Recombinant), Fc Fusion Protein for Intravenous Infusion): Side Effects, Interactions, Warning...
Assay, purification and characterization of a recombinant malaria circumsporozoite fusion protein by high-performance liquid...Assay, purification and characterization of a recombinant malaria circumsporozoite fusion protein by high-performance liquid...
A Safety and Efficacy Extension Study of a Recombinant Fusion Protein Linking Coagulation Factor IX With Albumin (rIX-FP) in...A Safety and Efficacy Extension Study of a Recombinant Fusion Protein Linking Coagulation Factor IX With Albumin (rIX-FP) in...
Effectiveness and harms of recombinant human bone morphogenetic protein-2 in spine fusion: a systematic review and meta...Effectiveness and harms of recombinant human bone morphogenetic protein-2 in spine fusion: a systematic review and meta...
Study to Evaluate the Safety, Efficacy, and Pharmacokinetics of Recombinant Coagulation Factor VIII Fc Fusion Protein (rFVIIIFc...Study to Evaluate the Safety, Efficacy, and Pharmacokinetics of Recombinant Coagulation Factor VIII Fc Fusion Protein (rFVIIIFc...
Study of Recombinant Factor VIIa Fusion Protein (rVIIa-FP, CSL689) for On-demand Treatment of Bleeding Episodes in Patients...Study of Recombinant Factor VIIa Fusion Protein (rVIIa-FP, CSL689) for On-demand Treatment of Bleeding Episodes in Patients...
Recombinant Albumin Fusion Protein sEphB4-HSA in Treating Patients With Metastatic or Recurrent Solid Tumors - Full Text View -...Recombinant Albumin Fusion Protein sEphB4-HSA in Treating Patients With Metastatic or Recurrent Solid Tumors - Full Text View -...
A trial of etanercept, a recombinant tumor necrosis factor receptor:Fc fusion protein, in patients with rheumatoid arthritis...A trial of etanercept, a recombinant tumor necrosis factor receptor:Fc fusion protein, in patients with rheumatoid arthritis...
Frontiers | A Recombinant Trivalent Fusion Protein F1-LcrV-HSP70(II) Augments Humoral and Cellular Immune Responses and Imparts...Frontiers | A Recombinant Trivalent Fusion Protein F1-LcrV-HSP70(II) Augments Humoral and Cellular Immune Responses and Imparts...
Optimising expression of the recombinant fusion protein biopesticide ω-hexatoxin-Hv1a/GNA in Pichia pastoris: sequence...Optimising expression of the recombinant fusion protein biopesticide ω-hexatoxin-Hv1a/GNA in Pichia pastoris: sequence...
Frontiers | Porous Nanoparticles With Self-Adjuvanting M2e-Fusion Protein and Recombinant Hemagglutinin Provide Strong and...Frontiers | Porous Nanoparticles With Self-Adjuvanting M2e-Fusion Protein and Recombinant Hemagglutinin Provide Strong and...
WO1998050432 RECOMBINANT ANTIBODY-ENZYME FUSION PROTEINSWO1998050432 RECOMBINANT ANTIBODY-ENZYME FUSION PROTEINS
Modeling and Simulation of Production of Metallothionein and Red Fluorescent Fusion Protein by Recombinant Escherichia Coli...Modeling and Simulation of Production of Metallothionein and Red Fluorescent Fusion Protein by Recombinant Escherichia Coli...
Factor ix albumin fusion protein recombinant (By injection) | Drug Notes | Health Information | St. Lukes HospitalFactor ix albumin fusion protein recombinant (By injection) | Drug Notes | Health Information | St. Luke's Hospital
Eloctate (antihemophilic factor (recombinant), fc fusion protein) dose, indications, adverse effects, interactions... from PDR...Eloctate (antihemophilic factor (recombinant), fc fusion protein) dose, indications, adverse effects, interactions... from PDR...
Study of Recombinant Factor IX Fc Fusion Protein (rFIXFc) in Subjects With Hemophilia B - Hemophilia Federation of AmericaStudy of Recombinant Factor IX Fc Fusion Protein (rFIXFc) in Subjects With Hemophilia B - Hemophilia Federation of America
Creating recombinant fusion protein conjugates for targeting SNARE protease into neuroendocrine cells - DORASCreating recombinant fusion protein conjugates for targeting SNARE protease into neuroendocrine cells - DORAS
Human αB-crystallin as fusion protein and molecular chaperone increases the expression and folding efficiency of recombinant...Human αB-crystallin as fusion protein and molecular chaperone increases the expression and folding efficiency of recombinant...
Respiratory syncytial virus subunit vaccine based on a recombinant fusion protein expressed transiently in mammalian cells -...Respiratory syncytial virus subunit vaccine based on a recombinant fusion protein expressed transiently in mammalian cells -...
Fermentation study on the engineering bacterial of recombinant human thrombopoietin fusion protein--《Joural of Biology...Fermentation study on the engineering bacterial of recombinant human thrombopoietin fusion protein--《Joural of Biology...
Combined effect of protein fusion and signal sequence greatly enhances the production of recombinant human GM-CSF in...Combined effect of protein fusion and signal sequence greatly enhances the production of recombinant human GM-CSF in...
Effectiveness and Harms of Recombinant Human Bone Morphogenetic Protein-2 in Spine Fusion - Spine SectionEffectiveness and Harms of Recombinant Human Bone Morphogenetic Protein-2 in Spine Fusion - Spine Section
AnatomyOrganismsDiseasesChemicals and DrugsAnalytical, Diagnostic and Therapeutic Techniques and EquipmentPhenomena and ProcessesInformation Science
Recombinant Fusion ProteinsMolecular Sequence DataAmino Acid SequenceRecombinant ProteinsCloning, MolecularEscherichia coliBase SequenceVaccines, SyntheticImmunotoxinsMembrane FusionEpitopesViral Fusion ProteinsCell FusionGenetic VectorsDNA, ComplementaryImmunoconjugatesCell LineProtein BindingSequence Homology, Amino AcidGlutathione TransferaseAntibodies, MonoclonalEnzyme-Linked Immunosorbent AssayGene ExpressionPlasmidsDNA PrimersMice, Inbred BALB CBlotting, WesternBinding SitesImmunoblottingElectrophoresis, Polyacrylamide GelBacterial ProteinsProtozoan ProteinsAntibody SpecificityImmunoglobulin GHepatocyte Nuclear Factor 3-betaDiphtheria ToxinMembrane GlycoproteinsAntigens, BacterialTumor Cells, CulturedPolymerase Chain ReactionAntibodies, BacterialAutoantibodiesOncogene Proteins, FusionKineticsMolecular WeightRabbitsCattleGene FusionSpinal FusionT-LymphocytesADP Ribose TransferasesProtein Structure, TertiaryTransfectionDNA, RecombinantGreen Fluorescent ProteinsPeptide FragmentsMembrane Fusion ProteinsCells, CulturedLuminescent ProteinsBacterial ToxinsMutationCricetinaeMaltose-Binding ProteinsMembrane ProteinsBaculoviridaeViral Envelope Proteinsbeta-GalactosidaseRecombination, GeneticCarrier ProteinsCercopithecus aethiopsViral ProteinsOncogene FusionMutagenesis, Site-DirectedProtein EngineeringCHO CellsCell MembraneHeLa CellsSpodopteraDNA-Binding ProteinsTranscription FactorsCOS CellsPeptidesVirus InternalizationTranscription, GeneticProtein ConformationRNA, MessengerImmunoglobulin Fc FragmentsRestriction MappingSubstrate SpecificitySaccharomyces cerevisiaeTranslocation, GeneticPichiaMicroscopy, FluorescenceGenes, BacterialDNAMice, Inbred C57BLSequence DeletionVesicular Transport ProteinsAquaporin 1Models, MolecularAntibodies, ViralProtein TransportGiant CellsVero Cells
Production of recombinantAntibodiesAntibodyEscherichiaPeptidesPurificationAntibodiesAlbumin fusionAntihemophilicProduce recombinantSubunit vaccinePeptideCompared with recombinant factorActivity of the recombinantVaccineSolubleGeneAntibody fusionInjectionSingle chain antibodyPurity2016Affinity chromatographyMycobacteriumSequencesBiologically activeCoagulationAntitumorELOCTATEVitroSpinalStudyMaltose-bindingHamster proteinsBoneCleavageSpeciesGeneticallyCervicalVaccinesAntigensFactor VIIIAdenovirusMembraneReceptorInsect cellsSelectivelyBindBiological
Production of recombinant1
Antibodies3
Antibody1
  • After vector optimization and process optimization the yield of an scFv-Fc antibody and a cytotoxic antibody-RNase fusion protein further increased 3-4-fold to more than 450 mg/L. Finally, an entirely new mammalian expression vector was constructed for single step in frame cloning of scFv genes from antibody phage display libraries. (biomedcentral.com)
Escherichia10
Peptides4
Purification13
Antibodies14
Albumin fusion14
Antihemophilic4
Produce recombinant1
  • To obtain a high expressing clone of P. pastoris to produce recombinant Hv1a/GNA, a straightforward method was used to produce multi-copy expression plasmids, which does not require multiple integrations to give clones of P. pastoris containing high copy numbers of the introduced gene. (springer.com)
Subunit vaccine3
Peptide8
  • To prevent proteolysis, the Hv1a/GNA fusion expression construct was modified by site-directed mutagenesis to remove a potential Kex2 cleavage site at the C-terminus of the Hv1a peptide. (springer.com)
  • Fitches EC, Pyati PS, King GF, Gatehouse JA (2012) Fusion to snowdrop lectin dramatically enhances the oral activity of the insecticidal peptide ω-hexatoxin-Hv1a by mediating its delivery to the central nervous system. (springer.com)
  • An alternative strategy was also adopted with a view to stapling a recombinant BoNT/AΔHCC-SNAP-25 protein (without the neuronal binding domain) with Vamp2.βNGF produced in E. coli, and a synthetic syntaxin-1 peptide via SNARE complex formation. (dcu.ie)
  • Encouragingly, after inclusion of this leader peptide sequence into a Vamp2.βNGF construct, it was expressed as an active protein, although with low yield. (dcu.ie)
  • ORCID: https://orcid.org/0000-0002-3882-6129 2016, Novel fusion proteins based on recombinant lectins for delivery of a cytotoxic peptide specifically to cancer cells , PhD thesis, University of Salford. (salford.ac.uk)
  • The short peptide was expressed directly as a fusion protein with a superfolder form of the green florescent protein ( sf GFP), resulting in a high yield expression of soluble sf GFP-mutacin fusion protein (30 kDa) in the cytoplasm of E. coli. (openmicrobiologyjournal.com)
  • This is the first report of three different fusion proteins with an antitumor-analgesic peptide obtained from Chinese scorpion Buthus martensii Karsch (BmKAGAP). (bvsalud.org)
  • Elastin‐like polypeptides (ELPs) are recombinant peptide‐based biopolymers that contain repetitive sequences enriched in glycine, valine, proline, and alanine. (ingentaconnect.com)
Compared with recombinant factor1
  • In the phase 3 B-LONG (Recombinant Factor IX Fc Fusion Protein [rFIXFc] in Subjects With Haemophilia B) study, rFIXFc demonstrated a prolonged half-life compared with recombinant factor IX (rFIX), and safety and efficacy for prophylaxis and treatment of bleeding in subjects with moderately-severe to severe haemophilia B. In this B-LONG sub-analysis, rFIXFc was evaluated for efficacy in subjects requiring major surgery. (elsevier.com)
Activity of the recombinant1
Vaccine5
  • The formation of this vaccine construction was accompanied by significant conformational changes in the chimeric protein. (mdpi.com)
  • We have previously developed a fusion protein with 3 copies of the ectodomain of matrix protein 2 (M2e), which is one of the most explored conserved influenza A virus antigens for a broadly protective vaccine known today. (frontiersin.org)
  • Findings in this and our earlier studies define the bivalent fusion protein rVE as a potent candidate vaccine molecule with the capability to concurrently stimulate humoral and cell mediated immune responses and a proof of concept for developing efficient subunit vaccines against Gram negative facultative intracellular bacterial pathogens. (uni-wuerzburg.de)
  • In this study, we evaluated a recombinant vaccine prepared from non-pathogenic Mycobacterium smegmatis (rMS) that expresses a fusion of early secreted antigenic target 6-kDa antigen (ESAT6) and culture filtrate protein 10 (CFP10). (semanticscholar.org)
  • METHODS: We compared the efficacies of the most commonly used vaccine constructs--adjuvanted protein, plasmid DNA, and live bacterial vectors--bearing the immunodominant secreted antigens early secreted antigen target-6 and antigen 85B, either alone or as a fusion protein. (mendeley.com)
Soluble3
  • This study was undertaken to determine whether the addition of etanercept, a soluble tumor necrosis factor receptor (p75):Fc fusion protein (TNFR:Fc), to methotrexate therapy would provide additional benefit to patients who had persistent rheumatoid arthritis despite receiving methotrexate. (nih.gov)
  • The aim of this study was to develop a strategy for pain management by generating a biotherapeutic that requires targeting of soluble N-ethylmaleimide-sensitive fusion protein (NSF) attachment protein receptor (SNARE) within the hyper-active sensory nerves. (dcu.ie)
  • Its concentration reached 30% of total protein, and exceeded 95% of all soluble proteins. (biomedcentral.com)
Gene14
  • Alternative splicing of downstream exons of the GNAS gene is observed, which results in different forms of the stimulatory G protein alpha subunit, a key element of the classical signal transduction pathway linking receptor-ligand interactions with the activation of adenylyl cyclase and a variety of cellular reponses. (abcam.com)
  • The recombinant protein was produced by transient gene expression (TGE) in suspension-adapted human embryonic kidney cells (HEK-293E) in 4L orbitally shaken bioreactors. (epfl.ch)
  • To overcome this problem we attached a signal sequence, as well as an amino-terminal His-tag fusion to the GM-CSF gene. (springer.com)
  • The sequence data showed a clear indication that the insert is our desired gene product allowing us to go on to design a fusion protein. (salford.ac.uk)
  • Its expression is induced by hypoxia and its role may be to protect hypoxic cells from apoptosis.This gene encodes a protein-disulfide isomerase. (antibody-antibodies.com)
  • After N-terminal amino acid sequence analysis, PCR-based strategy was used to clone the gene that encodes this protein. (pnas.org)
  • Nonetheless, from the clinical standpoint, gene transfer has limitations, including toxicity, limited control of the levels of protein expression, and difficulty in expressing more than one protein at a time. (jimmunol.org)
  • Protein transfer (or protein "painting"), which enables simultaneous delivery of well-defined amounts of multiple proteins to a cell, provides a valuable alternative means to gene transfer ( 9 , 10 ). (jimmunol.org)
  • Identifying proteins selectively associated with a genomic locus provides an important entry point toward understanding how a specific gene is regulated. (pnas.org)
  • Eukaryotic gene regulation is a complex process, often coordinated by the action of tens to hundreds of proteins. (pnas.org)
  • To fully understand the molecular mechanisms governing multiple steps in gene expression, including transcription and posttranscriptional regulation for a given gene, one must first identify the various protein factors involved in the process. (pnas.org)
  • F gene open reading frame (ORF) from NDV is 1650 bp, encoding a protein of 553 amino acids that can induce protective immunity alone. (org.ir)
  • Shafaati M R, Moghbeli M, Dorostkar R. Construction of Recombinant Bacmid DNA Encoding Newcastle Disease Virus (NDV) Fusion Protein Gene. (org.ir)
  • Plasminogen-related protein B is a protein that in humans is encoded by the PLGLB2 gene. (wikipedia.org)
Antibody fusion1
  • We have generated antibody fusion proteins directed against HER2, linked to sequences encoding an NKG2D-L, which can directly activate cytotoxic function in NK cells and also costimulate cytotoxic T cells. (aacrjournals.org)
Injection1
Single chain antibody1
Purity1
  • A large amount of the recombinant fusion proteins with high purity was obtained by applying a single step anion exchange chromatography or metal chelate affinity. (jascoinc.com)
20161
  • We analyzed the blood loss patterns of 617 consecutive adult patients undergoing lumbar and/or thoracic fusions requiring subfascial drain placement at a single institution from January 2009 to December 2016. (asianspinejournal.org)
Affinity chromatography8
Mycobacterium4
Sequences2
Biologically active1
Coagulation6
Antitumor3
ELOCTATE2
Vitro4
Spinal9
  • To independently assess the effectiveness and harms of rhBMP-2 in spinal fusion and reporting bias in industry-sponsored journal publications. (nih.gov)
  • In spinal fusion, rhBMP-2 has no proven clinical advantage over bone graft and may be associated with important harms, making it difficult to identify clear indications for rhBMP-2. (nih.gov)
  • The authors conclude that on the basis of the currently available evidence, it is difficult to identify clear indications for rhBMP-2 in spinal fusion. (spinesection.org)
  • Medtronic Sofamor Danek, Memphis, TN, USA) has been used as an osteoinductive adjuvant to enhance spinal fusions for more than 15 years [ 1 - 3 ]. (asianspinejournal.org)
  • Therefore, in this study, we aimed to use a retrospective cohort design to examine the impact of rhBMP-2 on the total perioperative blood loss (intraoperative estimated blood loss and postoperative drain output) following lumbar and thoracic spinal fusions involving the placement of a subfascial drain. (asianspinejournal.org)
  • Our study sought to empirically test the hypothesis that the use of rhBMP-2 during spinal fusion procedures reduces intraoperative and postoperative blood loss relative to the use of ICBG. (asianspinejournal.org)
  • We hypothesized that a high dose of rhBMP-2 in cervical spinal fusion could induce substantial alterations in bone, leading to mechanical impairment. (scienceopen.com)
  • Biologic manipulation for spinal fusion is an area undergoing active research. (eduhk.hk)
  • For this study, 24 adult New Zealand white rabbits underwent single-level unilateral posterior intertransverse process spinal fusion at L5-L6. (eduhk.hk)
Study9
  • In this study we looked into the possible reasons for poor expression and found that protein toxicity coupled with protease-based degradation was the principal reason for low productivity. (springer.com)
  • This study presents an approach for inhibiting p53-deficient tumor cell growth by using protein-based E4orf4 that had been genetically fused to epidermal growth factor (EGF) to ensure selective targeting of EGF receptor-overexpressing tumor cells. (ovid.com)
  • Included in this study are the first recombinant PRV strains expressing C terminal VP26-mCherry. (princeton.edu)
  • In our previous study, we established that the bivalent fusion protein (rVE) comprising immunologically active regions of Y pestis LcrV (100-270 aa) and YopE (50-213 aa) proteins conferred complete passive and active protection against lethal Y enterocolitica 8081 challenge. (uni-wuerzburg.de)
  • Phase 3 study of recombinant factor IX Fc fusion protein in hemophilia B . New England Journal of Medicine , 369 (24), 2313-2323. (elsevier.com)
  • Treatment of bleeding episodes with recombinant factor VIII Fc fusion protein in A-LONG study subjects with severe haemophilia A. (qmul.ac.uk)
  • Consequently, in this study, we delivered intratumorally via protein transfer four molecules, including the chemotactic molecules secondary lymphoid tissue chemokine and Fas ligand and the costimulatory molecules 4-1BBL and TNF-related activation-induced cytokine. (jimmunol.org)
  • A prospective randomized study of posterolateral lumbar fusion using osteogenic protein-1 (OP-1) versus local autograft with ceramic bone substitute: emphasis of surgical exploration and histologic assessment. (scienceopen.com)
  • This study also suggests a useful strategy to improve the yields of other ELP fusion proteins and repetitive polypeptides. (ingentaconnect.com)
Maltose-binding2
Hamster proteins1
  • IDELVION is contraindicated in patients who have had life-threatening hypersensitivity to the product or its components, including hamster proteins. (idelvion.com)
Bone11
  • For lumbar spine fusion, rhBMP-2 and iliac crest bone graft were similar in overall success, fusion, and other effectiveness measures and in risk for any adverse event, although rates were high across interventions (77% to 93% at 24 months from surgery). (nih.gov)
  • For both lumbar and cervical fusions, rhBMP-2 and iliac crest bone graft (ICBG) had similar results for fusion. (spinesection.org)
  • Previous studies on rhBMP-2 versus iliac crest bone grafting in thoracic and lumbar fusions have yielded mixed results regarding reductions in blood loss and have largely neglected the postoperative period when analyzing total blood loss. (asianspinejournal.org)
  • Since then, many studies have reported reduction in the operative time and hospital stays, as well as improved fusion rates in patients treated with rhBMP-2 compared with those treated with autologous iliac crest bone grafting (ICBG) [ 3 , 4 ]. (asianspinejournal.org)
  • n = 8/group) was used to quantify the consequences of a high rhBMP-2 dose (6 mg rhBMP-2) on fusion tissue compared to the 'gold standard' of autologous, cancellous bone graft. (scienceopen.com)
  • Although high-dose rhBMP-2 treatment led to an advanced radiological fusion result compared to autograft treatment, heterotopic bone formation and vertebral bone resorption were induced simultaneously. (scienceopen.com)
  • Histological evaluation unveiled highly active bone-forming processes ventral to the fusion segment after 12 weeks, while radiolucent areas showed still a partial loss of regular trabecular structure, with rare signs of remodelling and restoration. (scienceopen.com)
  • Despite qualitative alteration of the trabecular bone structure within the fusion site, the massive anterior heterotopic bone formation led to a substantial increase in mechanical stiffness compared to the autograft group. (scienceopen.com)
  • In 1965, Urist 14) discovered a subset of protein extract, which had a significant potential of inducing new bone formation even at the non-osseous tissues. (e-neurospine.org)
  • The proteins were termed bone morphogenetic proteins (BMPs). (e-neurospine.org)
  • 4) and in their letter they proposed that the containment of low dose (1.05 mg) rhBMP-2 within the cage and placing demineralized bone matrix (DBM) putty surrounding the INFUSE ensures a controlled delivery of rhBMP-2 in the vicinity of desired fusion site, which therefore is associated with excellent fusion rates with no adverse effects related to rhBMP-2. (e-neurospine.org)
Cleavage5
Species1
  • Fitches EC, Bell HA, Powell ME, Back E, Sargiotti C, Weaver RJ, Gatehouse JA (2010) Insecticidal activity of scorpion toxin (ButaIT) and snowdrop lectin (GNA) containing fusion proteins towards pest species of different orders. (springer.com)
Genetically1
  • These scFv were genetically fused with dimerization domains as well as with alkaline phosphatase, respectively, and diagnostic reagents were produced by expressing these fusion proteins in bacterial cultures. (gva.es)
Cervical2
Vaccines2
  • Can Multi-Stage Recombinant Fusion Proteins be Considered as Reliable Vaccines Against Tuberculosis? (mcjbums.com)
  • Keikha M, Karbalaei M. Can Multi-Stage Recombinant Fusion Proteins be Considered as Reliable Vaccines Against Tuberculosis? (mcjbums.com)
Antigens1
  • Likewise, the relative immunodominance of individual antigens in the fusion molecule is altered by the choice of delivery system. (mendeley.com)
Factor VIII2
  • Recombinant factor VIII Fc fusion protein: extended-interval dosing maintains low bleeding rates and correlates with von Willebrand factor levels. (eloctate.com)
  • Just as the blades of a windmill harness naturally occurring wind to produce energy, Fc Fusion utilizes naturally occurring Fc receptors in your body to keep Factor VIII temporarily recirculating in your bloodstream, protecting you from bleeds. (eloctate.com)
Adenovirus1
Membrane4
Receptor3
Insect cells1
Selectively1
Bind2
  • Therefore, surface proteins of M. leprae cell wall that bind laminin-2 are crucial for bacterial targeting to the peripheral nerves. (pnas.org)
  • Here, we applied our method to isolate the Drosophila melanogaster histone cluster in S2 cells to identify several factors including Vig and Vig2, two proteins that bind and regulate core histone H2A and H3 mRNA via interaction with their 3′ UTRs. (pnas.org)
Biological2